WORKLIST ENTRIES (1):

PNDRDTASEII View alignment View Structure     Pyridine nucleotide disulphide reductase class-II signature
 Type of fingerprint: COMPOUND with 10 elements
Links:
   PRINTS; PR00368 FADPNR; PR00370 FMOXYGENASE; PR00411 PNDRDTASEI
   PRINTS; PR00420 RNGMNOXGNASE
   INTERPRO; IPR000103
   PROSITE; PS00573 PYRIDINE_REDOX_2
   PDB; 1TRB 3Dinfo
   SCOP; 1TRB
   CATH; 1TRB

 Creation date 12-FEB-1996; UPDATE 30-JUN-1999

   1. KUYRIYAN, J., KRISHNA, T.S.R., WONG, L., GUENTHER, B., PAHLER, A.,
   WILLIAMS, C.H. AND MODEL, P.
   Convergent evolution of similar function in two structurally divergent
   enzymes.
   NATURE 352 172-174 (1991).

   2. RUSSEL M. AND MODEL P.
   Sequence of thioredoxin reductase from Escherichia coli. Relationship to 
   other flavoprotein disulfide oxidoreductases.
   J.BIOL.CHEM. 263 9015-9019 (1988).
   
   3. COHEN, G., ARGAMAN, A., SCHREIBER, R., MISLOVATI, M. AND AHARONOWITZ, Y.
   The thioredoxin system of Penicillium chrysogenum and its possible role in 
   penicillin biosynthesis.
   J.BACTERIOL. 176 973-984 (1994).

   4. TARTAGLIA, L.A., STORZ, G., BRODSKY, M.H., LAI, A. AND AMES B.N.
   Alkyl hydroperoxide reductase from Salmonella typhimurium. Sequence and
   homology to thioredoxin reductase and other flavoprotein disulfide
   oxidoreductases.
   J.BIOL.CHEM. 265 10535-10540 (1990).

   5. XU, X.M., KOYAMA, N., CUI, M., YAMAGISHI, A., NOSOH, Y. AND OSHIMA, T.
   Nucleotide sequence of the gene encoding NADH dehydrogenase from an
   alkalophile, Bacillus sp. strain YN-1.
   J.BIOCHEM.(TOKYO) 109 678-683 (1991).

   6. MATHIEU, I., MEYER, J. AND MOULIS, J.M.
   Cloning, sequencing and expression in Escherichia coli of the
   rubredoxin gene from Clostridium pasteurianum.
   BIOCHEM.J. 285 255-262 (1992).

   7. WAKSMAN, G., KRISHNA, T.S.R., WILLIAMS, C.H. AND KURIYAN, J.
   Crystal structure of Escherichia coli thioredoxin reductase refined at 2A
   resolution. Implications for a large conformational change during catalysis.
   J.MOL.BIOL. 236 800-816 (1994).

   8. MCKIE, J.H. AND DOUGLAS, K.T.
   Evidence for gene duplication forming similar binding folds for NAD(P)H
   and FAD in pyridine nucleotide-dependent flavoenzymes.
   FEBS LETT. 279 5-8 (1991).

   9. NIIMURA, Y., OHNISHI, K., YARITA, Y., HIDAKA, M., MASAKI, H., 
   UCHIMURA, T., SUZUKI, H., KOZAKI, M. AND UOZUMI, H.
   A flavoprotein functional as NADH oxidase from Amphibacillus xylanus Ep01:
   Purification and characterization of the enzyme and structural analysis of 
   its gene.
   J.BACTERIOL. 175 7945-7950 (1993). 

   10. HIGUCHI, M., SHIMADA, M., MATSUMOTO, J., YAMAMOTO, Y., RHAMAN, A.
   AND KAMIO, Y.
   Molecular cloning and sequence analysis of the gene encoding the H2O2-
   forming NADH oxidase from Streptococcus mutans.
   BIOSCI.BIOTECHNOL.BIOCHEM. 58 1603-1607 (1994).

   11. BRUCHHAUS, I. AND TANNICH, E. 
   Identification of an Entamoeba histolytica gene encoding a protein 
   homologous to prokaryotic disulphide oxidoreductases.
   MOL.BIOCHEM.PARASITOL. 70 187-191 (1995).

   The pyridine nucleotide-disulphide reductases (PNDR) use the isoalloxazine
   ring of FAD to shuttle reducing equivalents from NAD(P)H to a Cys residue
   that is usually a part of a redox-active disulphide bridge. In a second
   step, the reduced disulphide reduces the substrate. On the basis of sequence
   and structural similarities [1], PNDR can be categorised into 2 groups.
   Class II includes: prokaryotic and eukaryotic thioredoxin reductases [2,3];
   bacterial alkyl hydroperoxide reductases [4]; bacterial NADH:dehydrogenases
   [5]; a probable oxidoreductase encoded in the Clostridium pasteurianum
   rubredoxin operon [6]; and yeast hypothetical protein YHR106w. 
   
   The 3D structure of E.coli thioredoxin reductase (TR) has been solved [1,7].
   The protein exists as a homodimer, with 3 domains per monomer, which
   correspond to the FAD-binding, NAD(P)H-binding and central domains of
   glutathione reductase (GR) (cf. signature PNDRDTASEI). However, TR lacks
   the domain that provides the dimer interface in GR, and forms a completely 
   different dimeric structure. The relative orientation of these domains is
   very different in the 2 enzymes: when the FAD-binding domains of TR and GR
   are superimposed, the NADPH-binding domain of one is rotated by 66 degrees
   with respect to the other. The FAD- and NAD(P)H-binding domains have a 
   similar doubly-wound alpha/beta fold, suggesting they evolved by gene
   duplication [8]. While in GR the redox active disulphide is located in
   the FAD-binding domain, in TR it lies in the NADPH-binding domain. This
   suggests that the enzymes diverged from an ancestral nucleotide-binding
   protein and acquired their disulphide reductase activities independently [1]. 
  
   PNDRDTASEII is a 10-element fingerprint that provides a signature for the 
   PNDR class II family. The fingerprint was derived from an initial alignment
   of 14 sequences: motifs 1 and 6 contain 3 conserved Gly residues and
   correspond to the ADP moiety binding site for FAD and NAD(P) respectively
   (cf. motifs 1 and 3 of signature FADPNR); motif 5 contains 2 Cys residues 
   involved in the redox-active disulphide bond (motifs 5 and 6 include the
   region encoded by PROSITE pattern PYRIDINE_REDOX_2 (PS000573)); and motif 9
   encodes the binding site for the FAD flavin moiety (cf. motif 5 of FADPNR).
   Three iterations on OWL27.0 were required to reach convergence, at which
   point a true set comprising 24 sequences was identified, including the
   hydrogen peroxide-forming NADH oxidases from Amphibacillus xylanus (A49911)
   [9] and Streptococcus mutans (JC2311) [10], as well as the Entamoeba
   histolytica gEh-34 gene product (EHDO34) [11]. Numerous partial matches
   were also found, most of which are members of the PNDR family.
  
   An update on SPTR37_9f identified a true set of 41 sequences, and 151
   partial matches.

  SUMMARY INFORMATION
     41 codes involving 10 elements
      4 codes involving  9 elements
      1 codes involving  8 elements
      0 codes involving  7 elements
      0 codes involving  6 elements
      1 codes involving  5 elements
      7 codes involving  4 elements
     28 codes involving  3 elements
    110 codes involving  2 elements

   COMPOSITE FINGERPRINT INDEX
  
   10|  41   41   41   41   41   41   41   41   41   41  
    9|   4    4    1    4    4    4    4    3    4    4  
    8|   1    1    0    1    1    1    1    0    1    1  
    7|   0    0    0    0    0    0    0    0    0    0  
    6|   0    0    0    0    0    0    0    0    0    0  
    5|   1    1    0    1    1    1    0    0    0    0  
    4|   5    0    0    3    0    5    2    2    7    4  
    3|  18    1    2   11    0   14    7    5   23    3  
    2|  63    2    4   35    3   15   15   16   62    5  
   --+---------------------------------------------------
     |   1    2    3    4    5    6    7    8    9   10  

