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Conserved domains on  [gi|126920918|gb|AAI33528|]
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CPXM1 protein [Bos taurus]

Protein Classification

carboxypeptidase X family protein( domain architecture ID 10044218)

carboxypeptidase X (CPX) family protein is an M14 family zinc carboxypeptidase that relies on its substrate specificity and subcellular compartmentalization to prevent inappropriate cleavages that would otherwise damage the cell; it contains an extra C-terminal domain which may assist in folding of the carboxypeptidase domain, regulate enzyme activity, or be involved in interactions with other proteins or with membranes

CATH:  3.40.630.10
EC:  3.4.17.-
Gene Ontology:  GO:0006508|GO:0004181|GO:0008270
MEROPS:  M14
PubMed:  7674922|10493853

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
M14_CPX_like cd03869
Peptidase M14 carboxypeptidase subfamily N/E-like; Carboxypeptidase X subgroup; Peptidase ...
295-616 0e+00

Peptidase M14 carboxypeptidase subfamily N/E-like; Carboxypeptidase X subgroup; Peptidase M14-like domain of carboxypeptidase (CP)-like protein X (CPX), CPX forms a distinct subgroup of the N/E subfamily of the M14 family of metallocarboxypeptidases (MCPs). The M14 family are zinc-binding CPs which hydrolyze single, C-terminal amino acids from polypeptide chains, and have a recognition site for the free C-terminal carboxyl group, which is a key determinant of specificity. Proteins belonging to this subgroup include CP-like protein X1 (CPX1), CP-like protein X2 (CPX2), and aortic CP-like protein (ACLP) and its isoform adipocyte enhancer binding protein-1 (AEBP1). AEBP1 is a truncated form of ACLP, which may arise from alternative splicing of the gene. These proteins are inactive towards standard CP substrates because they lack one or more critical active site and substrate-binding residues that are necessary for activity. They may function as binding proteins rather than as active CPs or display catalytic activity toward other substrates. Proteins in this subgroup also contain an N-terminal discoidin domain. The CP domain is important for the function of AEBP1 as a transcriptional repressor. AEBP1 is involved in several biological processes including adipogenesis, macrophage cholesterol homeostasis, and inflammation. In macrophages, AEBP1 promotes the expression of IL-6, TNF-alpha, MCP-1, and iNOS whose expression is tightly regulated by NF-kappaB activity. ACLP, a secreted protein that associates with the extracellular matrix, is essential for abdominal wall development and contributes to dermal wound healing.


:

Pssm-ID: 349441  Cd Length: 322  Bit Score: 641.11  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126920918 295 HHDYKAMRKLMKQVNEQCPNITRIYSIGKSHQGLKLYVMEMSDQPGEHELGEPEVRYVAGMHGNEALGRELLLLLMQFLC 374
Cdd:cd03869    1 HHNYKDMRQLMKVVNEMCPNITRIYNIGKSYQGLKLYAMEISDNPGEHEVGEPEFRYVAGAHGNEVLGRELLLLLMQFLC 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126920918 375 HEFLRGDPRVTRLLTETRIHLLPSMNPDGYETAFRRGSELVGWAEGRWNHQGIDLNHNFADLNTPLWEAEDEGLVPDTVP 454
Cdd:cd03869   81 QEYLAGNPRIRHLVEETRIHLLPSVNPDGYEKAYEAGSELGGWSLGRWTSDGIDINHNFPDLNSLLWEAEDRKWVPRKVP 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126920918 455 NHHLPLPTYYTLPNATVAPETWAVIKWMQRIPFVLSANLHGGELVVSYPFDMTRTPWAARELTPTPDEAVFRWLSTVYAG 534
Cdd:cd03869  161 NHHIPIPEWYLSENATVAPETRAVIAWMEKIPFVLGGNLQGGELVVSYPYDMTRTPWKTQEYTPTPDDHVFRWLAYSYAS 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126920918 535 TNRAMQDPDRRPCHSQDFSLYGSIINGADWHTVPGSMNDFSYLHTNCFEVTVELSCDKFPHENELPQEWENNKDALLTYL 614
Cdd:cd03869  241 THRLMTDASRRPCHTEDFQKEDGTVNGASWHTVAGSMNDFSYLHTNCFELSIYLGCDKFPHESELPEEWENNRESLLVFM 320

                 ..
gi 126920918 615 EQ 616
Cdd:cd03869  321 EQ 322
FA58C cd00057
Coagulation factor 5/8 C-terminal domain, discoidin domain; Cell surface-attached ...
112-269 2.31e-46

Coagulation factor 5/8 C-terminal domain, discoidin domain; Cell surface-attached carbohydrate-binding domain, present in eukaryotes and assumed to have horizontally transferred to eubacterial genomes.


