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PR00765

Identifier
CRBOXYPTASEA  [View Relations]  [View Alignment]  
Accession
PR00765
No. of Motifs
4
Creation Date
18-JUN-1997  (UPDATE 14-JUN-1999)
Title
Carboxypeptidase A metalloprotease (M14) family signature 
Database References

PROSITE; PS00132 CARBOXYPEPT_ZN_1; PS00133 CARBOXYPEPT_ZN_2
PFAM; PF00246 Zn_carbOpep
INTERPRO; IPR000834
PDB; 1PCA
SCOP; 1PCA
CATH; 1PCA
Literature References
1. RAWLINGS, N.D. AND BARRETT, A.J.
Evolutionary families of metallopeptidases.
METHODS ENZYMOL. 248 183-228 (1995).
 
2. OSTERMAN, A.L., GRISHIN, N.V., SMULEVITCH, S.V., MATZ, M.V., ZAGNITKO,
O.P., REVINA, L.P. AND STEPANOV, V.M.
Primary structure of carboxypeptidase T: delineation of functionally
relevant features in Zn-carboxypeptidase family.
J.PROTEIN CHEM. 11 561-570 (1992).
 
3. REES, D.C., LEWIS, M. AND LIPSCOMB, W.N.
Refined crystal structure of carboxypeptidase A at 1.54A resoltion.
J.MOL.BIOL. 168 367-387 (1983).
 
4. GUASCH, A., COLL, M., AVILES, F.X. AND HUBER, R.
Three-dimensional structure of porcine pancreatic procarboxypeptidase A. A
comparison of the A and B zymogens and their determinants for inhibition 
and activation.
J.MOL.BIOL. 224 141-157 (1992).

Documentation
Metalloproteases are the most diverse of the four main types of protease,
with more than 30 families identified to date [1]. Of these, around
half contain the HEXXH motif, which has been shown in crystallographic
studies to form part of the metal-binding site [1]. The HEXXH motif is 
relatively common, but can be more stringently defined for metallo-
proteases as abXHEbbHbc, where a is most often valine or threonine and 
forms part of the S1' subsite in thermolysin and neprilysin, b is an
uncharged residue, and c a hydrophobic residue. Proline is never found
in this site, possibly because it would break the helical structure 
adopted by this motif in metalloproteases [1].
 
Metalloproteases can be split into five groups on the basis of their metal-
binding residues: the first three contain the HEXXH motif, the other two
do not [1]. In the first group, a glutamic acid completes the active site -
these are termed HEXXH+E: all families in this group show some sequence
relationship and have been assigned to clan MA [1]. The second group, which
have a third histidine as the extra metal-binding residue, are termed
HEXXH+H and are grouped into clan MB on the basis of their inter-relation-
ship [1]. In the third group, the additional metal-binding residues are
unidentified. The fourth group is diverse - the metal-binding residues are
known but do not form the HEXXH motif. And the fifth group comprises the
remaining families where the metal-binding residues are as yet unknown [1].
 
The carboxypeptidase A family (M14) can be divided into two subfamilies:
carboxypeptidase H (regulatory) and carboxypeptidase A (digestive) [1].
Members of the H family have longer C-termini than those of family A [2],
and carboxypeptidase M (a member of the H family) is bound to the membrane
by a glycosylphosphatidylinositol anchor, unlike the majority of the M14
family, which are soluble [1].
 
The zinc ligands have been determined as two histidines and a glutamate,
and the catalytic residue has been identified as a C-terminal glutamate,
but these do not form the characteristic metalloprotease HEXXH motif [1,3].
Members of the carboxypeptidase A family are synthesised as inactive
molecules with propeptides that must be cleaved to activate the enzyme.
Structural studies of carboxypeptidases A and B reveal the propeptide to
exist as a globular domain, followed by an extended alpha-helix; this
shields the catalytic site, without specifically binding to it, while the
substrate-binding site is blocked by making specific contacts [1,4]. 
 