True positives..
 TRXB_YEAST     TRXB_MYCSM     TRXB_NEUCR     O53592         
 TRXB_ECOLI     TRXB_MYCTU     YHQ6_YEAST     O84101         
 TRXB_MYCLE     TRXB_HAEIN     O22229         TRXB_STRCL     
 TRXB_SCHPO     TRXB_PENCH     TRB1_ARATH     TRXB_BUCAP     
 TRXB_CLOLI     O54079         TRXB_LISMO     TRXB_STRCO     
 TRXB_EUBAC     DHNA_BACSP     TRXB_COXBU     DHNA_BACSU     
 TRXB_BACSU     O82864         AHPF_SALTY     AHPF_ECOLI     
 Q24834         Q06369         R34K_CLOPA     O50134         
 Q54469         O66266         O28718         TRXB_BORBU     
 TRXB_TREPA     TRXB_MYCPN     O26804         TRXB_MYCGE     
 Q58931         
Subfamily:  Codes involving 9 elements
 Subfamily True positives..
 O22751         O06465         AHPF_STAAU     O66790         
Subfamily:  Codes involving 8 elements
 Subfamily True positives..
 TRXB_HELPY     
Subfamily:  Codes involving 5 elements
 Subfamily True positives..
 O54535         
Subfamily:  Codes involving 4 elements
 Subfamily True positives..
 O34399         P96219         O27685         O33474         
 O59547         O83717         O29311         
Subfamily:  Codes involving 3 elements
 Subfamily True positives..
 O86255         O59368         O29576         Q41219         
 O81413         DLDH_ALCEU     NADO_THEBR     DLDH_PEA       
 O29030         Q40360         GLSN_MEDSA     O05268         
 O67845         P77907         DLD1_BACSU     O84925         
 YPDA_BACSU     O31475         P74746         O08340         
 DLD1_BACST     O29985         O58606         Q59917         
 Q53125         P95457         O50286         DLDH_ECOLI     
Subfamily:  Codes involving 2 elements
 Subfamily True positives..
 P72300         Q48419         Q48410         O84596         
 O66724         O84561         DLDH_ZYMMO     O32886         
 O52473         BAIH_EUBSP     Q59160         P70933         
 DLDH_YEAST     NADB_ECOLI     DLD2_BACSU     O06595         
 Q50994         O59088         O05139         P95160         
 P95200         O32907         O52933         O51670         
 TODA_PSEPU     Q59822         Q02733         DLDH_PSEFL     
 Q52386         O69798         O24679         GSHR_BURCE     
 BEDA_PSEPU     O33997         GIDA_AQUAE     THCD_RHOSO     
 Y033_METJA     P95034         Q50756         DLDH_AZOVI     
 DHSA_BACSU     P72762         O27434         DLD2_PSEPU     
 DLDH_MYCPN     DLDH_TRYBB     NIR_NEUCR      DLD3_PSEPU     
 GLTD_AZOBR     O66715         O50311         Q57031         
 O93364         O29595         NASD_BACSU     O29966         
 O58308         NAPE_ENTFA     O17953         TYTR_TRYCR     
 SYA_ARATH      Q59299         O61143         O83891         
 P95596         O18480         AEGA_ECOLI     Q43497         
 O67007         GLTD_ECOLI     Q46811         P90597         
 P90599         P90598         NAOX_ENTFA     O28894         
 Q42711         O34324         P72259         O85962         
 ETFD_HUMAN     DLDH_CANFA     Q14131         Q56267         
 DLDH_PIG       DLDH_HUMAN     O66945         FRDA_PROVU     
 FRDA_ECOLI     Q54453         O29852         O01412         
 Q60151         DLDH_HAEIN     P91171         O08749         
 Q51973         O53355         Q40977         O85778         
 Q19655         O58643         O65946         Q51225


  PROTEIN TITLES
   TRXB_YEAST       THIOREDOXIN REDUCTASE 1 (EC 1.6.4.5) - SACCHAROMYCES CEREVIS
   TRXB_MYCSM       THIOREDOXIN REDUCTASE (EC 1.6.4.5) - MYCOBACTERIUM SMEGMATIS
   TRXB_NEUCR       THIOREDOXIN REDUCTASE (EC 1.6.4.5) - NEUROSPORA CRASSA.
   O53592           THIOREDOXIN REDUCTASE (EC 1.6.4.5) (TR) - MYCOBACTERIUM TUBE
   TRXB_ECOLI       THIOREDOXIN REDUCTASE (EC 1.6.4.5) - ESCHERICHIA COLI.
   TRXB_MYCTU       THIOREDOXIN REDUCTASE (EC 1.6.4.5) (TR) - MYCOBACTERIUM TUBE
   YHQ6_YEAST       THIOREDOXIN REDUCTASE 2, MITOCHONDRIAL PRECURSOR (EC 1.6.4.5
   O84101           THIOREDOXIN REDUCTASE - CHLAMYDIA TRACHOMATIS.
   TRXB_MYCLE       BIFUNCTIONAL THIOREDOXIN REDUCTASE/THIOREDOXIN [INCLUDES: TH
   TRXB_HAEIN       THIOREDOXIN REDUCTASE (EC 1.6.4.5) - HAEMOPHILUS INFLUENZAE.
   O22229           PUTATIVE THIOREDOXIN REDUCTASE - ARABIDOPSIS THALIANA (MOUSE
   TRXB_STRCL       THIOREDOXIN REDUCTASE (EC 1.6.4.5) - STREPTOMYCES CLAVULIGER
   TRXB_SCHPO       THIOREDOXIN REDUCTASE (EC 1.6.4.5) - SCHIZOSACCHAROMYCES POM
   TRXB_PENCH       THIOREDOXIN REDUCTASE (EC 1.6.4.5) - PENICILLIUM CHRYSOGENUM
   TRB1_ARATH       THIOREDOXIN REDUCTASE 1 (EC 1.6.4.5) (NADPH-DEPENDENT THIORE
   TRXB_BUCAP       THIOREDOXIN REDUCTASE (EC 1.6.4.5) - BUCHNERA APHIDICOLA.
   TRXB_CLOLI       THIOREDOXIN REDUCTASE (EC 1.6.4.5) - CLOSTRIDIUM LITORALE (B
   O54079           THIOREDOXIN REDUCTASE (EC 1.6.4.5) - STAPHYLOCOCCUS AUREUS.
   TRXB_LISMO       THIOREDOXIN REDUCTASE (EC 1.6.4.5) - LISTERIA MONOCYTOGENES.
   TRXB_STRCO       THIOREDOXIN REDUCTASE (EC 1.6.4.5) - STREPTOMYCES COELICOLOR
   TRXB_EUBAC       THIOREDOXIN REDUCTASE (EC 1.6.4.5) - EUBACTERIUM ACIDAMINOPH
   DHNA_BACSP       NADH DEHYDROGENASE (EC 1.6.99.3) (ALKYL HYDROPEROXIDE REDUCT
   TRXB_COXBU       THIOREDOXIN REDUCTASE (EC 1.6.4.5) - COXIELLA BURNETII.
   DHNA_BACSU       NADH DEHYDROGENASE (EC 1.6.99.3) (ALKYL HYDROPEROXIDE REDUCT
   TRXB_BACSU       THIOREDOXIN REDUCTASE (EC 1.6.4.5) (GENERAL STRESS PROTEIN 3
   O82864           ALKYL HYDROPEROXIDE REDUCTASE SUBUNIT F (EC 1.6.4.-) - PSEUD
   AHPF_SALTY       ALKYL HYDROPEROXIDE REDUCTASE SUBUNIT F (EC 1.6.4.-) (ALKYL 
   AHPF_ECOLI       ALKYL HYDROPEROXIDE REDUCTASE SUBUNIT F (EC 1.6.4.-) (ALKYL 
   Q24834           DISULPHIDE OXIDOREDUCTASE - ENTAMOEBA HISTOLYTICA.
   Q06369           NADH OXIDASE - AMPHIBACILLUS XYLANUS.
   R34K_CLOPA       34.2 KD PROTEIN IN RUBREDOXIN OPERON (EC 1.6.4.-) (ORF A) - 
   O50134           336AA LONG HYPOTHETICAL THIOREDOXIN REDUCTASE - PYROCOCCUS H
   Q54469           NADH OXIDASE - STREPTOCOCCUS MUTANS.
   O66266           NADH OXIDASE/ALKYL HYDROPEROXIDASE REDUCTASE - STREPTOCOCCUS
   O28718           THIOREDOXIN REDUCTASE (TRXB) - ARCHAEOGLOBUS FULGIDUS.
   TRXB_BORBU       THIOREDOXIN REDUCTASE (EC 1.6.4.5) - BORRELIA BURGDORFERI (L
   TRXB_TREPA       THIOREDOXIN REDUCTASE (EC 1.6.4.5) - TREPONEMA PALLIDUM.
   TRXB_MYCPN       THIOREDOXIN REDUCTASE (EC 1.6.4.5) - MYCOPLASMA PNEUMONIAE.
   O26804           THIOREDOXIN REDUCTASE - METHANOBACTERIUM THERMOAUTOTROPHICUM
   TRXB_MYCGE       THIOREDOXIN REDUCTASE (EC 1.6.4.5) - MYCOPLASMA GENITALIUM.
   Q58931           HYPOTHETICAL PROTEIN MJ1536 - METHANOCOCCUS JANNASCHII.
 
   O22751           NADPH THIOREDOXIN REDUCTASE - ARABIDOPSIS THALIANA (MOUSE-EA
   O06465           ALKYL HYDROPEROXIDE REDUCTASE SUBUNIT F (EC 1.6.4.-) - XANTH
   AHPF_STAAU       ALKYL HYDROPEROXIDE REDUCTASE SUBUNIT F (EC 1.6.4.-) - STAPH
   O66790           THIOREDOXIN REDUCTASE - AQUIFEX AEOLICUS.
 
   TRXB_HELPY       THIOREDOXIN REDUCTASE (EC 1.6.4.5) - HELICOBACTER PYLORI (CA
 
   O54535           SIMILAR TO MYCOBACTERIUM LEPRAE THIOREDOXIN REDUCTASE - HALO
 
   O34399           GLUTAMATE SYNTHASE (EC 1.4.1.13) (GLUTAMATE SYNTHASE (NADPH)
   P96219           HYPOTHETICAL 53.5 KD PROTEIN - MYCOBACTERIUM TUBERCULOSIS.
   O27685           DIHYDROLIPOAMIDE DEHYDROGENASE - METHANOBACTERIUM THERMOAUTO
   O33474           GLUTAMATE SYNTHASE - PYROCOCCUS SP.
   O59547           476AA LONG HYPOTHETICAL GLUTAMATE SYNTHASE SMALL CHAIN - PYR
   O83717           GLUTAMATE SYNTHASE (GLTA) - TREPONEMA PALLIDUM.
   O29311           NADH OXIDASE (NOXA-4) - ARCHAEOGLOBUS FULGIDUS.
 