:

Pssm-ID: 238014 [Multi-domain]  Cd Length: 143  Bit Score: 161.37  E-value: 2.31e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126920918 112 PPLGLESLRvSDNQLDASSSQSFGLGPHRGRLNIqsgledgdlfDGAWCAEQQDAEPWLQVDARHPTRFSGIITQGRNSI 191
Cdd:cd00057    1 EPLGMESGL-ADDQITASSSYSSGWEASRARLNS----------DNAWTPAVNDPPQWLQVDLGKTRRVTGIQTQGRKGG 69
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 126920918 192 WRYDWVTSYKVQFSNDSRTWWGSKNRssGMDAVFPANSDPETPVLNLLPEPQVARFIRLLPQTWlqGGASCLRAEILA 269
Cdd:cd00057   70 GSSEWVTSYKVQYSLDGETWTTYKDK--GEEKVFTGNSDGSTPVTNDFPPPIVARYIRILPTTW--NGNISLRLELYG 143
Peptidase_M14NE-CP-C_like cd11308
Peptidase associated domain: C-terminal domain of M14 N/E carboxypeptidase; putative folding, ...
620-696 2.63e-35

Peptidase associated domain: C-terminal domain of M14 N/E carboxypeptidase; putative folding, regulation, or interaction domain; This domain is found C-terminal to the M14 carboxypeptidase (CP) N/E subfamily containing zinc-binding enzymes that hydrolyze single C-terminal amino acids from polypeptide chains, and have a recognition site for the free C-terminal carboxyl group, which is a key determinant of specificity. The N/E subfamily includes enzymatically active members (carboxypeptidase N, E, M, D, and Z), as well as non-active members (carboxypeptidase-like protein 1, -2, aortic CP-like protein, and adipocyte enhancer binding protein-1) which lack the critical active site and substrate-binding residues considered necessary for activity. The active N/E enzymes fulfill a variety of cellular functions, including prohormone processing, regulation of peptide hormone activity, alteration of protein-protein or protein-cell interactions and transcriptional regulation. For M14 CPs, it has been suggested that this domain may assist in folding of the CP domain, regulate enzyme activity, or be involved in interactions with other proteins or with membranes; for carboxypeptidase M, it may interact with the bradykinin 1 receptor at the cell surface. This domain may also be found in other peptidase families.


:

Pssm-ID: 200604 [Multi-domain]  Cd Length: 76  Bit Score: 128.03  E-value: 2.63e-35
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 126920918 620 GIAGVVRDKDTElGIADAVISVDGINHDVTTAWGGDYWRLLTPGDYMVTASAEGYHTVTRSCRVTFEEGPVPCNFRL 696
Cdd:cd11308    1 GIKGFVTDATGN-PIANATISVEGINHDVTTAKDGDYWRLLLPGTYNVTASAPGYQPVTKTVTVPNNFSATVVNFTL 76
 
Name Accession Description Interval E-value
M14_CPX_like cd03869
Peptidase M14 carboxypeptidase subfamily N/E-like; Carboxypeptidase X subgroup; Peptidase ...
295-616 0e+00

Peptidase M14 carboxypeptidase subfamily N/E-like; Carboxypeptidase X subgroup; Peptidase M14-like domain of carboxypeptidase (CP)-like protein X (CPX), CPX forms a distinct subgroup of the N/E subfamily of the M14 family of metallocarboxypeptidases (MCPs). The M14 family are zinc-binding CPs which hydrolyze single, C-terminal amino acids from polypeptide chains, and have a recognition site for the free C-terminal carboxyl group, which is a key determinant of specificity. Proteins belonging to this subgroup include CP-like protein X1 (CPX1), CP-like protein X2 (CPX2), and aortic CP-like protein (ACLP) and its isoform adipocyte enhancer binding protein-1 (AEBP1). AEBP1 is a truncated form of ACLP, which may arise from alternative splicing of the gene. These proteins are inactive towards standard CP substrates because they lack one or more critical active site and substrate-binding residues that are necessary for activity. They may function as binding proteins rather than as active CPs or display catalytic activity toward other substrates. Proteins in this subgroup also contain an N-terminal discoidin domain. The CP domain is important for the function of AEBP1 as a transcriptional repressor. AEBP1 is involved in several biological processes including adipogenesis, macrophage cholesterol homeostasis, and inflammation. In macrophages, AEBP1 promotes the expression of IL-6, TNF-alpha, MCP-1, and iNOS whose expression is tightly regulated by NF-kappaB activity. ACLP, a secreted protein that associates with the extracellular matrix, is essential for abdominal wall development and contributes to dermal wound healing.


Pssm-ID: 349441  Cd Length: 322  Bit Score: 641.11  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126920918 295 HHDYKAMRKLMKQVNEQCPNITRIYSIGKSHQGLKLYVMEMSDQPGEHELGEPEVRYVAGMHGNEALGRELLLLLMQFLC 374
Cdd:cd03869    1 HHNYKDMRQLMKVVNEMCPNITRIYNIGKSYQGLKLYAMEISDNPGEHEVGEPEFRYVAGAHGNEVLGRELLLLLMQFLC 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126920918 375 HEFLRGDPRVTRLLTETRIHLLPSMNPDGYETAFRRGSELVGWAEGRWNHQGIDLNHNFADLNTPLWEAEDEGLVPDTVP 454
Cdd:cd03869   81 QEYLAGNPRIRHLVEETRIHLLPSVNPDGYEKAYEAGSELGGWSLGRWTSDGIDINHNFPDLNSLLWEAEDRKWVPRKVP 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126920918 455 NHHLPLPTYYTLPNATVAPETWAVIKWMQRIPFVLSANLHGGELVVSYPFDMTRTPWAARELTPTPDEAVFRWLSTVYAG 534
Cdd:cd03869  161 NHHIPIPEWYLSENATVAPETRAVIAWMEKIPFVLGGNLQGGELVVSYPYDMTRTPWKTQEYTPTPDDHVFRWLAYSYAS 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126920918 535 TNRAMQDPDRRPCHSQDFSLYGSIINGADWHTVPGSMNDFSYLHTNCFEVTVELSCDKFPHENELPQEWENNKDALLTYL 614
Cdd:cd03869  241 THRLMTDASRRPCHTEDFQKEDGTVNGASWHTVAGSMNDFSYLHTNCFELSIYLGCDKFPHESELPEEWENNRESLLVFM 320