CRBOXYPTASEA is a 4-element fingerprint that provides a signature for the
carboxypeptidase (M14) family of metalloproteases. The fingerprint was
derived from an initial alignment of 13 sequences: the motifs were drawn
from conserved regions around the active site, motifs 2 and 4 containing
the regions encoded by PROSITE patterns CARBOXYPEPT_ZN_1 (PS00132) and
CARBOXYPEPT_ZN_2 (PS00133), which contain the first His and Glu zinc
ligands, and the second zinc-binding His respectively. Three iterations on
OWL29.3 were required to reach convergence, at which point a true set
comprising 50 sequences was identified. Five partial matches were also
found: S51739 and JC5256 are AEBP1 transcription factors with carboxy-
peptidase activity that match motifs 2 and 4 (the zinc-binding regions);
ENP1_BACSH is a gamma-D-glutamyl-L-diamino acid endopeptidase I that shows
some C-terminal similarity to the carboxypeptidase A family; and PMASPA and
ACU37756 are fragments that match only 2 motifs.
 
An update on SPTR37_9f identified a true set of 52 sequences, and 13
partial matches.
Summary Information
  52 codes involving  4 elements
2 codes involving 3 elements
4 codes involving 2 elements
Composite Feature Index
452525252
32202
20413
1234
True Positives
CBP1_HUMAN    CBP1_RAT      CBP2_RAT      CBPA_ANOGA    
CBPA_BOVIN CBPB_ASTFL CBPB_BOVIN CBPB_CANFA
CBPB_HUMAN CBPB_PIG CBPB_RAT CBPC_HUMAN
CBPC_MOUSE CBPC_RAT CBPH_BOVIN CBPH_HUMAN
CBPH_LOPAM CBPH_MOUSE CBPH_RAT CBPN_HUMAN
CBPS_STRCP CBPS_STRGR CBPT_THEVU CPA2_HUMAN
O00520 O14418 O15377 O17754
O35850 O46058 O54858 O54859
O54860 O57512 O75976 O77063
O89001 P73902 P90667 P90668
P91359 P91755 P92190 Q15114
Q19121 Q22825 Q23099 Q23318
Q24094 Q24095 Q90240 YQGT_BACSU
True Positive Partials
Codes involving 3 elements
O74818 YHT2_YEAST
Codes involving 2 elements
ENP1_BACSH O88442 Q14113 Q61281
Sequence Titles
CBP1_HUMAN  CARBOXYPEPTIDASE A1 PRECURSOR (EC 3.4.17.1) - HOMO SAPIENS (HUMAN). 
CBP1_RAT CARBOXYPEPTIDASE A1 PRECURSOR (EC 3.4.17.1) - RATTUS NORVEGICUS (RAT).
CBP2_RAT CARBOXYPEPTIDASE A2 PRECURSOR (EC 3.4.17.15) - RATTUS NORVEGICUS (RAT).
CBPA_ANOGA ZINC CARBOXYPEPTIDASE A PRECURSOR (EC 3.4.17.-) - ANOPHELES GAMBIAE (AFRICAN MALARIA MOSQUITO).
CBPA_BOVIN CARBOXYPEPTIDASE A PRECURSOR (EC 3.4.17.1) - BOS TAURUS (BOVINE).
CBPB_ASTFL CARBOXYPEPTIDASE B (EC 3.4.17.2) - ASTACUS FLUVIATILIS (BROAD-FINGERED CRAYFISH) (ASTACUS ASTACUS).
CBPB_BOVIN CARBOXYPEPTIDASE B (EC 3.4.17.2) - BOS TAURUS (BOVINE).
CBPB_CANFA CARBOXYPEPTIDASE B PRECURSOR (EC 3.4.17.2) (47 KD ZYMOGEN GRANULE MEMBRANE ASSOCIATED PROTEIN) (ZAP47) - CANIS FAMILIARIS (DOG).
CBPB_HUMAN CARBOXYPEPTIDASE B PRECURSOR (EC 3.4.17.2) (PANCREAS-SPECIFIC PROTEIN) (PASP) - HOMO SAPIENS (HUMAN).
CBPB_PIG CARBOXYPEPTIDASE B PRECURSOR (EC 3.4.17.2) - SUS SCROFA (PIG).
CBPB_RAT CARBOXYPEPTIDASE B PRECURSOR (EC 3.4.17.2) - RATTUS NORVEGICUS (RAT).
CBPC_HUMAN MAST CELL CARBOXYPEPTIDASE A PRECURSOR (EC 3.4.17.1) (MC-CPA) (CARBOXYPEPTIDASE A3) - HOMO SAPIENS (HUMAN).
CBPC_MOUSE MAST CELL CARBOXYPEPTIDASE A PRECURSOR (EC 3.4.17.1) (MC-CPA) (CARBOXYPEPTIDASE A3) - MUS MUSCULUS (MOUSE).
CBPC_RAT MAST CELL CARBOXYPEPTIDASE (EC 3.4.17.1) (RMC-CP) (CARBOXYPEPTIDASE A3) - RATTUS NORVEGICUS (RAT).