   O86255           THIOREDOXIN REDUCTASE - KLEBSIELLA OXYTOCA.
   O59368           482AA LONG HYPOTHETICAL D-NOPALINE DEHYDROGENASE - PYROCOCCU
   O29576           SUCCINATE DEHYDROGENASE, FLAVOPROTEIN SUBUNIT A (SDHA) - ARC
   Q41219           FERRIC LEGHEMOGLOBIN REDUCTASE - GLYCINE MAX (SOYBEAN).
   O81413           FERRIC LEGHEMOGLOBIN REDUCTASE-2 PRECURSOR - GLYCINE MAX (SO
   DLDH_ALCEU       DIHYDROLIPOAMIDE DEHYDROGENASE (EC 1.8.1.4) (E3 COMPONENT OF
   NADO_THEBR       NADH OXIDASE (EC 1.-.-.-) - THERMOANAEROBACTER BROCKII (THER
   DLDH_PEA         DIHYDROLIPOAMIDE DEHYDROGENASE, MITOCHONDRIAL PRECURSOR (EC 
   O29030           HETERODISULFIDE REDUCTASE, SUBUNIT A/METHYLVIOLOGEN REDUCING
   Q40360           NADH-DEPENDENT GLUTAMATE SYNTHASE - MEDICAGO SATIVA (ALFALFA
   GLSN_MEDSA       GLUTAMATE SYNTHASE [NADH] PRECURSOR (EC 1.4.1.14) (NADH-GOGA
   O05268           THIOREDOXINE REDUCTASE - BACILLUS SUBTILIS.
   O67845           GLUTAMATE SYNTHASE SMALL SUBUNIT GLTD - AQUIFEX AEOLICUS.
   P77907           FORMATE DEHYDROGENASE BETA SUBUNIT (EC 1.2.1.43) (FORMATE DE
   DLD1_BACSU       DIHYDROLIPOAMIDE DEHYDROGENASE (EC 1.8.1.4) (E3 COMPONENT OF
   O84925           NADH OXIDASE - STREPTOCOCCUS PNEUMONIAE.
   YPDA_BACSU       HYPOTHETICAL 36.3 KD PROTEIN IN RECQ-CMK INTERGENIC REGION -
   O31475           YCGT PROTEIN - BACILLUS SUBTILIS.
   P74746           HYPOTHETICAL 36.0 KD PROTEIN - SYNECHOCYSTIS SP. (STRAIN PCC
   O08340           GLUTAMATE SYNTHASE (EC 1.4.1.13) (GLUTAMATE SYNTHASE (NADPH)
   DLD1_BACST       DIHYDROLIPOAMIDE DEHYDROGENASE (EC 1.8.1.4) (E3 COMPONENT OF
   O29985           NADH OXIDASE (NOXA-1) - ARCHAEOGLOBUS FULGIDUS.
   O58606           472AA LONG HYPOTHETICAL GLUTAMATE SYNTHASE SMALL CHAIN - PYR
   Q59917           NADH OXIDASE (EC 1.6.99.3) (NOXASE) - TREPONEMA HYODYSENTERI
   Q53125           BIPHENYL DIOXYGENASE - RHODOCOCCUS SP.
   P95457           GLUTAMATE SYNTHASE SMALL SUBUNIT - PSEUDOMONAS AERUGINOSA.
   O50286           LIPOAMIDE DEHYDROGENASE - VIBRIO PARAHAEMOLYTICUS.
   DLDH_ECOLI       DIHYDROLIPOAMIDE DEHYDROGENASE (EC 1.8.1.4) (E3 COMPONENT OF
 
   P72300           OOXA - RHIZOBIUM MELILOTI.
   Q48419           DIHYDROLIPOAMIDE DEHYDROGENASE (EC 1.8.1.4) (E3 COMPONENT OF
   Q48410           DIHYDROLIPOAMIDE DEHYDROGENASE (EC 1.8.1.4) (E3 COMPONENT OF
   O84596           SUCCINATE DEHYDROGENASE - CHLAMYDIA TRACHOMATIS.
   O66724           HYPOTHETICAL 21.8 KD PROTEIN - AQUIFEX AEOLICUS.
   O84561           LIPOAMIDE DEHYDROGENASE - CHLAMYDIA TRACHOMATIS.
   DLDH_ZYMMO       DIHYDROLIPOAMIDE DEHYDROGENASE (EC 1.8.1.4) (E3 COMPONENT OF
   O32886           POSSIBLE FERREDOXIN - MYCOBACTERIUM LEPRAE.
   O52473           NADH DEHYDROGENASE - MYCOBACTERIUM SMEGMATIS.
   BAIH_EUBSP       NADH-DEPENDENT FLAVIN OXIDOREDUCTASE (EC 1.-.-.-) - EUBACTER
   Q59160           OOXA (EC 1.5.1.19) (D-NOPALINE DEHYDROGENASE) (D-NOPALINE SY
   P70933           SUCCINATE DEHYDROGENASE SUBUNIT A - PAENIBACILLUS MACERANS (
   DLDH_YEAST       DIHYDROLIPOAMIDE DEHYDROGENASE, MITOCHONDRIAL PRECURSOR (EC 
   NADB_ECOLI       L-ASPARTATE OXIDASE (EC 1.4.3.16) (QUINOLINATE SYNTHETASE B)
   DLD2_BACSU       DIHYDROLIPOAMIDE DEHYDROGENASE (EC 1.8.1.4) (E3 COMPONENT OF
   O06595           NADB - MYCOBACTERIUM TUBERCULOSIS.
   Q50994           SUCAB-LPD OPERON, SUCB AND LPD GENES, COMPLETE CDS, SUCA GEN
   O59088           493AA LONG HYPOTHETICAL PROTEIN - PYROCOCCUS HORIKOSHII.
   O05139           SOLUBLE PYRIDINE NUCLEOTIDE TRANSHYDROGENASE - PSEUDOMONAS F
   P95160           HYPOTHETICAL 49.6 KD PROTEIN - MYCOBACTERIUM TUBERCULOSIS.
   P95200           HYPOTHETICAL 50.4 KD PROTEIN - MYCOBACTERIUM TUBERCULOSIS.
   O32907           DEHYDROGENASE - MYCOBACTERIUM LEPRAE.
   O52933           2-ENOATE REDUCTASE (EC 1.3.1.31) - CLOSTRIDIUM TYROBUTYRICUM
   O51670           NADH OXIDASE, WATER-FORMING (NOX) - BORRELIA BURGDORFERI (LY
   TODA_PSEPU       TOLUENE 1,2-DIOXYGENASE SYSTEM FERREDOXIN--NAD(+) REDUCTASE 
   Q59822           DIHYDROLIPOAMIDE DEHYDROGENASE (EC 1.8.1.4) (E3 COMPONENT OF
   Q02733           LPB14P - SACCHAROMYCES CEREVISIAE (BAKER'S YEAST).
   DLDH_PSEFL       DIHYDROLIPOAMIDE DEHYDROGENASE (EC 1.8.1.4) (E3 COMPONENT OF
   Q52386           CHLOROBENZENE DIOXYGENASE, NADH-FERREDOXIN REDUCTASE - PSEUD
   O69798           REDUCTASE - RALSTONIA SP.
   O24679           TECA4 - BURKHOLDERIA SP.
   GSHR_BURCE       GLUTATHIONE REDUCTASE (EC 1.6.4.2) (GR) (GRASE) - BURKHOLDER
   BEDA_PSEPU       BENZENE 1,2-DIOXYGENASE SYSTEM FERREDOXIN--NAD(+) REDUCTASE 
   O33997           ADENYLYLSULFATE REDUCTASE ALPHA SUBUNIT - CHROMATIUM VINOSUM
   GIDA_AQUAE       GLUCOSE INHIBITED DIVISION PROTEIN A - AQUIFEX AEOLICUS.
   THCD_RHOSO       RHODOCOXIN REDUCTASE (EC 1.18.1.-) - RHODOCOCCUS SP. (STRAIN
   Y033_METJA       HYPOTHETICAL FAD FLAVOPROTEIN OXIDASE MJ0033 - METHANOCOCCUS
   P95034           HYPOTHETICAL 43.0 KD PROTEIN - MYCOBACTERIUM TUBERCULOSIS.
   Q50756           HETERODISULFIDE REDUCTASE, SUBUNIT HDRA (EC 1.97.1-.) (GLYA 