                 ..
gi 126920918 615 EQ 616
Cdd:cd03869  321 EQ 322
Peptidase_M14 pfam00246
Zinc carboxypeptidase;
301-609 2.80e-81

Zinc carboxypeptidase;


Pssm-ID: 459730 [Multi-domain]  Cd Length: 287  Bit Score: 260.31  E-value: 2.80e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126920918  301 MRKLMKQVNEQCPNITRIYSIGKSHQGLKLYVMEMSDQPGEHELGEPEVRYVAGMHGNEALGRELLLLLMQFLCHEFLRg 380
Cdd:pfam00246   1 IEAWLDALAARYPDLVRLVSIGKSVEGRPLKVLKISSGPGEHNPGKPAVFIDGGIHAREWIGPATALYLIHQLLTNYGR- 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126920918  381 DPRVTRLLTETRIHLLPSMNPDGYETAFrrgSELVGWAEGRWNHQ-----GIDLNHNFADlntpLWeaedeglvpDTVPN 455
Cdd:pfam00246  80 DPEITELLDDTDIYILPVVNPDGYEYTH---TTDRLWRKNRSNANgssciGVDLNRNFPD----HW---------NEVGA 143
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126920918  456 HHLPLPTYYTLPNATVAPETWAVIKWMQR-IPFVLSANLHGGELVVSYPFDMTRTpwaarelTPTPDEAVFRWLSTVYAG 534
Cdd:pfam00246 144 SSNPCSETYRGPAPFSEPETRAVADFIRSkKPFVLYISLHSYSQVLLYPYGYTRD-------EPPPDDEELKSLARAAAK 216
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126920918  535 TNRAMqdpdrrpCHSQDFSlYGsIINGADWHTVPGSMNDFSYLHTNC-FEVTVELSCDK----FPHENELPQEWENNKDA 609
Cdd:pfam00246 217 ALQKM-------VRGTSYT-YG-ITNGATIYPASGGSDDWAYGRLGIkYSYTIELRDTGrygfLLPASQIIPTAEETWEA 287
Zn_pept smart00631
Zn_pept domain;
295-602 1.47e-66

Zn_pept domain;


Pssm-ID: 214748 [Multi-domain]  Cd Length: 277  Bit Score: 221.06  E-value: 1.47e-66
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126920918   295 HHDYKAMRKLMKQVNEQCPNITRIYSIGKSHQGLKLYVMEMSDQPGEhelGEPEVRYVAGMHGNEALGRELLLLLMQFLC 374
Cdd:smart00631   1 YHSYEEIEAWLKELAARYPDLVRLVSIGKSVEGRPIWVLKISNGGSH---DKPAIFIDAGIHAREWIGPATALYLINQLL 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126920918   375 HEFLRgDPRVTRLLTETRIHLLPSMNPDGYEtaFRRGSElVGWAEGRWNHQ---GIDLNHNFADlntpLWEAedeglvpd 451
Cdd:smart00631  78 ENYGR-DPRVTNLLDKTDIYIVPVLNPDGYE--YTHTGD-RLWRKNRSPNSncrGVDLNRNFPF----HWGE-------- 141
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126920918   452 tvpnHHLPLPTYYTLPNATVAPETWAVIKWM-QRIPFVLSANLHGGELVVSYPFDMTRTpwaarELTPTPDE--AVFRWL 528
Cdd:smart00631 142 ----TGNPCSETYAGPSPFSEPETKAVRDFIrSNRRFKLYIDLHSYSQLILYPYGYTKN-----DLPPNVDDldAVAKAL 212
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126920918   529 STVYAgtnramqdpdrrpchsqdfSLYGS-----IINGADWHtVPGSMNDFSYLHTN-CFEVTVELSCD-----KFPHEN 597
Cdd:smart00631 213 AKALA-------------------SVHGTrytygISNGAIYP-ASGGSDDWAYGVLGiPFSFTLELRDDgrygfLLPPSQ 272

                   ....*
gi 126920918   598 ELPQE 602
Cdd:smart00631 273 IIPTG 277
FA58C cd00057
Coagulation factor 5/8 C-terminal domain, discoidin domain; Cell surface-attached ...
112-269 2.31e-46

Coagulation factor 5/8 C-terminal domain, discoidin domain; Cell surface-attached carbohydrate-binding domain, present in eukaryotes and assumed to have horizontally transferred to eubacterial genomes.


