WORKLIST ENTRIES (1):
CRBOXYPTASEA View alignment Carboxypeptidase A metalloprotease (M14) family signature
Type of fingerprint: COMPOUND with 4 elements
Links:
PRINTS; PR00756 ALADIPTASE; PR00791 PEPDIPTASEA; PR00730 THERMOLYSIN
PRINTS; PR00787 NEUTRALPTASE; PR00782 LSHMANOLYSIN; PR00931 MICOLLPTASE
PRINTS; PR00997 FRAGILYSIN; PR00786 NEPRILYSIN; PR00932 AMINO1PTASE
PRINTS; PR00789 OSIALOPTASE; PR00933 BLYTICPTASE; PR00934 XHISDIPTASE
PRINTS; PR00919 THERMOPTASE; PR00998 CRBOXYPTASET; PR00768 DEUTEROLYSIN
PRINTS; PR00999 FUNGALYSIN; PR01000 SREBPS2PTASE
INTERPRO; IPR000834
PROSITE; PS00132 CARBOXYPEPT_ZN_1; PS00133 CARBOXYPEPT_ZN_2
PFAM; PF00246 Zn_carbOpep
PDB; 1PCA 3Dinfo
SCOP; 1PCA
CATH; 1PCA
Creation date 18-JUN-1997; UPDATE 14-JUN-1999
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).
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
11 codes involving 2 elements
COMPOSITE FINGERPRINT INDEX
4| 52 52 52 52
3| 2 2 0 2
2| 1 10 5 6
--+---------------------
| 1 2 3 4
True positives..
O89001 O35850 O15377 O75976
O57512 Q90240 O77063 O46058
Q24094 Q24095 CBPH_LOPAM CBPH_BOVIN
CBPN_HUMAN CBPH_HUMAN CBPH_MOUSE CBPH_RAT
P91359 Q22825 P90667 P90668
P92190 O17754 O00520 O54858
O54859 CBPA_BOVIN CBP1_RAT CBP1_HUMAN
CPA2_HUMAN CBPC_RAT CBPB_HUMAN CBP2_RAT
CBPC_HUMAN CBPC_MOUSE CBPB_RAT CBPB_BOVIN
Q15114 CBPB_CANFA CBPT_THEVU CBPB_PIG
Q19121 CBPB_ASTFL O54860 CBPS_STRCP
Q23318 P73902 Q23099 P91755
CBPA_ANOGA O14418 CBPS_STRGR YQGT_BACSU
Subfamily: Codes involving 3 elements
Subfamily True positives..
YHT2_YEAST O74818
Subfamily: Codes involving 2 elements
Subfamily True positives..
O88442 Q61281 Q14113 ENP1_BACSH
PROTEIN TITLES
O89001 GP180-CARBOXYPEPTIDASE D-LIKE ENZYME - MUS MUSCULUS (MOUSE).
O35850 CARBOXYPEPTIDASE D PRECURSOR - RATTUS NORVEGICUS (RAT).
O15377 CARBOXYPEPTIDASE D PRECURSOR - HOMO SAPIENS (HUMAN).
O75976 GP180-CARBOXYPEPTIDASE D-LIKE ENZYME - HOMO SAPIENS (HUMAN).
O57512 CARBOXYPEPTIDASE D - ANAS PLATYRHYNCHOS (DOMESTIC DUCK).
Q90240 CARBOXYPEPTIDASE GP180 - ANAS SP. (DUCK).
O77063 CARBOXYPEPTIDASE D - APLYSIA CALIFORNICA (CALIFORNIA SEA HAR
O46058 COSMID 171D11 - DROSOPHILA MELANOGASTER (FRUIT FLY).
Q24094 CARBOXYPEPTIDASE PRECURSOR - DROSOPHILA MELANOGASTER (FRUIT
Q24095 CARBOXYPEPTIDASE SILVER - DROSOPHILA MELANOGASTER (FRUIT FLY
CBPH_LOPAM CARBOXYPEPTIDASE H PRECURSOR (EC 3.4.17.10) (CPH) (CARBOXYPE
CBPH_BOVIN CARBOXYPEPTIDASE H (EC 3.4.17.10) (CPH) (CARBOXYPEPTIDASE E)
CBPN_HUMAN CARBOXYPEPTIDASE N CATALYTIC CHAIN PRECURSOR (EC 3.4.17.3) (
CBPH_HUMAN CARBOXYPEPTIDASE H PRECURSOR (EC 3.4.17.10) (CPH) (CARBOXYPE
CBPH_MOUSE CARBOXYPEPTIDASE H PRECURSOR (EC 3.4.17.10) (CPH) (CARBOXYPE
CBPH_RAT CARBOXYPEPTIDASE H PRECURSOR (EC 3.4.17.10) (CPH) (CARBOXYPE
P91359 SIMILARITY TO THE M14 PEPTIDASE FAMILY - CAENORHABDITIS ELEG
Q22825 T27A8.1 PROTEIN - CAENORHABDITIS ELEGANS.