   DLDH_AZOVI       DIHYDROLIPOAMIDE DEHYDROGENASE (EC 1.8.1.4) (E3 COMPONENT OF
   DHSA_BACSU       SUCCINATE DEHYDROGENASE FLAVOPROTEIN SUBUNIT (EC 1.3.99.1) -
   P72762           NADH-GLUTAMATE SYNTHASE SMALL SUBUNIT - SYNECHOCYSTIS SP. (S
   O27434           HETERODISULFIDE REDUCTASE, SUBUNIT A - METHANOBACTERIUM THER
   DLD2_PSEPU       DIHYDROLIPOAMIDE DEHYDROGENASE (EC 1.8.1.4) (E3 COMPONENT OF
   DLDH_MYCPN       DIHYDROLIPOAMIDE DEHYDROGENASE (EC 1.8.1.4) (E3 COMPONENT OF
   DLDH_TRYBB       DIHYDROLIPOAMIDE DEHYDROGENASE (EC 1.8.1.4) - TRYPANOSOMA BR
   NIR_NEUCR        NITRITE REDUCTASE [NAD(P)H] (EC 1.6.6.4) - NEUROSPORA CRASSA
   DLD3_PSEPU       DIHYDROLIPOAMIDE DEHYDROGENASE 3 (EC 1.8.1.4) (LPD-3) - PSEU
   GLTD_AZOBR       GLUTAMATE SYNTHASE [NADPH] SMALL CHAIN (EC 1.4.1.13) (GLUTAM
   O66715           HETERODISULFIDE REDUCTASE SUBUNIT A - AQUIFEX AEOLICUS.
   O50311           DIHYDROLIPOAMIDE DEHYDROGENASE (EC 1.8.1.4) (E3 COMPONENT OF
   Q57031           FERREDOXIN REDUCTASE BPH - RHODOCOCCUS GLOBERULUS, RHODOCOCC
   O93364           L-AMINO ACID OXIDASE PRECURSOR (EC 1.4.3.2) (LAO) - CROTALUS
   O29595           HETERODISULFIDE REDUCTASE, SUBUNIT A/METHYLVIOLOGEN REDUCING
   NASD_BACSU       NITRITE REDUCTASE [NAD(P)H] (EC 1.6.6.4) - BACILLUS SUBTILIS
   O29966           SARCOSINE OXIDASE, SUBUNIT ALPHA (SOXA) - ARCHAEOGLOBUS FULG
   O58308           445AA LONG HYPOTHETICAL NADH OXIDASE - PYROCOCCUS HORIKOSHII
   NAPE_ENTFA       NADH PEROXIDASE (EC 1.11.1.1) (NPXASE) - ENTEROCOCCUS FAECAL
   O17953           LLC1.3 PROTEIN - CAENORHABDITIS ELEGANS.
   SYA_ARATH        ALANYL-TRNA SYNTHETASE, MITOCHONDRIAL PRECURSOR (EC 6.1.1.7)
   Q59299           DIHYDROLIPOAMIDE DEHYDROGENASE (EC 1.8.1.4) (LIPOAMIDE REDUC
   O61143           NAD(P)H-DEPENDENT GLUTAMATE SYNTHASE - PLASMODIUM FALCIPARUM
   P95596           DIHYDROLIPOAMIDE DEHYDROGENASE (EC 1.8.1.4) (E3 COMPONENT OF
   O18480           DIHYDROLIPOAMIDE DEHYDROGENASE (EC 1.8.1.4) (E3) - MANDUCA S
   AEGA_ECOLI       AEGA PROTEIN - ESCHERICHIA COLI.
   Q43497           ASCORBATE FREE RADICAL REDUCTASE - LYCOPERSICON ESCULENTUM (
   O67007           NADH OXIDASE - AQUIFEX AEOLICUS.
   GLTD_ECOLI       GLUTAMATE SYNTHASE [NADPH] SMALL CHAIN (EC 1.4.1.13) (GLUTAM
   Q46811           WAS O492P AND O826P BEFORE SPLICE - ESCHERICHIA COLI.
   P90597           DIHYDROLIPOAMIDE DEHYDROGENASE (EC 1.8.1.4) - TRYPANOSOMA CR
   P90599           DIHYDROLIPOAMIDE DEHYDROGENASE (EC 1.8.1.4) - TRYPANOSOMA CR
   P90598           DIHYDROLIPOAMIDE DEHYDROGENASE (EC 1.8.1.4) - TRYPANOSOMA CR
   NAOX_ENTFA       NADH OXIDASE (EC 1.6.99.3) (NOXASE) - ENTEROCOCCUS FAECALIS 
   O28894           HETERODISULFIDE REDUCTASE, SUBUNIT A (HDRA-2) - ARCHAEOGLOBU
   Q42711           MONODEHYDROASCORBATE REDUCTASE (EC 1.6.5.4) - CUCUMIS SATIVU
   O34324           LIPOAMIDE DEHYDROGENASE COMPONENT OF PYRUVATE DEHYDROGENASE 
   P72259           ISOPROPYLBENZENE 2,3-DIOXYGENASE - RHODOCOCCUS ERYTHROPOLIS.
   ETFD_HUMAN       ELECTRON TRANSFER FLAVOPROTEIN-UBIQUINONE OXIDOREDUCTASE PRE
   DLDH_CANFA       DIHYDROLIPOAMIDE DEHYDROGENASE, MITOCHONDRIAL PRECURSOR (EC 
   Q14131           DIHYDROLIPOAMIDE DEHYDROGENASE, MITOCHONDRIAL PRECURSOR (EC 
   DLDH_PIG         DIHYDROLIPOAMIDE DEHYDROGENASE, MITOCHONDRIAL PRECURSOR (EC 
   DLDH_HUMAN       DIHYDROLIPOAMIDE DEHYDROGENASE, MITOCHONDRIAL PRECURSOR (EC 
   O66945           DIHYDROLIPOAMIDE DEHYDROGENASE - AQUIFEX AEOLICUS.
   FRDA_PROVU       FUMARATE REDUCTASE FLAVOPROTEIN SUBUNIT (EC 1.3.99.1) - PROT
   FRDA_ECOLI       FUMARATE REDUCTASE FLAVOPROTEIN SUBUNIT (EC 1.3.99.1) - ESCH
   Q54453           H2O-FORMING NADH OXIDASE - STREPTOCOCCUS MUTANS.
   O29852           NADH OXIDASE (NOXA-2) - ARCHAEOGLOBUS FULGIDUS.
   Q60151           GLUTATHIONE REDUCTASE (EC 1.6.4.2) (GLUTATHIONE REDUCTASE (N
   DLDH_HAEIN       DIHYDROLIPOAMIDE DEHYDROGENASE (EC 1.8.1.4) (E3 COMPONENT OF
   P91171           SIMILAR TO FLAVIN-CONTAINING MONOOXYGENASES - CAENORHABDITIS
   O08749           DIHYDROLIPOAMIDE DEHYDROGENASE, MITOCHONDRIAL PRECURSOR (EC 
   Q51973           P-CUMATE DIOXYGENASE FERREDOXIN REDUCTASE SUBUNIT - PSEUDOMO
   O53355           DIHYDROLIPOAMIDE DEHYDROGENASE - MYCOBACTERIUM TUBERCULOSIS.
   Q40977           MONODEHYDROASCORBATE REDUCTASE - PISUM SATIVUM (GARDEN PEA).
   O85778           PUTATIVE FERREDOXIN REDUCTASE MOCF - RHIZOBIUM LEGUMINOSARUM
   Q19655           SIMILAR TO OXIDOREDUCTASE - CAENORHABDITIS ELEGANS.
   O58643           397AA LONG HYPOTHETICAL NADH OXIDASE - PYROCOCCUS HORIKOSHII
   O65946           REDA2 PROTEIN - SPHINGOMONAS SP.
   Q56267           GLUTAMATE SYNTHASE SMALL SUBUNIT GLTD - THIOBACILLUS FERROOX
   O85962           FERREDOXIN REDUCTASE SUBUNIT AROMATIC OXYGENASE - SPHINGOMON
   O83891           NADH OXIDASE - TREPONEMA PALLIDUM.
   TYTR_TRYCR       TRYPANOTHIONE REDUCTASE (EC 1.6.4.8) (TR) (N1,N8- BIS(GLUTAT
   O01412           GLUTATHIONE REDUCTASE - ONCHOCERCA VOLVULUS.
   Q51225           OUTER MEMBRANE PROTEIN P64K OR PM-6 - NEISSERIA MENINGITIDIS