CBPH_BOVIN CARBOXYPEPTIDASE H (EC 3.4.17.10) (CPH) (CARBOXYPEPTIDASE E) (CPE) (ENKEPHALIN CONVERTASE) (PROHORMONE PROCESSING CARBOXYPEPTIDASE) - BOS TAURUS (BOVINE).
CBPH_HUMAN CARBOXYPEPTIDASE H PRECURSOR (EC 3.4.17.10) (CPH) (CARBOXYPEPTIDASE E) (CPE) (ENKEPHALIN CONVERTASE) (PROHORMONE PROCESSING CARBOXYPEPTIDASE) - HOMO SAPIENS (HUMAN).
CBPH_LOPAM CARBOXYPEPTIDASE H PRECURSOR (EC 3.4.17.10) (CPH) (CARBOXYPEPTIDASE E) (CPE) (ENKEPHALIN CONVERTASE) (PROHORMONE PROCESSING CARBOXYPEPTIDASE) - LOPHIUS AMERICANUS (AMERICAN GOOSEFISH) (ANGLERFISH).
CBPH_MOUSE CARBOXYPEPTIDASE H PRECURSOR (EC 3.4.17.10) (CPH) (CARBOXYPEPTIDASE E) (CPE) (ENKEPHALIN CONVERTASE) (PROHORMONE PROCESSING CARBOXYPEPTIDASE) - MUS MUSCULUS (MOUSE).
CBPH_RAT CARBOXYPEPTIDASE H PRECURSOR (EC 3.4.17.10) (CPH) (CARBOXYPEPTIDASE E) (CPE) (ENKEPHALIN CONVERTASE) (PROHORMONE PROCESSING CARBOXYPEPTIDASE) - RATTUS NORVEGICUS (RAT).
CBPN_HUMAN CARBOXYPEPTIDASE N CATALYTIC CHAIN PRECURSOR (EC 3.4.17.3) (ARGININE CARBOXYPEPTIDASE) (KININASE 1) (SERUM CARBOXYPEPTIDASE N) (SCPN) (ANAPHYLATOXIN INACTIVATOR) (PLASMA CARBOXYPEPTIDASE B) - HOMO SAPIENS (HUMAN).
CBPS_STRCP ZINC-CARBOXYPEPTIDASE PRECURSOR (EC 3.4.17.-) - STREPTOMYCES CAPREOLUS.
CBPS_STRGR ZINC-CARBOXYPEPTIDASE PRECURSOR (EC 3.4.17.-) (CPASE SG) (CPSG) - STREPTOMYCES GRISEUS.
CBPT_THEVU CARBOXYPEPTIDASE T PRECURSOR (EC 3.4.17.18) - THERMOACTINOMYCES VULGARIS.
CPA2_HUMAN CARBOXYPEPTIDASE A2 PRECURSOR (EC 3.4.17.15) - HOMO SAPIENS (HUMAN).
O00520 CARBOXYPEPTIDASE Z PRECURSOR - HOMO SAPIENS (HUMAN).
O14418 CARBOXYPEPTIDASE - METARHIZIUM ANISOPLIAE.
O15377 CARBOXYPEPTIDASE D PRECURSOR - HOMO SAPIENS (HUMAN).
O17754 F01D4.4 PROTEIN - CAENORHABDITIS ELEGANS.
O35850 CARBOXYPEPTIDASE D PRECURSOR - RATTUS NORVEGICUS (RAT).
O46058 COSMID 171D11 - DROSOPHILA MELANOGASTER (FRUIT FLY).
O54858 CARBOXYPEPTIDASE Z - RATTUS NORVEGICUS (RAT).
O54859 CARBOXYPEPTIDASE Z - RATTUS NORVEGICUS (RAT).
O54860 CARBOXYPEPTIDASE X2 - MUS MUSCULUS (MOUSE).
O57512 CARBOXYPEPTIDASE D - ANAS PLATYRHYNCHOS (DOMESTIC DUCK).
O75976 GP180-CARBOXYPEPTIDASE D-LIKE ENZYME - HOMO SAPIENS (HUMAN).
O77063 CARBOXYPEPTIDASE D - APLYSIA CALIFORNICA (CALIFORNIA SEA HARE).
O89001 GP180-CARBOXYPEPTIDASE D-LIKE ENZYME - MUS MUSCULUS (MOUSE).
P73902 HYPOTHETICAL 63.9 KD PROTEIN - SYNECHOCYSTIS SP. (STRAIN PCC 6803).
P90667 CARBOXYPEPTIDASE E - APLYSIA CALIFORNICA (CALIFORNIA SEA HARE).
P90668 CARBOXYPEPTIDASE E-3 - APLYSIA CALIFORNICA (CALIFORNIA SEA HARE).
P91359 SIMILARITY TO THE M14 PEPTIDASE FAMILY - CAENORHABDITIS ELEGANS.
P91755 PREPROCARBOXYPEPTIDASE (EC 3.4.-.-) - LUMBRICUS RUBELLUS (HUMUS EARTHWORM).
P92190 CARBOXYPEPTIDASE E-1 - APLYSIA CALIFORNICA (CALIFORNIA SEA HARE).
Q15114 PREPRO-PLASMA CARBOXYPEPTIDASE B - HOMO SAPIENS (HUMAN).
Q19121 F02D8.4 PROTEIN - CAENORHABDITIS ELEGANS.
Q22825 T27A8.1 PROTEIN - CAENORHABDITIS ELEGANS.
Q23099 W01A8.6 PROTEIN - CAENORHABDITIS ELEGANS.
Q23318 ZC434.9 PROTEIN - CAENORHABDITIS ELEGANS.
Q24094 CARBOXYPEPTIDASE PRECURSOR - DROSOPHILA MELANOGASTER (FRUIT FLY).
Q24095 CARBOXYPEPTIDASE SILVER - DROSOPHILA MELANOGASTER (FRUIT FLY).
Q90240 CARBOXYPEPTIDASE GP180 - ANAS SP. (DUCK).
YQGT_BACSU HYPOTHETICAL 43.4 KD PROTEIN IN SODA-COMGA INTERGENIC REGION - BACILLUS SUBTILIS.