Pssm-ID: 238014 [Multi-domain]  Cd Length: 143  Bit Score: 161.37  E-value: 2.31e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126920918 112 PPLGLESLRvSDNQLDASSSQSFGLGPHRGRLNIqsgledgdlfDGAWCAEQQDAEPWLQVDARHPTRFSGIITQGRNSI 191
Cdd:cd00057    1 EPLGMESGL-ADDQITASSSYSSGWEASRARLNS----------DNAWTPAVNDPPQWLQVDLGKTRRVTGIQTQGRKGG 69
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 126920918 192 WRYDWVTSYKVQFSNDSRTWWGSKNRssGMDAVFPANSDPETPVLNLLPEPQVARFIRLLPQTWlqGGASCLRAEILA 269
Cdd:cd00057   70 GSSEWVTSYKVQYSLDGETWTTYKDK--GEEKVFTGNSDGSTPVTNDFPPPIVARYIRILPTTW--NGNISLRLELYG 143
Peptidase_M14NE-CP-C_like cd11308
Peptidase associated domain: C-terminal domain of M14 N/E carboxypeptidase; putative folding, ...
620-696 2.63e-35

Peptidase associated domain: C-terminal domain of M14 N/E carboxypeptidase; putative folding, regulation, or interaction domain; This domain is found C-terminal to the M14 carboxypeptidase (CP) N/E subfamily containing zinc-binding enzymes that hydrolyze single C-terminal amino acids from polypeptide chains, and have a recognition site for the free C-terminal carboxyl group, which is a key determinant of specificity. The N/E subfamily includes enzymatically active members (carboxypeptidase N, E, M, D, and Z), as well as non-active members (carboxypeptidase-like protein 1, -2, aortic CP-like protein, and adipocyte enhancer binding protein-1) which lack the critical active site and substrate-binding residues considered necessary for activity. The active N/E enzymes fulfill a variety of cellular functions, including prohormone processing, regulation of peptide hormone activity, alteration of protein-protein or protein-cell interactions and transcriptional regulation. For M14 CPs, it has been suggested that this domain may assist in folding of the CP domain, regulate enzyme activity, or be involved in interactions with other proteins or with membranes; for carboxypeptidase M, it may interact with the bradykinin 1 receptor at the cell surface. This domain may also be found in other peptidase families.


Pssm-ID: 200604 [Multi-domain]  Cd Length: 76  Bit Score: 128.03  E-value: 2.63e-35
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 126920918 620 GIAGVVRDKDTElGIADAVISVDGINHDVTTAWGGDYWRLLTPGDYMVTASAEGYHTVTRSCRVTFEEGPVPCNFRL 696
Cdd:cd11308    1 GIKGFVTDATGN-PIANATISVEGINHDVTTAKDGDYWRLLLPGTYNVTASAPGYQPVTKTVTVPNNFSATVVNFTL 76
F5_F8_type_C pfam00754
F5/8 type C domain; This domain is also known as the discoidin (DS) domain family.
129-267 9.40e-31

F5/8 type C domain; This domain is also known as the discoidin (DS) domain family.


Pssm-ID: 459925 [Multi-domain]  Cd Length: 127  Bit Score: 117.16  E-value: 9.40e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126920918  129 SSSQSFGLGPHRGRLniqsgleDGDLfDGAWCAEQQDAEPWLQVDARHPTRFSGIITQGRNSIWRYdWVTSYKVQFSNDS 208
Cdd:pfam00754   4 ASSSYSGEGPAAAAL-------DGDP-NTAWSAWSGDDPQWIQVDLGKPKKITGVVTQGRQDGSNG-YVTSYKIEYSLDG 74
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 126920918  209 RTWwgsknrSSGMDAVFPANSDPETPVLNLLPEPQVARFIRLLPQTWLQGGASCLRAEI 267
Cdd:pfam00754  75 ENW------TTVKDEKIPGNNDNNTPVTNTFDPPIKARYVRIVPTSWNGGNGIALRAEL 127
FA58C smart00231
Coagulation factor 5/8 C-terminal domain, discoidin domain; Cell surface-attached ...
113-270 1.92e-30

Coagulation factor 5/8 C-terminal domain, discoidin domain; Cell surface-attached carbohydrate-binding domain, present in eukaryotes and assumed to have horizontally transferred to eubacterial genomes.


Pssm-ID: 214572  Cd Length: 139  Bit Score: 116.45  E-value: 1.92e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126920918   113 PLGLESlrvsDNQLDASSSqsfGLGPHRGRLNIQSgledgdlfDGAWCAEQQDAEPWLQVDARHPTRFSGIITQGRNSiw 192
Cdd:smart00231   5 PLGLES----DSQITASSS---YWAAKIARLNGGS--------DGGWCPAKNDLPPWIQVDLGRLRTVTGVITGRRHG-- 67
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 126920918   193 rYDWVTSYKVQFSNDSRTWWGSKNrssGMDAVFPANSDPETPVLNLLPEPQVARFIRLLPQTWlqGGASCLRAEILAC 270
Cdd:smart00231  68 -NGDWVTYKLEYSDDGVNWTTYKD---GNSKVFPGNSDAGTVVLNDFPPPIVARYVRILPTGW--NGNIILRVELLGC 139
MpaA COG2866
Murein tripeptide amidase MpaA [Cell wall/membrane/envelope biogenesis];
294-527 7.01e-29