SCAN HISTORY OWL27_0 3 600 NSINGLE SPTR37_9f 3 230 NSINGLE INITIAL MOTIF SETS PNDRDTASEII1 Length of motif = 23 Motif number = 1 Pyridine nucleotide disulphide reductase-II motif I - 1 PCODE ST INT SLIILGSGPAGYTDAIYVARANL TRXB_COXBU 8 8 EVIVIGSGPAGYTAALYAARAQL TRXB_MYCLE 13 13 NVIIIGSGPAGYTAALYTARASL TRXB_STRCL 5 5 RLCIVGSGPAAHTAAIYAARAEL S44027 10 10 KVVIIGSGAGAHTAAIYLSRAEL TRXB_PENCH 4 4 KLLILGSGPAGYTAAIYAARANL TRXB_HAEIN 8 8 KVVIIGSGPAAHTAAIYLARAEL NEUCYS9 4 4 KLLILGSGPAGYTAAVYAARANL TRXB_ECOLI 7 7 KVTIIGSGPAAHTAAIYLARAEI A55468 5 5 DLVIIGAGPAGLTAAIYAIRAKL R34K_CLOPA 8 8 DVLVIGGGPAGNSAAIYAARKGV JC2311 210 210 DVLIVGSGPAGAAAAVYSARKGI AHPF_SALTY 214 214 DVLVIGGGPAGASSAIYAARKGI A49911 210 210 DVLVVGGGPAGASSAIYAARKGI DHNA_BACSP 210 210 PNDRDTASEII2 Length of motif = 16 Motif number = 2 Pyridine nucleotide disulphide reductase-II motif II - 1 PCODE ST INT GGQLMTTTDVANWPGE TRXB_COXBU 41 10 GGALMTTTEVENYPGF TRXB_MYCLE 46 10 GGALMNTTDVENFPGF TRXB_STRCL 39 11 GGQLTTTTDVENFPGF S44027 48 15 GGQLTTTTDVENFPGF TRXB_PENCH 42 15 GGQLTTTDEIENWPGD TRXB_HAEIN 41 10 GGQLTTTTEIENFPGF NEUCYS9 42 15 GGQLTTTTEVENWPGD TRXB_ECOLI 40 10 GGQLTTTTEIENFPGF A55468 43 15 GGQIRETYTVENFPGF R34K_CLOPA 41 10 GGQVMETVGIENMIGT JC2311 242 9 GGQVLDTVDIENYISV AHPF_SALTY 246 9 GGQVMDTLGIENFIGT A49911 242 9 GGQIMDTLSIENFISQ DHNA_BACSP 242 9 PNDRDTASEII3 Length of motif = 11 Motif number = 3 Pyridine nucleotide disulphide reductase-II motif III - 1 PCODE ST INT GPKLLERMQKH TRXB_COXBU 62 5 GPELMDDMREQ TRXB_MYCLE 67 5 GPDLMDNMRAQ TRXB_STRCL 60 5 GVELTDKFRKQ S44027 69 5 GAELMDNMRAQ TRXB_PENCH 63 5 GSGLMQRMLQH TRXB_HAEIN 62 5 GQELMDKMKAQ NEUCYS9 63 5 GPLLMERMHEH TRXB_ECOLI 61 5 GSELMDRMREQ A55468 64 5 GADLADKMEEH R34K_CLOPA 61 4 GPQLMAQVEEH JC2311 262 4 GQKLAGALKAH AHPF_SALTY 266 4 GPKLISEIEQH A49911 262 4 GPKLAASLEEH DHNA_BACSP 262 4 PNDRDTASEII4 Length of motif = 9 Motif number = 4 Pyridine nucleotide disulphide reductase-II motif IV - 1 PCODE ST INT DALIIATGA TRXB_COXBU 108 35 RAVILAMGT TRXB_MYCLE 113 35 KAVIVTTGS TRXB_STRCL 106 35 DAVILAIGA S44027 114 34 DAVIIATGA TRXB_PENCH 115 41 DALIIATGA TRXB_HAEIN 107 34 DSIILATGA NEUCYS9 111 37 DALIIATGA TRXB_ECOLI 106 34 DAIILATGA A55468 113 38 KALIIATGA R34K_CLOPA 107 35 KTAVLALGA JC2311 308 35 RSIIIATGA AHPF_SALTY 316 39 KTIILATGA A49911 308 35 KSVILSTGA DHNA_BACSP 308 35 PNDRDTASEII5 Length of motif = 13 Motif number = 5 Pyridine nucleotide disulphide reductase-II motif V - 1 PCODE ST INT MGKGVSACATCDG TRXB_COXBU 130 13 LGRGVSACATCDG TRXB_MYCLE 135 13 SGRGVSWCATCDG TRXB_STRCL 128 13 WNRGISACAVCDG S44027 140 17 WQNGISACAVCDG TRXB_PENCH 137 13 KGRGVSACATCDG TRXB_HAEIN 129 13 WQNGISACAVCDG NEUCYS9 133 13 KGRGVSACATCDG TRXB_ECOLI 128 13 WQKGISACAVCDG A55468 135 13 HGKVIHYCELCDG R34K_CLOPA 129 13 FNKGVTYCPHCDG JC2311 330 13 RTKGVTYCPHCDG AHPF_SALTY 338 13 KNKGVAYCTHCDA A49911 330 13 KNKGVAYCPHCDG DHNA_BACSP 330 13 PNDRDTASEII6 Length of motif = 25 Motif number = 6 Pyridine nucleotide disulphide reductase-II motif VI - 1 PCODE ST INT YRAKKVAVVGGGNTSVEEALYLSHI TRXB_COXBU 145 2 FRGQDIAVIGGGDSAMEEALFLTRF TRXB_MYCLE 150 2 FKDQDIVVVGGGDTAMEEATFLSRF TRXB_STRCL 143 2 FRNKPLAVIGGGDSAMEEANFLTKY S44027 157 4 FRNKPLYVIGGGDSAAEEAMFLAKY TRXB_PENCH 154 4 YRNKPVGVIGGGNTAVEEALYLANI TRXB_HAEIN 144 2 FRNKHLVVIGGGDSAAEEAMYLTKY NEUCYS9 150 4 YRNQKVAVIGGGNTAVEEALYLSNI TRXB_ECOLI 143 2 FRNKPLAVIGGGDSACEEAQFLTKY A55468 152 4 YQGKDLVVVGGGNSAVEAAIFLTKY R34K_CLOPA 144 2 FTDKKVAVIGGGNSGLEAAIDLAGL JC2311 345 2 FKGKRVAVIGGGNSGVEAAIDLAGI AHPF_SALTY 353 2 FEGKHVAVVGGGNSGIESALDLAGI A49911 345 2 FEGKDVAVIGGGNSGVEAAIDLAGI DHNA_BACSP 345 2 PNDRDTASEII7 Length of motif = 17 Motif number = 7 Pyridine nucleotide disulphide reductase-II motif VII - 1 PCODE ST INT KVAIVWSHVIEEVLGDD TRXB_COXBU 200 30 KIKFITNHTVVAVNGYT TRXB_MYCLE 202 27 KISFAWNSEVATIHGEQ TRXB_STRCL 195 27 KIDVIWNSSVVEAYGDG S44027 209 27 KCKVRFNTVATEVIGEN TRXB_PENCH 206 27 KIVLHTDRTLDEVLGDN TRXB_HAEIN 199 30 KVTVRFNTVGVEVKGDD NEUCYS9 202 27 NIILHTNRTLEEVTGDQ TRXB_ECOLI 198 30 KIEILYNTVALEAKGDG A55468 204 27 NVKIIWDSEIRNIVGEN R34K_CLOPA 196 27 NITILTNVATKEIIGND JC2311 397 27 NVDIILNAQTTEVKGDG AHPF_SALTY 405 27 NVDVILNAQTTEITGDE A49911 397 27 NVTVIKNAQTKEITGDD DHNA_BACSP 397 27 PNDRDTASEII8 Length of motif = 22 Motif number = 8 Pyridine nucleotide disulphide reductase-II motif VIII - 1 PCODE ST INT GLFIAIGHDPNTKIFKEQLEMD TRXB_COXBU 239 22 GVFVAIGHEPRSSLVSDVVDID TRXB_MYCLE 240 21 GLFIAVGHDPRTELFKGQLDLD TRXB_STRCL 233 21 GLFFAIGHEPATKFLDGGVELD S44027 250 24 GLFYAVGHDPASGLVKGQVELD TRXB_PENCH 248 25 GLFVAIGHSPNTEIFQGQLELN TRXB_HAEIN 238 22 GLFYAIGHDPATALVKGQLETD NEUCYS9 242 23 GLFVAIGHSPNTAIFEGQLELE TRXB_ECOLI 238 23 GLFYAIGHTPATKIVAGQVDTD A55468 243 22 GVFVYIGYEPKTELFKDSININ R34K_CLOPA 234 21 GVFVQIGLVPSTDWLKDSGLAL JC2311 435 21 GIFVQIGLLPNTHWLEGALERN AHPF_SALTY 444 22 GAFIQIGLAPNTEWLGDTVERN A49911 435 21 GVFVQIGLVPNTDWLDGTLERN DHNA_BACSP 435 21 PNDRDTASEII9 Length of motif = 19 Motif number = 9 Pyridine nucleotide disulphide reductase-II motif IX - 1 PCODE ST INT TNIPGVFPAVVVRGQLYRQ TRXB_COXBU 278 17 TSMDGVFAAGDLVDRTYRQ TRXB_MYCLE 275 13 TNLTGVFAAGDVVDHTYRQ TRXB_STRCL 268 13 TSVPGVFAAGDVQDKKYRQ S44027 285 13 TNVEGVFACGDVQDKRYRQ TRXB_PENCH 283 13 TSVEGVFAAGDVMDHNYRQ TRXB_HAEIN 276 16 TSVEGVFAAGDVQDKRYRQ NEUCYS9 277 13 TSIPGVFAAGDVMDHIYRQ TRXB_ECOLI 276 16 TSVPGFFAAGDVQDSKYRQ A55468 278 13 TNIKGVFAAGDVRSKLIRQ R34K_CLOPA 268 12 TNIPAIFAAGDCTDSAYKQ JC2311 470 13 TSVKGVFAAGDCTTVPYKQ AHPF_SALTY 