O74818 CARBOXYPEPTIDASE PRECURSOR - SCHIZOSACCHAROMYCES POMBE (FISSION YEAST).
YHT2_YEAST HYPOTHETICAL 49.8 KD PROTEIN IN ACT3-YCK1 INTERGENIC REGION PRECURSOR - SACCHAROMYCES CEREVISIAE (BAKER'S YEAST).

ENP1_BACSH GAMMA-D-GLUTAMYL-L-DIAMINO ACID ENDOPEPTIDASE I (EC 3.4.19.11) (GAMMA-D-GLUTAMYL-MESO-DIAMINOPIMELATE PEPTIDASE I) (ENDOPEPTIDASE I) - BACILLUS SPHAERICUS.
O88442 AORTIC CARBOXYPEPTIDASE-LIKE PROTEIN ACLP - MUS MUSCULUS (MOUSE).
Q14113 AEBP1 - HOMO SAPIENS (HUMAN).
Q61281 AE-BINDING PROTEIN 1 (TRANSCRIPTIONAL REPRESSOR AEBP1) - MUS MUSCULUS (MOUSE).
Scan History
OWL29_3    3  150  NSINGLE    
SPTR37_9f 3 450 NSINGLE
Initial Motifs
Motif 1  width=13
Element Seqn Id St Int Rpt
VGRSFEGRELLVI CBPH_HUMAN 79 79 -
IGRSYEGRPIYVL CBPA_BOVIN 148 148 -
IGNTYEGRPIYVL CBP1_HUMAN 148 148 -
IGSSFENRPMNVL CPA2_HUMAN 147 147 -
GGKSYEGREIRGV CBPZ_SIMVI 28 28 -
IGKSVKGRNLWVL CBPM_HUMAN 44 44 -
IGRSYEGRPIYVL NRL_1PCAA 132 132 -
VGKSYQGRDLWML CBPS_STRCP 149 149 -
IGKSYEGRELWAV CBPT_THEVU 133 133 -
IGTTFEGRTIYLL CBPB_CANFA 144 144 -
IGSTVEDNPLYVL CBPC_MOUSE 145 145 -
LGSSFENRPMNVL CBP2_RAT 147 147 -
IGESFEGRELLVL CBPH_LOPAM 57 57 -