Murein tripeptide amidase MpaA [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442113 [Multi-domain]  Cd Length: 337  Bit Score: 118.25  E-value: 7.01e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126920918 294 RHHDYKAMRKLMKQVnEQCPNITRIYSIGKSHQGLKLYVMEMSDQPGehelGEPEVRYVAGMHGNEALGRELllllMQFL 373
Cdd:COG2866   18 RYYTYEELLALLAKL-AAASPLVELESIGKSVEGRPIYLLKIGDPAE----GKPKVLLNAQQHGNEWTGTEA----LLGL 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126920918 374 CHEFLRG-DPRVTRLLTETRIHLLPSMNPDGYETAFRRgselvgwaegrwNHQGIDLNHNFADlntpLWEAEdeglvpdt 452
Cdd:COG2866   89 LEDLLDNyDPLIRALLDNVTLYIVPMLNPDGAERNTRT------------NANGVDLNRDWPA----PWLSE-------- 144
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 126920918 453 vpnhhlplptyytlpnatvaPETWAVIKWMQRIPFVLSANLHGGELVVSYPFDMTRTPWAarELTPTPDEAVFRW 527
Cdd:COG2866  145 --------------------PETRALRDLLDEHDPDFVLDLHGQGELFYWFVGTTEPTGS--FLAPSYDEEREAF 197
CarboxypepD_reg pfam13620
Carboxypeptidase regulatory-like domain;
620-696 5.29e-11

Carboxypeptidase regulatory-like domain;


Pssm-ID: 433354 [Multi-domain]  Cd Length: 81  Bit Score: 59.22  E-value: 5.29e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126920918  620 GIAGVVRDKDTElGIADAVISV----DGINHDVTTAWGGDYW-RLLTPGDYMVTASAEGYHTVTRScRVTFEEG-PVPCN 693
Cdd:pfam13620   1 TISGTVTDPSGA-PVPGATVTVtntdTGTVRTTTTDADGRYRfPGLPPGTYTVTVSAPGFKTATRT-GVTVTAGqTTTLD 78

                  ...
gi 126920918  694 FRL 696
Cdd:pfam13620  79 VTL 81
 
Name Accession Description Interval E-value
M14_CPX_like cd03869
Peptidase M14 carboxypeptidase subfamily N/E-like; Carboxypeptidase X subgroup; Peptidase ...
295-616 0e+00

Peptidase M14 carboxypeptidase subfamily N/E-like; Carboxypeptidase X subgroup; Peptidase M14-like domain of carboxypeptidase (CP)-like protein X (CPX), CPX forms a distinct subgroup of the N/E subfamily of the M14 family of metallocarboxypeptidases (MCPs). The M14 family are zinc-binding CPs which hydrolyze single, C-terminal amino acids from polypeptide chains, and have a recognition site for the free C-terminal carboxyl group, which is a key determinant of specificity. Proteins belonging to this subgroup include CP-like protein X1 (CPX1), CP-like protein X2 (CPX2), and aortic CP-like protein (ACLP) and its isoform adipocyte enhancer binding protein-1 (AEBP1). AEBP1 is a truncated form of ACLP, which may arise from alternative splicing of the gene. These proteins are inactive towards standard CP substrates because they lack one or more critical active site and substrate-binding residues that are necessary for activity. They may function as binding proteins rather than as active CPs or display catalytic activity toward other substrates. Proteins in this subgroup also contain an N-terminal discoidin domain. The CP domain is important for the function of AEBP1 as a transcriptional repressor. AEBP1 is involved in several biological processes including adipogenesis, macrophage cholesterol homeostasis, and inflammation. In macrophages, AEBP1 promotes the expression of IL-6, TNF-alpha, MCP-1, and iNOS whose expression is tightly regulated by NF-kappaB activity. ACLP, a secreted protein that associates with the extracellular matrix, is essential for abdominal wall development and contributes to dermal wound healing.


Pssm-ID: 349441  Cd Length: 322  Bit Score: 641.11  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126920918 295 HHDYKAMRKLMKQVNEQCPNITRIYSIGKSHQGLKLYVMEMSDQPGEHELGEPEVRYVAGMHGNEALGRELLLLLMQFLC 374
Cdd:cd03869    1 HHNYKDMRQLMKVVNEMCPNITRIYNIGKSYQGLKLYAMEISDNPGEHEVGEPEFRYVAGAHGNEVLGRELLLLLMQFLC 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126920918 375 HEFLRGDPRVTRLLTETRIHLLPSMNPDGYETAFRRGSELVGWAEGRWNHQGIDLNHNFADLNTPLWEAEDEGLVPDTVP 454
Cdd:cd03869   81 QEYLAGNPRIRHLVEETRIHLLPSVNPDGYEKAYEAGSELGGWSLGRWTSDGIDINHNFPDLNSLLWEAEDRKWVPRKVP 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126920918 455 NHHLPLPTYYTLPNATVAPETWAVIKWMQRIPFVLSANLHGGELVVSYPFDMTRTPWAARELTPTPDEAVFRWLSTVYAG 534
Cdd:cd03869  161 NHHIPIPEWYLSENATVAPETRAVIAWMEKIPFVLGGNLQGGELVVSYPYDMTRTPWKTQEYTPTPDDHVFRWLAYSYAS 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126920918 535 TNRAMQDPDRRPCHSQDFSLYGSIINGADWHTVPGSMNDFSYLHTNCFEVTVELSCDKFPHENELPQEWENNKDALLTYL 614
Cdd:cd03869  241 THRLMTDASRRPCHTEDFQKEDGTVNGASWHTVAGSMNDFSYLHTNCFELSIYLGCDKFPHESELPEEWENNRESLLVFM 320