478 12 TSVPGIFAAGDCTDTPYKQ A49911 469 12 TNVPGVFAAGDCTNSAYKQ DHNA_BACSP 469 12 PNDRDTASEII10 Length of motif = 20 Motif number = 10 Pyridine nucleotide disulphide reductase-II motif X - 1 PCODE ST INT QTIAAAGMGCMPALDAERYL TRXB_COXBU 296 -1 QAITAAGSGCAAAIDAERWL TRXB_MYCLE 293 -1 QAITAAGTGCSAALDAERYL TRXB_STRCL 286 -1 QAITAAGTGCMAALDAEHYL S44027 303 -1 QAITSAGSGCVAALEAEKFI TRXB_PENCH 301 -1 QAITSAGTGCMAALDAERYL TRXB_HAEIN 294 -1 QAITSAGTGCMAALDAEKFL NEUCYS9 295 -1 QAITSAGTGCMAALDAERYL TRXB_ECOLI 294 -1 QAITSAGSGCMAALDAEKYL A55468 296 -1 QLTTAVSDGTVAALMAEKYI R34K_CLOPA 286 -1 QIIISMGSGATAALGAFDYL JC2311 488 -1 QIIIATGEGAKASLSAFDYL AHPF_SALTY 496 -1 QIIVSMGAGATAALGAFDYL A49911 487 -1 QIIISMGSGATAALGAFDYL DHNA_BACSP 487 -1 FINAL MOTIF SETS PNDRDTASEII1 Length of motif = 23 Motif number = 1 Pyridine nucleotide disulphide reductase-II motif I - 3 PCODE ST INT KVTIIGSGPAAHTAAIYLARAEI TRXB_YEAST 4 4 DVIIIGSGPAGYTAAIYAARAQL TRXB_MYCSM 9 9 KVVIIGSGPAAHTAAIYLARAEL TRXB_NEUCR 4 4 DVIVIGSGPAGYTAALYAARAQL O53592 16 16 KLLILGSGPAGYTAAVYAARANL TRXB_ECOLI 7 7 DVIVIGSGPAGYTAALYAARAQL TRXB_MYCTU 16 16 KVTIIGSGPAAHTAAIYLARAEM YHQ6_YEAST 28 28 KLVIIGSGPAGYTAAIYASRALL O84101 44 44 EVIVIGSGPAGYTAALYAARAQL TRXB_MYCLE 13 13 KLLILGSGPAGYTAAIYAARANL TRXB_HAEIN 8 8 NVVIIGSGPAGYTAAIYAARANL O22229 85 85 NVIIIGSGPAGYTAALYTARASL TRXB_STRCL 5 5 KVVIIGSGPAGHTAAIYLARGEL TRXB_SCHPO 5 5 KVVIIGSGAGAHTAAIYLSRAEL TRXB_PENCH 4 4 RLCIVGSGPAAHTAAIYAARAEL TRB1_ARATH 10 10 KIIILGSGPAGYTAAIYSSRANL TRXB_BUCAP 8 8 DIAIIGSGPAGLAAALYGARAKM TRXB_CLOLI 6 6 DIAIIGAGPAGMTAAVYASRANL O54079 7 7 DVIIIGAGPAGMTAALYTSRADL TRXB_LISMO 9 9 NVIIIGSGPAGYTAALYTARRSL TRXB_STRCO 5 5 DLAIIGSGPAGLAAALYGARAKM TRXB_EUBAC 6 6 DVLVVGGGPAGASSAIYAARKGI DHNA_BACSP 210 210 SLIILGSGPAGYTDAIYVARANL TRXB_COXBU 8 8 DVLVVGGGPAGASAAIYTARKGI DHNA_BACSU 210 210 DVIIIGAGPAGMTAAVYTSRANL TRXB_BACSU 7 7 DVLVVGGGPAGAAAAIYAARKGI O82864 213 213 DVLIVGSGPAGAAAAVYSARKGI AHPF_SALTY 214 214 DVLIVGSGPAGAAAAIYSARKGI AHPF_ECOLI 214 214 DVVIIGSGPAAHTAAIYLGRSSL Q24834 6 6 DVLVIGGGPAGASSAIYAARKGI Q06369 210 210 DLVIIGAGPAGLTAAIYAIRAKL R34K_CLOPA 8 8 DVIIIGAGPAGYTAAIYAARFGL O50134 25 25 DVLVIGGGPAGNSAAIYAARKGV Q54469 210 210 DVLVIGGGPAGNSAAIYAARKGV O66266 210 210 DVAIIGGGPAGLTAALYSARYGL O28718 3 3 DVIIVGSGPAGLTAGIYSVMSNY TRXB_BORBU 27 27 DVIIVGAGAAGLSAAQYACRANL TRXB_TREPA 6 6 DVAIVGAGPAGIAAGIYGKRANL TRXB_MYCPN 17 17 DMIVIGAGPAGLTAGIYGGRQGS O26804 6 6 DLVIVGAGPAGIASAIYGKRANL TRXB_MYCGE 17 17 DTIIIGAGPGGLTAGIYAMRGKL Q58931 4 4 PNDRDTASEII2 Length of motif = 16 Motif number = 2 Pyridine nucleotide disulphide reductase-II motif II - 3 PCODE ST INT GGQLTTTTEIENFPGF TRXB_YEAST 42 15 GGALMTTTEVENYPGF TRXB_MYCSM 42 10 GGQLTTTTEIENFPGF TRXB_NEUCR 42 15 GGALMTTTDVENYPGF O53592 49 10 GGQLTTTTEVENWPGD TRXB_ECOLI 40 10 GGALMTTTDVENYPGF TRXB_MYCTU 49 10 GGQLTTTTDIENFPGF YHQ6_YEAST 66 15 GGQLMTTTEVENFPGF O84101 80 13 GGALMTTTEVENYPGF TRXB_MYCLE 46 10 GGQLTTTDEIENWPGD TRXB_HAEIN 41 10 GGQLMTTTEVENFPGF O22229 122 14 GGALMNTTDVENFPGF TRXB_STRCL 39 11 GGQLTTTTDVENFPGF TRXB_SCHPO 43 15 GGQLTTTTDVENFPGF TRXB_PENCH 42 15 PGGQLNQPPRENFPGF TRB1_ARATH 47 14 GGQLMNTNEIENWPGD TRXB_BUCAP 41 10 GGQIVITHEVANYPGS TRXB_CLOLI 39 10 GGQMANTEEVENFPGF O54079 40 10 GGQMVNTAEVENYPGF TRXB_LISMO 42 10 GGALMNTTEVENFPGF TRXB_STRCO 39 11 GGQIVITHEVANYPGS TRXB_EUBAC 39 10 GGQIMDTLSIENFISQ DHNA_BACSP 242 9 GGQLMTTTDVANWPGE TRXB_COXBU 41 10 GGQVLDTMSIENFISV DHNA_BACSU 242 9 GGQMANTEDVENYPGF TRXB_BACSU 40 10 GGQVLDTLAIENFISV O82864 245 9 GGQVLDTVDIENYISV AHPF_SALTY 246 9 GGQILDTVDIENYISV AHPF_ECOLI 246 9 GGQLTTTTIIENFRIS Q24834 44 15 GGQVMDTLGIENFIGT Q06369 242 9 GGQIRETYTVENFPGF R34K_CLOPA 41 10 GGNMAITDLIENYPGF O50134 57 9 GGQVMETVGIENMIGT Q54469 242 9 GGQVMETVGIENMIGT O66266 242 9 VSQLSLAAKIENYPGF O28718 36 10 GGQLTTTTEVYNYPGF TRXB_BORBU 60 10 GGQALLIDSLENYPGY TRXB_TREPA 39 10 GGKVVKTNIVENYPGY TRXB_MYCPN 50 10 GGLGLEVPMMENYPGF O26804 39 10 GGKIVKTNIVENYPGF TRXB_MYCGE 50 10 GGRIAEAGIVENYPGF Q58931 37 10 PNDRDTASEII3 Length of motif = 11 Motif number = 3 Pyridine nucleotide disulphide reductase-II motif III - 3 PCODE ST INT GSELMDRMREQ TRXB_YEAST 63 5 GPELMDQMREQ TRXB_MYCSM 63 5 GQELMDKMKAQ TRXB_NEUCR 63 5 GPELMDEMREQ O53592 70 5 GPLLMERMHEH TRXB_ECOLI 61 5 GPELMDEMREQ TRXB_MYCTU 70 5 GSELMERMRKQ YHQ6_YEAST 87 5 GHQLMDLMKTQ O84101 101 5 GPELMDDMREQ TRXB_MYCLE 67 5 GSGLMQRMLQH TRXB_HAEIN 62 5 GPDLMEKMRKQ O22229 143 5 GPDLMDNMRAQ TRXB_STRCL 60 5 GTTLTENFRAQ TRXB_SCHPO 64 5 GAELMDNMRAQ TRXB_PENCH 63 5 GVELTDKFRKQ TRB1_ARATH 68 5 GPELMNRMHEH TRXB_BUCAP 62 5 GPSLIGRMEEQ TRXB_CLOLI 60 5 GPDLSTKMFEH O54079 60 4 GPDLSDKMLSG TRXB_LISMO 62 4 GPELMDNMRAQ TRXB_STRCO 60 5 GPSLIERMEEQ TRXB_EUBAC 60 5 GPKLAASLEEH DHNA_BACSP 262 4 GPKLLERMQKH TRXB_COXBU 62 5 GPKLAASLEEH DHNA_BACSU 262 4 GPELSNKMFEH TRXB_BACSU 60 4 GPKLATALEEH O82864 265 4 GQKLAGALKAH AHPF_SALTY 266 4 GQKLAGALKVH AHPF_ECOLI 266 4 GNELMMNMRTQ Q24834 67 7 GPKLISEIEQH Q06369 262 4 GADLADKMEEH R34K_CLOPA 61 4 GSELSKKMYDQ O50134 78 5 GPQLMAQVEEH Q54469 262 4 GPQLMAQVEEH O66266 262 4 GMELLEKMKEQ O28718 55 3 GRNLMLNMREQ TRXB_BORBU 81 5 GFEYAENMKKQ TRXB_TREPA 60 5 GPDLGLEMYNH TRXB_MYCPN 70 4 GMSLVTKMKKQ O26804 59 4 GPELGLEMYNH TRXB_MYCGE 70 4 GYELAEKFKNH Q58931 57 4 PNDRDTASEII4 Length of motif = 9 Motif number = 4 Pyridine nucleotide disulphide reductase-II motif IV - 3 PCODE ST INT DAIILATGA TRXB_YEAST 112 38 RAVILAMGA TRXB_MYCSM 108 34 DSIILATGA TRXB_NEUCR 111 37 RAVILAMGA O53592 116 35 DALIIATGA TRXB_ECOLI 