Motif 2 width=15
Element Seqn Id St Int Rpt
PAIWLDAGIHAREWV CPA2_HUMAN 168 8 -
PAIWIDSGIHSREWI NRL_1PCAA 154 9 -
PEFKYVANMHGDETV CBPM_HUMAN 70 13 -
PVVMVESNIHAREWI CBPZ_SIMVI 49 8 -
PEFKYIANMHGNEAV CBPH_LOPAM 83 13 -
PEFKYIGNMHGNEAV CBPH_HUMAN 105 13 -
PAIWIDLGIHSREWI CBPA_BOVIN 170 9 -
PAIWIDTGIHSREWV CBP1_HUMAN 170 9 -
PAIWLDAGIHAREWV CBP2_RAT 168 8 -
KAIFMDCGIHAREWI CBPC_MOUSE 167 9 -
PAIFMDCGFHAREWI CBPB_CANFA 166 9 -
PEVLYTALHHAREHL CBPT_THEVU 158 12 -
PEVLFTCNMHAREHL CBPS_STRCP 174 12 -

Motif 3 width=9
Element Seqn Id St Int Rpt
GSDSNRNWD NRL_1PCAA 234 65 -
GVDLNRNFP CBPH_LOPAM 162 64 -
GIDLNRNFP CBPH_HUMAN 184 64 -
GVDANRNWD CBPA_BOVIN 250 65 -
GVDPNRNWD CBP1_HUMAN 250 65 -
GVDPNRNWD CPA2_HUMAN 248 65 -
GVDPNRNWD CBP2_RAT 248 65 -
GTDLNRNFD CBPC_MOUSE 247 65 -
GTDPTRNFD CBPB_CANFA 246 65 -
GTDLNRNYG CBPT_THEVU 240 67 -
GTDPNRNWG CBPS_STRCP 254 65 -
GTDPNRNWN CBPZ_SIMVI 127 63 -
QYDLNRNFP CBPM_HUMAN 145 60 -