P90667 CARBOXYPEPTIDASE E - APLYSIA CALIFORNICA (CALIFORNIA SEA HAR
P90668 CARBOXYPEPTIDASE E-3 - APLYSIA CALIFORNICA (CALIFORNIA SEA H
P92190 CARBOXYPEPTIDASE E-1 - APLYSIA CALIFORNICA (CALIFORNIA SEA H
O17754 F01D4.4 PROTEIN - CAENORHABDITIS ELEGANS.
O00520 CARBOXYPEPTIDASE Z PRECURSOR - HOMO SAPIENS (HUMAN).
O54858 CARBOXYPEPTIDASE Z - RATTUS NORVEGICUS (RAT).
O54859 CARBOXYPEPTIDASE Z - RATTUS NORVEGICUS (RAT).
CBPA_BOVIN CARBOXYPEPTIDASE A PRECURSOR (EC 3.4.17.1) - BOS TAURUS (BOV
CBP1_RAT CARBOXYPEPTIDASE A1 PRECURSOR (EC 3.4.17.1) - RATTUS NORVEGI
CBP1_HUMAN CARBOXYPEPTIDASE A1 PRECURSOR (EC 3.4.17.1) - HOMO SAPIENS (
CPA2_HUMAN CARBOXYPEPTIDASE A2 PRECURSOR (EC 3.4.17.15) - HOMO SAPIENS
CBPC_RAT MAST CELL CARBOXYPEPTIDASE (EC 3.4.17.1) (RMC-CP) (CARBOXYPE
CBPB_HUMAN CARBOXYPEPTIDASE B PRECURSOR (EC 3.4.17.2) (PANCREAS-SPECIFI
CBP2_RAT CARBOXYPEPTIDASE A2 PRECURSOR (EC 3.4.17.15) - RATTUS NORVEG
CBPC_HUMAN MAST CELL CARBOXYPEPTIDASE A PRECURSOR (EC 3.4.17.1) (MC-CPA
CBPC_MOUSE MAST CELL CARBOXYPEPTIDASE A PRECURSOR (EC 3.4.17.1) (MC-CPA
CBPB_RAT CARBOXYPEPTIDASE B PRECURSOR (EC 3.4.17.2) - RATTUS NORVEGIC
CBPB_BOVIN CARBOXYPEPTIDASE B (EC 3.4.17.2) - BOS TAURUS (BOVINE).
Q15114 PREPRO-PLASMA CARBOXYPEPTIDASE B - HOMO SAPIENS (HUMAN).
CBPB_CANFA CARBOXYPEPTIDASE B PRECURSOR (EC 3.4.17.2) (47 KD ZYMOGEN GR
CBPT_THEVU CARBOXYPEPTIDASE T PRECURSOR (EC 3.4.17.18) - THERMOACTINOMY
CBPB_PIG CARBOXYPEPTIDASE B PRECURSOR (EC 3.4.17.2) - SUS SCROFA (PIG
Q19121 F02D8.4 PROTEIN - CAENORHABDITIS ELEGANS.
CBPB_ASTFL CARBOXYPEPTIDASE B (EC 3.4.17.2) - ASTACUS FLUVIATILIS (BROA
O54860 CARBOXYPEPTIDASE X2 - MUS MUSCULUS (MOUSE).
CBPS_STRCP ZINC-CARBOXYPEPTIDASE PRECURSOR (EC 3.4.17.-) - STREPTOMYCES
Q23318 ZC434.9 PROTEIN - CAENORHABDITIS ELEGANS.
P73902 HYPOTHETICAL 63.9 KD PROTEIN - SYNECHOCYSTIS SP. (STRAIN PCC
Q23099 W01A8.6 PROTEIN - CAENORHABDITIS ELEGANS.
P91755 PREPROCARBOXYPEPTIDASE (EC 3.4.-.-) - LUMBRICUS RUBELLUS (HU
CBPA_ANOGA ZINC CARBOXYPEPTIDASE A PRECURSOR (EC 3.4.17.-) - ANOPHELES
O14418 CARBOXYPEPTIDASE - METARHIZIUM ANISOPLIAE.
CBPS_STRGR ZINC-CARBOXYPEPTIDASE PRECURSOR (EC 3.4.17.-) (CPASE SG) (CP
YQGT_BACSU HYPOTHETICAL 43.4 KD PROTEIN IN SODA-COMGA INTERGENIC REGION
YHT2_YEAST HYPOTHETICAL 49.8 KD PROTEIN IN ACT3-YCK1 INTERGENIC REGION
O74818 CARBOXYPEPTIDASE PRECURSOR - SCHIZOSACCHAROMYCES POMBE (FISS
O88442 AORTIC CARBOXYPEPTIDASE-LIKE PROTEIN ACLP - MUS MUSCULUS (MO
Q61281 AE-BINDING PROTEIN 1 (TRANSCRIPTIONAL REPRESSOR AEBP1) - MUS
Q14113 AEBP1 - HOMO SAPIENS (HUMAN).