106 34 RAVILAMGA TRXB_MYCTU 116 35 DAIILATGA YHQ6_YEAST 136 38 DACIIATGA O84101 146 34 RAVILAMGT TRXB_MYCLE 113 35 DALIIATGA TRXB_HAEIN 107 34 HSIIYATGA O22229 188 34 KAVIVTTGS TRXB_STRCL 106 35 DSVILATGA TRXB_SCHPO 113 38 DAVIIATGA TRXB_PENCH 115 41 DAVILAIGA TRB1_ARATH 113 34 DAVIIATGA TRXB_BUCAP 107 34 KAVIVATGA TRXB_CLOLI 105 34 KAVIIATGA O54079 105 34 RAIIIATGA TRXB_LISMO 107 34 KAVIVTTGS TRXB_STRCO 106 35 KSVILATGA TRXB_EUBAC 105 34 KSVILSTGA DHNA_BACSP 308 35 DALIIATGA TRXB_COXBU 108 35 KTVILSTGA DHNA_BACSU 308 35 RAVIIAAGA TRXB_BACSU 105 34 KTVILATGA O82864 314 38 RSIIIATGA AHPF_SALTY 316 39 RSIIVATGA AHPF_ECOLI 316 39 KSVIIASNA Q24834 113 35 KTIILATGA Q06369 308 35 KALIIATGA R34K_CLOPA 107 35 KTIIIAVGA O50134 131 42 KTAVLALGA Q54469 308 35 KTAVLALGA O66266 308 35 KAIIVATGG O28718 100 34 KAVIIAVGS TRXB_BORBU 126 34 MSVILATGA TRXB_TREPA 105 34 KTVIYATGM TRXB_MYCPN 116 35 SAIIFATGS O26804 103 33 KTVIYATGM TRXB_MYCGE 116 35 KTIVIATGT Q58931 102 34 PNDRDTASEII5 Length of motif = 13 Motif number = 5 Pyridine nucleotide disulphide reductase-II motif V - 3 PCODE ST INT WQKGISACAVCDG TRXB_YEAST 134 13 TGMGVSTCATCDG TRXB_MYCSM 130 13 WQNGISACAVCDG TRXB_NEUCR 133 13 LGRGVSSCATCDG O53592 138 13 KGRGVSACATCDG TRXB_ECOLI 128 13 LGRGVSSCATCDG TRXB_MYCTU 138 13 WQQGISACAVCDG YHQ6_YEAST 158 13 WQKGVTACAVCDG O84101 170 15 LGRGVSACATCDG TRXB_MYCLE 135 13 KGRGVSACATCDG TRXB_HAEIN 129 13 WSRGISACAICDG O22229 210 13 SGRGVSWCATCDG TRXB_STRCL 128 13 WQAGISACAVCDG TRXB_SCHPO 135 13 WQNGISACAVCDG TRXB_PENCH 137 13 WNRGISACAVCDG TRB1_ARATH 139 17 KGKGISTCAVCDG TRXB_BUCAP 129 13 TGKGVSYCATCDA TRXB_CLOLI 127 13 GGRGVSYCAVCDG O54079 127 13 SGRGVSYCAVCDG TRXB_LISMO 129 13 SGRGVSWCATCDG TRXB_STRCO 128 13 TGKGVSYCATCDA TRXB_EUBAC 127 13 KNKGVAYCPHCDG DHNA_BACSP 330 13 MGKGVSACATCDG TRXB_COXBU 130 13 KNKGVAYCPHCDG DHNA_BACSU 330 13 GGRGVSYCAVCDG TRXB_BACSU 127 13 RGRGVAYCPHCDG O82864 336 13 RTKGVTYCPHCDG AHPF_SALTY 338 13 RTKGVTYCPHCDG AHPF_ECOLI 338 13 AKIGVSACAICDG Q24834 135 13 KNKGVAYCTHCDA Q06369 330 13 HGKVIHYCELCDG R34K_CLOPA 129 13 TGRGVSYCATCDG O50134 153 13 FNKGVTYCPHCDG Q54469 330 13 FNKGVTYCPHCDG O66266 330 13 IGRGVSYCATCDG O28718 122 13 WNKGISVCAICDG TRXB_BORBU 149 14 LGRGVSYCATCDG TRXB_TREPA 127 13 YGKGISYCAICDG TRXB_MYCPN 138 13 LGRGVCYCATCDG O26804 125 13 YGKGISYCAICDA TRXB_MYCGE 138 13 IGRGISYCTMCDA Q58931 123 12 PNDRDTASEII6 Length of motif = 25 Motif number = 6 Pyridine nucleotide disulphide reductase-II motif VI - 3 PCODE ST INT FRNKPLAVIGGGDSACEEAQFLTKY TRXB_YEAST 151 4 FRDQDIVVVGGGDSAMEEATFLTRF TRXB_MYCSM 145 2 FRNKHLVVIGGGDSAAEEAMYLTKY TRXB_NEUCR 150 4 FRDQDIAVIGGGDSAMEEATFLTRF O53592 153 2 YRNQKVAVIGGGNTAVEEALYLSNI TRXB_ECOLI 143 2 FRDQDIAVIGGGDSAMEEATFLTRF TRXB_MYCTU 153 2 FRNKPLAVIGGGDSACEEAEFLTKY YHQ6_YEAST 175 4 FRDKDLFVVGGGDSALEEAMFLTRY O84101 187 4 FRGQDIAVIGGGDSAMEEALFLTRF TRXB_MYCLE 150 2 YRNKPVGVIGGGNTAVEEALYLANI TRXB_HAEIN 144 2 FKGQVLAVVGGGDTATEEALYLTKY O22229 227 4 FKDQDIVVVGGGDTAMEEATFLSRF TRXB_STRCL 143 2 YRNKPLAVVGGGDSAAEEAQFLTKY TRXB_SCHPO 152 4 FRNKPLYVIGGGDSAAEEAMFLAKY TRXB_PENCH 154 4 FRNKPLAVIGGGDSAMEEANFLTKY TRB1_ARATH 156 4 YKNKEIAVVGGGNTAIEETLYLSNF TRXB_BUCAP 144 2 FEDMEVFVIGGGDTAVEEAMFLTKF TRXB_CLOLI 142 2 FKNKRLFVIGGGDSAVEEGTFLTKF O54079 142 2 FKNRELIVVGGGDSAVEEGTYLTRY TRXB_LISMO 144 2 FFKDQDIAVIGGDTAMEEATFLSRF TRXB_STRCO 142 1 FEDMEVFVVGGGDTAVEEAMYLAKF TRXB_EUBAC 142 2 FEGKDVAVIGGGNSGVEAAIDLAGI DHNA_BACSP 345 2 YRAKKVAVVGGGNTSVEEALYLSHI TRXB_COXBU 145 2 FEGKDVAVIGGGNSGIEAAIDLAGI DHNA_BACSU 345 2 FKGKELVVVGGGDSAVEEGVYLTRF TRXB_BACSU 142 2 FKGKRVAVIGGGNSGVEAAIDLAGI O82864 351 2 FKGKRVAVIGGGNSGVEAAIDLAGI AHPF_SALTY 353 2 FKGKRVAVIGGGNSGVEAAIDLAGI AHPF_ECOLI 353 2 FRNKVLMVEGGGDAAMEEALHLTKY Q24834 152 4 FEGKHVAVVGGGNSGIESALDLAGI Q06369 345 2 YQGKDLVVVGGGNSAVEAAIFLTKY R34K_CLOPA 144 2 FVGKEVIVVGGGNTALQEALYLHSI O50134 168 2 FTDKKVAVIGGGNSGLEAAIDLAGL Q54469 345 2 FTDKKVAVIGGGNSGLEAAIDLAGL O66266 345 2 FRGKKVIVYGSGKEAIEDAIYLHDI O28718 137 2 FKGKRVAVIGGGNTALSESIYLSKL TRXB_BORBU 164 2 FRNKHVVVIGGGDAACDESLVLSRL TRXB_TREPA 142 2 YKDQVVGVVGGGNSAIQEALYLASM TRXB_MYCPN 153 2 YKGRKVLMVGGGNSAAQEAVFLKNI O26804 140 2 YKGKTVGVVGGGNSAIQEAIYLSSI TRXB_MYCGE 153 2 YLNKEVIVIGRDTPAIMSAINLKDI Q58931 138 2 PNDRDTASEII7 Length of motif = 17 Motif number = 7 Pyridine nucleotide disulphide reductase-II motif VII - 3 PCODE ST INT KIEILYNTVALEAKGDG TRXB_YEAST 203 27 KITFLTNTEITQIEGDP TRXB_MYCSM 197 27 KVTVRFNTVGVEVKGDD TRXB_NEUCR 202 27 KIRFLTNHTVVAVDGDT O53592 205 27 NIILHTNRTLEEVTGDQ TRXB_ECOLI 198 30 KIRFLTNHTVCAVDGDT TRXB_MYCTU 205 27 NIIVLFNTVALEAKGDG YHQ6_YEAST 227 27 KIFFLWNSEIVKISGDT O84101 239 27 KIKFITNHTVVAVNGYT TRXB_MYCLE 202 27 KIVLHTDRTLDEVLGDN TRXB_HAEIN 199 30 NITVHYNTETVDVLSNT O22229 279 27 KISFAWNSEVATIHGEQ TRXB_STRCL 195 27 KVEVLWNTVAEEAQGDG TRXB_SCHPO 204 27 KCKVRFNTVATEVIGEN TRXB_PENCH 206 27 KIDVIWNSSVVEAYGDG TRB1_ARATH 208 27 KVILHLNSTIEDILGNN TRXB_BUCAP 199 30 KLNFMWNTVIEEIKGDG TRXB_CLOLI 194 27 KIDFIWSHTLKSINEKD O54079 194 27 KVDFIWNSTVEEIVGDG TRXB_LISMO 196 27 KISFVWDSEVAEVQGDQ TRXB_STRCO 194 27 KLDFMWNSAIEEIKGDG TRXB_EUBAC 194 27 NVTVIKNAQTKEITGDD DHNA_BACSP 397 27 KVAIVWSHVIEEVLGDD TRXB_COXBU 200 30 NVTVVKNAQTKEITGDQ DHNA_BACSU 397 27 KVDFLWNKTVKEIHEEN TRXB_BACSU 194 27 NVNVITSALTTEVLGNG O82864 403 27 NVDIILNAQTTEVKGDG AHPF_SALTY 405 27 NVDIILNAQTTEVKGDG AHPF_ECOLI 405 27 KIEVIWNSELVELEGDG Q24834 204 27 NVDVILNAQTTEITGDE Q06369 397 27 NVKIIWDSEIRNIVGEN R34K_CLOPA 196 27 GIPAILNTVVTEIKGTN