Motif 4 width=14
Element Seqn Id St Int Rpt
IILHSYSQLLMFPY CPA2_HUMAN 301 44 -
ITLHSYSQLLMFPY CBP2_RAT 301 44 -
ITFHSYSQMLLIPY CBPC_MOUSE 301 45 -
LTIHSYSQMMLYPY CBPB_CANFA 300 45 -
ITFHTYSELILYPY CBPT_THEVU 299 50 -
IDWHTYSELILWPY CBPS_STRCP 312 49 -
ANLHGGDLVANYPY CBPH_HUMAN 245 52 -
LSIHSYSQLLLYPY CBPA_BOVIN 303 44 -
ANLHGGDVVANYPY CBPH_LOPAM 223 52 -
LAFHSYSQLLLFPY CBPZ_SIMVI 181 45 -
ANLHGGALVASYPF CBPM_HUMAN 183 29 -
ISIHSYSQLLLYPY NRL_1PCAA 287 44 -
ISIHSYSQLLMYPY CBP1_HUMAN 303 44 -
Final Motifs
Motif 1  width=13
Element Seqn Id St Int Rpt
IGSSVEGRPLWVL O89001 90 90 -
IGNSVEGRPLWVL O35850 90 90 -
IGRSVEGRPLWVL O15377 83 83 -
IGRSVEGRPLWVL O75976 85 85 -
IGRSVEGRPLWVL O57512 75 75 -
IGRSVEGRPLWVL Q90240 74 74 -
IGQSVQGRDLWVL O77063 494 494 -
IGKSVQGRDLWVL O46058 482 482 -
IGKSVQGRDLWVL Q24094 482 482 -
IGKSVQGRDLWVL Q24095 480 480 -
IGESFEGRELLVL CBPH_LOPAM 57 57 -
VGRSFEGRELLVL CBPH_BOVIN 37 37 -
IGRSVEGRHLYVL CBPN_HUMAN 51 51 -
VGRSFEGRELLVI CBPH_HUMAN 79 79 -
VGRSFEGRELLVI CBPH_MOUSE 79 79 -
VGRSFEGRELLVI CBPH_RAT 79 79 -
AGKSVEGRELWVL P91359 104 104 -
AGQSVQGRELWVL Q22825 84 84 -
SEPSVEKRNLTVL P90667 74 74 -
SEPSVEKRNLTVL P90668 74 74 -
SEPSVEKRNLTVL P92190 74 74 -
IGQSVEGRPLVVI O17754 66 66 -
IGRSFDGRELLVI O00520 202 202 -
IGRSFEGKDLVVI O54858 216 216 -
IGRSFEGKDLVVI O54859 216 216 -
IGRSYEGRPIYVL CBPA_BOVIN 148 148 -
IGNTFEGRPIHVL CBP1_RAT 148 148 -
IGNTYEGRPIYVL CBP1_HUMAN 148 148 -
IGSSFENRPMNVL CPA2_HUMAN 147 147 -
IGSTVEDNPLYVL CBPC_RAT 37 37 -
IGTTFEGRAIYLL CBPB_HUMAN 145 145 -
LGSSFENRPMNVL CBP2_RAT 147 147 -
IGSTVEDNPLYVL CBPC_HUMAN 145 145 -
IGSTVEDNPLYVL CBPC_MOUSE 145 145 -
IGTTFEGRNMYVL CBPB_RAT 143 143 -
IGTTFLGNTIYLL CBPB_BOVIN 35 35 -
IGSSFEKYPLYVL Q15114 149 149 -
IGTTFEGRTIYLL CBPB_CANFA 144 144 -
IGKSYEGRELWAV CBPT_THEVU 133 133 -
IGTTFDGDNIYLL CBPB_PIG 130 130 -
IGNSYEGRSITAV Q19121 20 20 -
VGLSYEGRTMKLL CBPB_ASTFL 32 32 -
IGKSHQGLKLYAV O54860 352 352 -
VGKSYQGRDLWML CBPS_STRCP 149 149 -
MGTTSEGRPIQGI Q23318 167 167 -
IGQSYAGRDIWVA P73902 37 37 -
IGRTREGRPLLGV Q23099 54 54 -
IGYTVLGRPMQIL P91755 102 102 -
AGRSHQNRTMKGV CBPA_ANOGA 157 157 -
SGTTGDGNTITGL O14418 144 144 -
IGKTYQGRDVIAV CBPS_STRGR 158 158 -
IGRSVLGRPIWEL YQGT_BACSU 108 108 -