                 ..
gi 126920918 615 EQ 616
Cdd:cd03869  321 EQ 322
M14_CP_N-E_like cd03858
Peptidase M14 carboxypeptidase subfamily N/E-like; Carboxypeptidase (CP) N/E-like subfamily of ...
295-616 4.44e-152

Peptidase M14 carboxypeptidase subfamily N/E-like; Carboxypeptidase (CP) N/E-like subfamily of the M14 family of metallocarboxypeptidases (MCPs). The M14 family are zinc-binding CPs which hydrolyze single, C-terminal amino acids from polypeptide chains, and have a recognition site for the free C-terminal carboxyl group, which is a key determinant of specificity. The N/E subfamily includes eight members, of which five (CPN, CPE, CPM, CPD, CPZ) are considered enzymatically active, while the other three are non-active (CPX1, PCX2, ACLP/AEBP1) and lack the critical active site and substrate-binding residues considered necessary for CP activity. These non-active members may function as binding proteins or display catalytic activity towards other substrates. Unlike the A/B CP subfamily, enzymes belonging to the N/E subfamily are not produced as inactive precursors that require proteolysis to produce the active form; rather, they rely on their substrate specificity and subcellular compartmentalization to prevent inappropriate cleavages that would otherwise damage the cell. In addition, all members of the N/E subfamily contain an extra C-terminal domain that is not present in the A/B subfamily. This domain has structural homology to transthyretin and other proteins and has been proposed to function as a folding domain. The active N/E enzymes fulfill a variety of cellular functions, including prohormone processing, regulation of peptide hormone activity, alteration of protein-protein or protein-cell interactions and transcriptional regulation.


Pssm-ID: 349431 [Multi-domain]  Cd Length: 292  Bit Score: 443.63  E-value: 4.44e-152
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126920918 295 HHDYKAMRKLMKQVNEQCPNITRIYSIGKSHQGLKLYVMEMSDQPGEHELGEPEVRYVAGMHGNEALGRELLLLLMQFLC 374
Cdd:cd03858    1 HHNYEELEEFLKQVAKRYPNITRLYSIGKSVEGRELWVLEISDNPGVHEPGEPEFKYVANMHGNEVVGRELLLLLAEYLC 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126920918 375 HEFlRGDPRVTRLLTETRIHLLPSMNPDGYETAfrrGSELVGWAEGRWNHQGIDLNHNFADLNTPLWeaedeglvpdtvp 454
Cdd:cd03858   81 ENY-GKDPRVTQLVNSTRIHIMPSMNPDGYEKA---QEGDCGGLIGRNNANGVDLNRNFPDQFFQVY------------- 143
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126920918 455 nhhlplptyytLPNATVAPETWAVIKWMQRIPFVLSANLHGGELVVSYPFDMTRTPwAARELTPTPDEAVFRWLSTVYAG 534
Cdd:cd03858  144 -----------SDNNPRQPETKAVMNWLESIPFVLSANLHGGALVANYPYDDTRSG-KSTEYSPSPDDAVFRMLARSYSD 211
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126920918 535 TNRAMQDPDRRPCHSqDFSLYGSIINGADWHTVPGSMNDFSYLHTNCFEVTVELSCDKFPHENELPQEWENNKDALLTYL 614
Cdd:cd03858  212 AHPTMSMGKPCCCDD-DENFPNGITNGAAWYSVSGGMQDFNYLHTNCFEITLELGCCKYPPASELPKYWEDNKRSLLNFL 290

                 ..
gi 126920918 615 EQ 616
Cdd:cd03858  291 EQ 292
M14_CPZ cd03867
Peptidase M14 carboxypeptidase subfamily N/E-like; Carboxypeptidase Z subgroup; Peptidase ...
295-615 4.17e-127

Peptidase M14 carboxypeptidase subfamily N/E-like; Carboxypeptidase Z subgroup; Peptidase M14-like domain of carboxypeptidase (CP) Z (CPZ), CPZ belongs to the N/E subfamily of the M14 family of metallocarboxypeptidases (MCPs). The M14 family are zinc-binding CPs which hydrolyze single, C-terminal amino acids from polypeptide chains, and have a recognition site for the free C-terminal carboxyl group, which is a key determinant of specificity. CPZ is a secreted Zn-dependent enzyme whose biological function is largely unknown. Unlike other members of the N/E subfamily, CPZ has a bipartite structure, which consists of an N-terminal cysteine-rich domain (CRD) whose sequence is similar to Wnt-binding proteins, and a C-terminal CP catalytic domain that removes C-terminal Arg residues from substrates. CPZ is enriched in the extracellular matrix and is widely distributed during early embryogenesis. That the CRD of CPZ can bind to Wnt4 suggests that CPZ plays a role in Wnt signaling.