O50134 219 26 NITILTNVATKEIIGND Q54469 397 27 NITILTNVATKEIIGND O66266 397 27 GIPVHYSTTIRKIIGSG O28718 188 26 NIEILYNSEAIEVDGKS TRXB_BORBU 216 27 HIAVQWNTTLEAVRGET TRXB_TREPA 194 27 NVVFHLNYTVKELLGNN TRXB_MYCPN 205 27 EIPVIWNSVVKEIGGDE O26804 191 26 NVVFHLNATVKQLIGQE TRXB_MYCGE 205 27 NVEIIYNAKPLEIVGEE Q58931 191 28 PNDRDTASEII8 Length of motif = 22 Motif number = 8 Pyridine nucleotide disulphide reductase-II motif VIII - 3 PCODE ST INT GLFYAIGHTPATKIVAGQVDTD TRXB_YEAST 242 22 GVFVAIGHDPRSELVRGQVELD TRXB_MYCSM 235 21 GLFYAIGHDPATALVKGQLETD TRXB_NEUCR 242 23 GVFVAIGHEPRSGLVREAIDVD O53592 243 21 GLFVAIGHSPNTAIFEGQLELE TRXB_ECOLI 238 23 GVFVAIGHEPRSGLVREAIDVD TRXB_MYCTU 243 21 GLFYAIGHSPATDIVKGQVDEE YHQ6_YEAST 266 22 GVFFAIGHQPNTAFLGGQVALD O84101 277 21 GVFVAIGHEPRSSLVSDVVDID TRXB_MYCLE 240 21 GLFVAIGHSPNTEIFQGQLELN TRXB_HAEIN 238 22 GLFYGIGHSPNSQLLEGQVELD O22229 319 23 GLFIAVGHDPRTELFKGQLDLD TRXB_STRCL 233 21 GLFYAIGHIPATKLVAEQIELD TRXB_SCHPO 243 22 GLFYAVGHDPASGLVKGQVELD TRXB_PENCH 248 25 GLFFAIGHEPATKFLDGGVELD TRB1_ARATH 249 24 GLFVAIGYIPNTDIFTDQLKMK TRXB_BUCAP 240 24 GIFVFIGYDPKSALVEGKLELD TRXB_CLOLI 238 27 GVFIYIGMKPLTAPFKDLGITN O54079 233 22 GVFIYVGLVPLTKAFLNLGITD TRXB_LISMO 235 22 ALFIAIGHDPRTELFKGQLDLD TRXB_STRCO 232 21 GIFVFIGYIPKSDVFKGKITLD TRXB_EUBAC 238 27 GVFVQIGLVPNTDWLDGTLERN DHNA_BACSP 435 21 GLFIAIGHDPNTKIFKEQLEMD TRXB_COXBU 239 22 GVFVQIGLVPNTEWLEGTVERN DHNA_BACSU 435 21 GVFIYIGMLPLSKPFENLGITN TRXB_BACSU 233 22 GIFVQIGLLPNTDWLKGTVELS O82864 442 22 GIFVQIGLLPNTHWLEGALERN AHPF_SALTY 444 22 GIFVQIGLLPNTNWLEGAVERN AHPF_ECOLI 444 22 GLFYAIGHSQNSKFLGGQVKTA Q24834 243 22 GAFIQIGLAPNTEWLGDTVERN Q06369 435 21 GVFVYIGYEPKTELFKDSININ R34K_CLOPA 234 21 GVFIFIGYEPKTDFVKHLGITD O50134 257 21 GVFVQIGLVPSTDWLKDSGLAL Q54469 435 21 GVFVQIGLVPSTDWLKDSGLAL O66266 435 21 GIFVAIGMRPATDVVAELGVER O28718 226 21 AVFMAVGYKPNTEFLKGFLDLD TRXB_BORBU 254 21 AVFFFIGMVPITGLLPDAEKDS TRXB_TREPA 232 21 CVFPYIGFESITKPVEHLNLKL TRXB_MYCPN 243 21 GVFIAIGEEPLNQLAVDLGVEV O26804 229 21 CLFPYIGFESNNKPVLDLKLNL TRXB_MYCGE 243 21 GIFISLGHVPNTEFLKDSGIEL Q58931 227 19 PNDRDTASEII9 Length of motif = 19 Motif number = 9 Pyridine nucleotide disulphide reductase-II motif IX - 3 PCODE ST INT TSVPGFFAAGDVQDSKYRQ TRXB_YEAST 277 13 TSLDGVFAAGDLVDHTYRQ TRXB_MYCSM 270 13 TSVEGVFAAGDVQDKRYRQ TRXB_NEUCR 277 13 TSLPGVFAAGDLVDRTYRQ O53592 278 13 TSIPGVFAAGDVMDHIYRQ TRXB_ECOLI 276 16 TSLPGVFAAGDLVDRTYRQ TRXB_MYCTU 278 13 TSVPGFFAAGDVQDSRYRQ YHQ6_YEAST 301 13 TSVPGVFAAGDVQDKYYRQ O84101 312 13 TSMDGVFAAGDLVDRTYRQ TRXB_MYCLE 275 13 TSVEGVFAAGDVMDHNYRQ TRXB_HAEIN 276 16 TSVEGVFAAGDVQDHEWRQ O22229 354 13 TNLTGVFAAGDVVDHTYRQ TRXB_STRCL 268 13 TSIPGFFAAGDVQDKVFRQ TRXB_SCHPO 278 13 TNVEGVFACGDVQDKRYRQ TRXB_PENCH 283 13 TSVPGVFAAGDVQDKKYRQ TRB1_ARATH 284 13 TNIPGVFAAGDVIDHVYRQ TRXB_BUCAP 278 16 TNVEGVFAAGDIRVKSLRQ TRXB_CLOLI 272 12 TSVPGIFAAGDVRDKGLRQ O54079 267 12 TNLPGIFAAGDVRAKSLRQ TRXB_LISMO 269 12 TNLTGVFGAGDVVDHTYRQ TRXB_STRCO 266 12 TNVEGVFAAGDIRVKSLRQ TRXB_EUBAC 272 12 TNVPGVFAAGDCTNSAYKQ DHNA_BACSP 469 12 TNIPGVFPAVVVRGQLYRQ TRXB_COXBU 278 17 TSVPGLFAAGDCTDSAYNQ DHNA_BACSU 469 12 TKVEGIFAAGDIREKSLRQ TRXB_BACSU 267 12 TSIPGVFAAGDVTTVPYKQ O82864 476 12 TSVKGVFAAGDCTTVPYKQ AHPF_SALTY 478 12 TNVKGVFAAGDCTTVPYKQ AHPF_ECOLI 478 12 TSVDGVFACGDVCDRVYRQ Q24834 276 11 TSVPGIFAAGDCTDTPYKQ Q06369 469 12 TNIKGVFAAGDVRSKLIRQ R34K_CLOPA 268 12 TKVPGIFAAGDITNVFKQI O50134 291 12 TNIPAIFAAGDCTDSAYKQ Q54469 470 13 TNIPAIFAAGDCTDSAYKQ O66266 470 13 TNVEGVFAAGDCCDNPLKQ O28718 261 13 TSVDGVFSCGDVSNKLYAQ TRXB_BORBU 288 12 TSVEGIFAAGDVRAKSFRQ TRXB_TREPA 265 11 TSLKGLFAAGDCRSKHFRQ TRXB_MYCPN 278 13 TNVPLVYAAGDITGGLNQW O26804 264 13 TNIKGFYVAGDCRSKSFRQ TRXB_MYCGE 278 13 TNIDGIYAVGDVRGGVMQV Q58931 262 13 PNDRDTASEII10 Length of motif = 20 Motif number = 10 Pyridine nucleotide disulphide reductase-II motif X - 3 PCODE ST INT QAITSAGSGCMAALDAEKYL TRXB_YEAST 295 -1 QAITAAGSGCAASIDAERWL TRXB_MYCSM 288 -1 QAITSAGTGCMAALDAEKFL TRXB_NEUCR 295 -1 QAVTAAGSGCAAAIDAERWL O53592 296 -1 QAITSAGTGCMAALDAERYL TRXB_ECOLI 294 -1 QAVTAAGSGCAAAIDAERWL TRXB_MYCTU 296 -1 QAVTSAGSGCIAALDAERYL YHQ6_YEAST 319 -1 QAITSAGSGCMAALDAERFL O84101 330 -1 QAITAAGSGCAAAIDAERWL TRXB_MYCLE 293 -1 QAITSAGTGCMAALDAERYL TRXB_HAEIN 294 -1 QAVTAAGSGCIAALSAERYL O22229 372 -1 QAITAAGTGCSAALDAERYL TRXB_STRCL 286 -1 QAITSAGSGCQAALLAMHYL TRXB_SCHPO 296 -1 QAITSAGSGCVAALEAEKFI TRXB_PENCH 301 -1 QAITAAGTGCMAALDAEHYL TRB1_ARATH 302 -1 QAITSSASGCMAALDSERYL TRXB_BUCAP 296 -1 QVVTATADGAIAAVQAEKYI TRXB_CLOLI 290 -1 QIVTATGDGSIAAQSAAEYI O54079 285 -1 QIVTATGDGGLAGQNAQKYV TRXB_LISMO 287 -1 QAITAAGTGCSAAVDAEPFL TRXB_STRCO 284 -1 QVVTACADGAIAATQAEKYV TRXB_EUBAC 290 -1 QIIISMGSGATAALGAFDYL DHNA_BACSP 487 -1 QTIAAAGMGCMPALDAERYL TRXB_COXBU 296 -1 QIIISMGSGATAALGAFDYL DHNA_BACSU 487 -1 QIVTATGDGSIAAQSVQHYV TRXB_BACSU 285 -1 QIVIAVGEGAKASLAAFDHL O82864 494 -1 QIIIATGEGAKASLSAFDYL AHPF_SALTY 496 -1 QIIIATGEGAKASLSAFDYL AHPF_ECOLI 496 -1 QAIVAAGSGCMAALSCEKWL Q24834 294 -1 QIIVSMGAGATAALGAFDYL Q06369 487 -1 QLTTAVSDGTVAALMAEKYI R34K_CLOPA 286 -1 QIAVAVGQGAIAANSAKEFI O50134 308 -2 QIIISMGSGATAALGAFDYL Q54469 488 -1 QIIISMGSGATAALGAFDYL O66266 488 -1 QVVTACGDGAVAAYSAYKYL O28718 279 -1 QAITAAAEGFIASVELGNFL TRXB_BORBU 306 -1 QVITATSDGALAAHAAASYI TRXB_TREPA 283 -1 QIGTAINDGIIAVLTIRDVL TRXB_MYCPN 296 -1 QWVTACAEGAIAATYAYREI O26804 281 -2 QIATAISDGVTAVLKVRDDI TRXB_MYCGE 296 -1 QVAKAVGDGCVAMANIIKYL Q58931 279 -2

User query: Display/Full Code "PNDRDTASEII"