Motif 2 width=15
Element Seqn Id St Int Rpt
PEFKYIGNMHGNEVV O89001 554 451 -
PEFKYIGNMHGNEVV O35850 555 452 -
PEFKYIGNMHGNEVV O15377 552 456 -
PEFKYIGNMHGNEVV O75976 555 457 -
PEFKYIGNMHGNEVV O57512 562 474 -
PEFKYIGNMHGNEVV Q90240 564 477 -
PEFKYIGNMHGNEVV O77063 520 13 -
PEFKYVANMHGNEVV O46058 508 13 -
PEFKYVANMHGNEVV Q24094 508 13 -
PEFKYVANMHGNEVV Q24095 506 13 -
PEFKYIANMHGNEAV CBPH_LOPAM 83 13 -
PEFKYIGNMHGNEAV CBPH_BOVIN 63 13 -
PEVKYVGNMHGNEAL CBPN_HUMAN 77 13 -
PEFKYIGNMHGNEAV CBPH_HUMAN 105 13 -
PEFKYIGNMHGNEAV CBPH_MOUSE 105 13 -
PEFKYIGNMHGNEAV CBPH_RAT 105 13 -
PELKIVGNMHGNEVV P91359 130 13 -
PEFKYVANMHGNEVT Q22825 110 13 -
PEFKYVANMHGNEVV P90667 100 13 -
PEFKYVANMHGNEVV P90668 100 13 -
PEFKYVANMHGNEVV P92190 100 13 -
PEVKLIGNMHGNEPI O17754 92 13 -
PEVKLIGNIHGNEVA O00520 228 13 -
PEVKLIGNIHGNEVA O54858 242 13 -
PEVKLIGNIHGNEVA O54859 242 13 -
PAIWIDLGIHSREWI CBPA_BOVIN 170 9 -
PAIWIDTGIHSREWV CBP1_RAT 170 9 -
PAIWIDTGIHSREWV CBP1_HUMAN 170 9 -
PAIWLDAGIHAREWV CPA2_HUMAN 168 8 -
KAIFMDCGIHAREWV CBPC_RAT 59 9 -
PAIFMDCGFHAREWI CBPB_HUMAN 167 9 -
PAIWLDAGIHAREWV CBP2_RAT 168 8 -
KAIFMDCGIHAREWV CBPC_HUMAN 167 9 -
KAIFMDCGIHAREWI CBPC_MOUSE 167 9 -
PAIFIDCGFHAREWI CBPB_RAT 165 9 -
PAVFMDCGFHAREWI CBPB_BOVIN 57 9 -
NAIWIDCGIHAREWI Q15114 172 10 -
PAIFMDCGFHAREWI CBPB_CANFA 166 9 -
PEVLYTALHHAREHL CBPT_THEVU 158 12 -
PAIFMDCGFHAREWI CBPB_PIG 152 9 -
PIVWIDAGIHAREWI Q19121 42 9 -
PIIFIDGGIHAREWI CBPB_ASTFL 54 9 -
PEFHYIAGAHGNEVL O54860 378 13 -
PEVLFTCNMHAREHL CBPS_STRCP 174 12 -
RIFWIDGGIHAREWA Q23318 191 11 -
PGYWIDANTHAGEVT P73902 63 13 -
IAVWLDGGNHAREWP Q23099 79 12 -
WRVWMDAGVHAREWL P91755 124 9 -
PGVFLEGGIHAREWI CBPA_ANOGA 178 8 -
PAVVFHGTVHAREWI O14418 168 11 -
PEVLFTAHQHAREHL CBPS_STRGR 183 12 -
KKVHMNASFHANEWI YQGT_BACSU 129 8 -

Motif 3 width=9
Element Seqn Id St Int Rpt
NFDLNRNFP O89001 629 60 -
NFDLNRNFP O35850 630 60 -
NFDLNRNFP O15377 627 60 -
NFDLNRNFP O75976 630 60 -
NYDLNRNFP O57512 637 60 -
NYDLNRNFP Q90240 639 60 -
LVDLNRNFP O77063 595 60 -
GIDLNRNFP O46058 583 60 -
GIDLNRNFP Q24094 583 60 -
GIDLNRNFP Q24095 581 60 -
GVDLNRNFP CBPH_LOPAM 162 64 -
GIDLNRNFP CBPH_BOVIN 142 64 -
GVDLNRNFP CBPN_HUMAN 156 64 -
GIDLNRNFP CBPH_HUMAN 184 64 -
GIDLNRNFP CBPH_MOUSE 184 64 -
GIDLNRNFP CBPH_RAT 184 64 -
DVDLNRNFP P91359 205 60 -
GKDLNRNFP Q22825 185 60 -
DVDLNRNFP P90667 181 66 -
DVDLNRNFP P90668 181 66 -
DVDLNRNFP P92190 181 66 -
GVDLNRDFP O17754 171 64 -
NLDLNRNFP O00520 307 64 -
NLDLNRNFP O54858 321 64 -
NLDLNRNFP O54859 321 64 -
GVDANRNWD CBPA_BOVIN 250 65 -
GVDPNRNWD CBP1_RAT 250 65 -
GVDPNRNWD CBP1_HUMAN 250 65 -
GVDPNRNWD CPA2_HUMAN 248 65 -
GTDLNRNFD CBPC_RAT 139 65 -
GTDPNRNFD CBPB_HUMAN 247 65 -
GVDPNRNWD CBP2_RAT 248 65 -
GTDLNRNFN CBPC_HUMAN 247 65 -
GTDLNRNFD CBPC_MOUSE 247 65 -
GVRPNRNFN CBPB_RAT 245 65 -
GTDLNRNFD CBPB_BOVIN 137 65 -
GTDLNRNFA Q15114 252 65 -
GTDPTRNFD CBPB_CANFA 246 65 -
GTDLNRNYG CBPT_THEVU 240 67 -
GTDPNRNFN CBPB_PIG 232 65 -
GADANRNYP Q19121 118 61 -
GADPNRNWS CBPB_ASTFL 132 63 -
GIDINNNFP O54860 457 64 -
GTDPNRNWG CBPS_STRCP 254 65 -
GVDLNRNYD Q23318 242 36 -
GLDFNRNYP P73902 215 137 -
GVDLNRNYD Q23099 172 78 -
GVDLNRNFG P91755 204 65 -
GADPNRNWD CBPA_ANOGA 255 62 -
GTDPNRNWP O14418 248 65 -
GTDLNRNWA CBPS_STRGR 265 67 -
GVDLNKQFP YQGT_BACSU 226 82 -