Pssm-ID: 349439  Cd Length: 315  Bit Score: 380.39  E-value: 4.17e-127
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126920918 295 HHDYKAMRKLMKQVNEQCPNITRIYSIGKSHQGLKLYVMEMSDQPGEHELGEPEVRYVAGMHGNEALGRELLLLLMQFLC 374
Cdd:cd03867    1 HHSYSQMVRVLKKTAARCAHIARTYSIGRSFEGKDLLVIEFSSNPGQHELLEPEVKYIGNMHGNEVVGREMLIYLAQYLC 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126920918 375 HEFLRGDPRVTRLLTETRIHLLPSMNPDGYETAFRRGSELVGWAEGRWNHQGIDLNHNFADLNTPLWE-AEDEGLVPDtv 453
Cdd:cd03867   81 SEYLLGNPRIQTLINTTRIHLLPSMNPDGYEVAAEEGAGYNGWTSGRQNAQNLDLNRNFPDLTSEAYRlARTRGARLD-- 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126920918 454 pnhHLPLPTYYTLpnATVAPETWAVIKWMQRIPFVLSANLHGGELVVSYPFDMTRTPWAARELTPTPDEAVFRWLSTVYA 533
Cdd:cd03867  159 ---HIPIPQSYWW--GKVAPETKAVMKWMRSIPFVLSASLHGGDLVVSYPYDFSKHPLEEKMFSPTPDEKMFKLLAKAYA 233
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126920918 534 GTNRAMQDPDRRPChSQDFSLYGSIINGADWHTVPGSMNDFSYLHTNCFEVTVELSCDKFPHENELPQEWENNKDALLTY 613
Cdd:cd03867  234 DAHPMMSDRSENRC-GGNFLKRGGIINGAEWYSFTGGMADFNYLHTNCFEVTVELGCEKFPPEEELYTIWQENKEALLNF 312

                 ..
gi 126920918 614 LE 615
Cdd:cd03867  313 ME 314
M14_CPE cd03865
Peptidase M14 carboxypeptidase subfamily N/E-like; Carboxypeptidase E subgroup; Peptidase M14 ...
295-616 1.57e-122

Peptidase M14 carboxypeptidase subfamily N/E-like; Carboxypeptidase E subgroup; Peptidase M14 Carboxypeptidase (CP) E (CPE, also known as carboxypeptidase H, and enkephalin convertase; EC 3.4.17.10) belongs to the N/E subfamily of the M14 family of metallocarboxypeptidases (MCPs).The M14 family are zinc-binding CPs which hydrolyze single, C-terminal amino acids from polypeptide chains, and have a recognition site for the free C-terminal carboxyl group, which is a key determinant of specificity. CPE is an important enzyme responsible for the proteolytic processing of prohormone intermediates (such as pro-insulin, pro-opiomelanocortin, or pro-gonadotropin-releasing hormone) by specifically removing C-terminal basic residues. In addition, it has been proposed that the regulated secretory pathway (RSP) of the nervous and endocrine systems utilizes membrane-bound CPE as a sorting receptor. A naturally occurring point mutation in CPE reduces the stability of the enzyme and causes its degradation, leading to an accumulation of numerous neuroendocrine peptides that result in obesity and hyperglycemia. Reduced CPE enzyme and receptor activity could underlie abnormal placental phenotypes from the observation that CPE is down-regulated in enlarged placentas of interspecific hybrid (interspecies hybrid placental dysplasia, IHPD) and cloned mice.


Pssm-ID: 349437 [Multi-domain]  Cd Length: 319  Bit Score: 368.93  E-value: 1.57e-122
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126920918 295 HHDYKAMRKLMKQVNEQCPNITRIYSIGKSHQGLKLYVMEMSDQPGEHELGEPEVRYVAGMHGNEALGRELLLLLMQFLC 374
Cdd:cd03865    1 YHRYPELREALVSVWLQCPAISRIYTVGRSFEGRELLVIEVSDNPGEHEPGEPEFKYVGNMHGNEAVGRELLIFLAQYLC 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126920918 375 HEFLRGDPRVTRLLTETRIHLLPSMNPDGYETAFRRGSELVGWAEGRWNHQGIDLNHNFADLNTPLWEAEDEGlvpdtVP 454
Cdd:cd03865   81 NEYQKGNETIINLIHSTRIHIMPSLNPDGFEKAASQPGELKDWFVGRSNAQGIDLNRNFPDLDRIVYVNEKEG-----GP 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126920918 455 NHHLPLPTYYTL-PNATVAPETWAVIKWMQRIPFVLSANLHGGELVVSYPFDMTRTPwAARELTPTPDEAVFRWLSTVYA 533
Cdd:cd03865  156 NNHLLKNMKKAVdQNTKLAPETKAVIHWIMDIPFVLSANLHGGDLVANYPYDETRSG-SAHEYSSCPDDAIFQSLARAYS 234
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126920918 534 GTNRAMQDPDRRPC--HSQDFSLYGSIINGADWHTVPGSMNDFSYLHTNCFEVTVELSCDKFPHENELPQEWENNKDALL 611
Cdd:cd03865  235 SLNPAMSDPNRPPCrkNDDDSSFVDGTTNGGAWYSVPGGMQDFNYLSSNCFEITVELSCEKFPPEETLKGYWEDNKNSLI 314

