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"