Motif 4 width=14
Element Seqn Id St Int Rpt
ANLHGGSLVVNYPY O89001 667 29 -
ANLHGGSLVVNYPY O35850 668 29 -
ANLHGGSLVVNYPF O15377 665 29 -
ANLHGGSLVVNYPF O75976 668 29 -
ANLHGGSLVVNYPF O57512 675 29 -
ANLHGGSLVVNYPF Q90240 677 29 -
ANLHGGSLVANYPY O77063 635 31 -
ANLHGGSLVANYPF O46058 623 31 -
ANLHGGSLVANYPF Q24094 623 31 -
ANLHGGSLVANYPF Q24095 621 31 -
ANLHGGDVVANYPY CBPH_LOPAM 223 52 -
ANLHGGDLVANYPY CBPH_BOVIN 203 52 -
ANLHGGAVVANYPY CBPN_HUMAN 213 48 -
ANLHGGDLVANYPY CBPH_HUMAN 245 52 -
ANLHGGDLVANYPY CBPH_MOUSE 245 52 -
ANLHGGDLVANYPY CBPH_RAT 245 52 -
TNLHGGSLVANYPY P91359 248 34 -
ANLHGGTTLVNYPF Q22825 225 31 -
SNLHGGDLVANYPY P90667 242 52 -
SNLHGGDLVANYPY P90668 242 52 -
SNLHGGDLVANYPY P92190 242 52 -
ANFHEGDLVANYPF O17754 229 49 -
ASLHGGDLVVSYPF O00520 366 50 -
ASLHGGDLVVSYPF O54858 380 50 -
ASLHGGDLVVSYPF O54859 380 50 -
LSIHSYSQLLLYPY CBPA_BOVIN 303 44 -
ISIHSYSQLLLYPY CBP1_RAT 303 44 -
ISIHSYSQLLMYPY CBP1_HUMAN 303 44 -
IILHSYSQLLMFPY CPA2_HUMAN 301 44 -
ITFHSYSQMLLFPY CBPC_RAT 193 45 -
LTIHSYSQMMIYPY CBPB_HUMAN 301 45 -
ITLHSYSQLLMFPY CBP2_RAT 301 44 -
ITFHSYSQMLLFPY CBPC_HUMAN 301 45 -
ITFHSYSQMLLIPY CBPC_MOUSE 301 45 -
LTIHSYSQMMLYPY CBPB_RAT 299 45 -
LTIHSYSQMMLYPY CBPB_BOVIN 191 45 -
ISMHSYSQHIVFPY Q15114 307 46 -
LTIHSYSQMMLYPY CBPB_CANFA 300 45 -
ITFHTYSELILYPY CBPT_THEVU 299 50 -
LTIHSYSQMILYPY CBPB_PIG 286 45 -
IALHSYGQEILYPW Q19121 172 45 -
LTFHSYSQLWMYPW CBPB_ASTFL 186 45 -
GNLQGGELVVAYPY O54860 522 56 -
IDWHTYSELILWPY CBPS_STRCP 312 49 -
ITLHTYSQMWIHPY Q23318 285 34 -
ISYHTYSAVILRPY P73902 262 38 -
VSMHTHGQLWILPY Q23099 229 48 -
SDWSRGTANINYPY P91755 320 107 -
IAFHSYSQLLLFPY CBPA_ANOGA 309 45 -
IDWHSYSQLFMTPY O14418 304 47 -
IDFHTYSELVLWPF CBPS_STRGR 324 50 -
LALHTQGEEIYWGY YQGT_BACSU 280 45 -