ENP1_BACSH GAMMA-D-GLUTAMYL-L-DIAMINO ACID ENDOPEPTIDASE I (EC 3.4.19.1
SCAN HISTORY
OWL29_3 3 150 NSINGLE
SPTR37_9f 3 450 NSINGLE
INITIAL MOTIF SETS
CRBOXYPTASEA1 Length of motif = 13 Motif number = 1
Carboxypeptidase A family motif I - 1
PCODE ST INT
IGRSYEGRPIYVL CBPA_BOVIN 148 148
IGRSYEGRPIYVL NRL_1PCAA 132 132
IGESFEGRELLVL CBPH_LOPAM 57 57
IGNTYEGRPIYVL CBP1_HUMAN 148 148
IGKSYEGRELWAV CBPT_THEVU 133 133
VGRSFEGRELLVI CBPH_HUMAN 79 79
IGKSVKGRNLWVL CBPM_HUMAN 44 44
IGSSFENRPMNVL CPA2_HUMAN 147 147
IGTTFEGRTIYLL CBPB_CANFA 144 144
LGSSFENRPMNVL CBP2_RAT 147 147
GGKSYEGREIRGV CBPZ_SIMVI 28 28
IGSTVEDNPLYVL CBPC_MOUSE 145 145
VGKSYQGRDLWML CBPS_STRCP 149 149
CRBOXYPTASEA2 Length of motif = 15 Motif number = 2
Carboxypeptidase A family motif II - 1
PCODE ST INT
PAIWIDLGIHSREWI CBPA_BOVIN 170 9
PAIWIDSGIHSREWI NRL_1PCAA 154 9
PEFKYIANMHGNEAV CBPH_LOPAM 83 13
PAIWIDTGIHSREWV CBP1_HUMAN 170 9
PEVLYTALHHAREHL CBPT_THEVU 158 12
PEFKYIGNMHGNEAV CBPH_HUMAN 105 13
PEFKYVANMHGDETV CBPM_HUMAN 70 13
PAIWLDAGIHAREWV CPA2_HUMAN 168 8
PAIFMDCGFHAREWI CBPB_CANFA 166 9
PAIWLDAGIHAREWV CBP2_RAT 168 8
PVVMVESNIHAREWI CBPZ_SIMVI 49 8
KAIFMDCGIHAREWI CBPC_MOUSE 167 9
PEVLFTCNMHAREHL CBPS_STRCP 174 12
CRBOXYPTASEA3 Length of motif = 9 Motif number = 3
Carboxypeptidase A family motif III - 1
PCODE ST INT
GVDANRNWD CBPA_BOVIN 250 65
GSDSNRNWD NRL_1PCAA 234 65
GVDLNRNFP CBPH_LOPAM 162 64
GVDPNRNWD CBP1_HUMAN 250 65
GTDLNRNYG CBPT_THEVU 240 67
GIDLNRNFP CBPH_HUMAN 184 64
QYDLNRNFP CBPM_HUMAN 145 60
GVDPNRNWD CPA2_HUMAN 248 65
GTDPTRNFD CBPB_CANFA 246 65
GVDPNRNWD CBP2_RAT 248 65
GTDPNRNWN CBPZ_SIMVI 127 63
GTDLNRNFD CBPC_MOUSE 247 65
GTDPNRNWG CBPS_STRCP 254 65
CRBOXYPTASEA4 Length of motif = 14 Motif number = 4
Carboxypeptidase A family motif IV - 1
PCODE ST INT
LSIHSYSQLLLYPY CBPA_BOVIN 303 44
ISIHSYSQLLLYPY NRL_1PCAA 287 44
ANLHGGDVVANYPY CBPH_LOPAM 223 52
ISIHSYSQLLMYPY CBP1_HUMAN 303 44
ITFHTYSELILYPY CBPT_THEVU 299 50
ANLHGGDLVANYPY CBPH_HUMAN 245 52
ANLHGGALVASYPF CBPM_HUMAN 183 29
IILHSYSQLLMFPY CPA2_HUMAN 301 44
LTIHSYSQMMLYPY CBPB_CANFA 300 45
ITLHSYSQLLMFPY CBP2_RAT 301 44
LAFHSYSQLLLFPY CBPZ_SIMVI 181 45
ITFHSYSQMLLIPY CBPC_MOUSE 301 45
IDWHTYSELILWPY CBPS_STRCP 312 49
FINAL MOTIF SETS
CRBOXYPTASEA1 Length of motif = 13 Motif number = 1
Carboxypeptidase A family motif I - 3
PCODE ST INT
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
CRBOXYPTASEA2 Length of motif = 15 Motif number = 2
Carboxypeptidase A family motif II - 3
PCODE ST INT
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
CRBOXYPTASEA3 Length of motif = 9 Motif number = 3
Carboxypeptidase A family motif III - 3
PCODE ST INT
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
CRBOXYPTASEA4 Length of motif = 14 Motif number = 4
Carboxypeptidase A family motif IV - 3
PCODE ST INT
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
User query: Display/Full Code "CRBOXYPTASEA"