                 ....*
gi 126920918 612 TYLEQ 616
Cdd:cd03865  315 NYIEQ 319
M14_CPN cd03864
Peptidase M14 carboxypeptidase subfamily N/E-like; Carboxypeptidase N subgroup; Peptidase M14 ...
295-616 2.06e-121

Peptidase M14 carboxypeptidase subfamily N/E-like; Carboxypeptidase N subgroup; Peptidase M14 Carboxypeptidase N (CPN, also known as kininase I, creatine kinase conversion factor, plasma carboxypeptidase B, arginine carboxypeptidase, and protaminase; EC 3.4.17.3) is an extracellular glycoprotein synthesized in the liver and released into the blood, where it is present in high concentrations. CPN belongs to the N/E subfamily of the M14 family of metallocarboxypeptidases (MCPs).The M14 family are zinc-binding carboxypeptidases (CPs) which hydrolyze single, C-terminal amino acids from polypeptide chains, and have a recognition site for the free C-terminal carboxyl group, which is a key determinant of specificity. CPN plays an important role in protecting the body from excessive buildup of potentially deleterious peptides that normally act as local autocrine or paracrine hormones. It specifically removes C-terminal basic residues. As CPN can cleave lysine more avidly than arginine residues it is also called lysine carboxypeptidase. CPN substrates include peptides found in the bloodstream, such as kinins (e.g. bradykinin, kalinin, met-lys-bradykinin), complement anaphylatoxins and creatine kinase MM (CK-MM). By removing just one amino acid, CPN can alter peptide activity and receptor binding. For example Bradykinin, a nine-residue peptide released from kiningen in response to tissue injury which is inactivated by CPN, anaphylatoxins which are regulated by CPN by the cleaving and removal of their C-terminal arginines resulting in a reduction in their biological activities of 10-100-fold, and creatine kinase MM, a cytosolic enzyme that catalyzes the reversible transfer of a phosphate group from ATP to creatine, and is regulated by CPN by the cleavage of C-terminal lysines. Like the other N/E subfamily members, two surface loops surrounding the active-site groove restrict access to the catalytic center, thus restricting larger protein carboxypeptidase inhibitors from inhibiting CPN.


Pssm-ID: 349436 [Multi-domain]  Cd Length: 313  Bit Score: 365.79  E-value: 2.06e-121
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126920918 295 HHDYKAMRKLMKQVNEQCPNITRIYSIGKSHQGLKLYVMEMSDQPGEHELGEPEVRYVAGMHGNEALGRELLLLLMQFLC 374
Cdd:cd03864    1 HHRYDDLVRALYAVQNECPYITRIYSIGRSVEGRHLYVLEFSDNPGIHEPLEPEFKYVGNMHGNEVLGRELLIQLSEFLC 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126920918 375 HEFLRGDPRVTRLLTETRIHLLPSMNPDGYETAFRRGSELVGWAEGRWNHQGIDLNHNFADLNTPLWEAEDEGlvpdtVP 454
Cdd:cd03864   81 EEYRNGNERITRLIQDTRIHILPSMNPDGYEVAARQGPEFNGYLVGRNNANGVDLNRNFPDLNTLMYYNEKYG-----GP 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126920918 455 NHHLPLPTYYtlpNATVAPETWAVIKWMQRIPFVLSANLHGGELVVSYPFDMTRTP----WAARELTPTPDEAVFRWLST 530
Cdd:cd03864  156 NHHLPLPDNW---KSQVEPETLAVIQWMQNYNFVLSANLHGGAVVANYPYDKSREPrvrgFRRTAYSPTPDDKLFQKLAK 232
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126920918 531 VYAGTNRAMQdpdrRPCHSQDFSLYGsIINGADWHTVPGSMNDFSYLHTNCFEVTVELSCDKFPHENELPQEWENNKDAL 610
Cdd:cd03864  233 TYSYAHGWMH----KGWNCGDYFDEG-ITNGASWYSLSKGMQDFNYLHTNCFEITLELSCDKFPPEEELEREWLGNREAL 307

                 ....*.
gi 126920918 611 LTYLEQ 616
Cdd:cd03864  308 ISYMEQ 313
M14_CPD_I cd03868
Peptidase M14 carboxypeptidase subfamily N/E-like; Carboxypeptidase D, domain I subgroup; The ...
296-616 7.36e-113

Peptidase M14 carboxypeptidase subfamily N/E-like; Carboxypeptidase D, domain I subgroup; The first carboxypeptidase (CP)-like domain of Carboxypeptidase D (CPD; EC 3.4.17.22), domain I. CPD differs from all other metallocarboxypeptidases in that it contains multiple CP-like domains. CPD belongs to the N/E-like subfamily of the M14 family of metallocarboxypeptidases (MCPs).The M14 family are zinc-binding CPs which hydrolyze single, C-terminal amino acids from polypeptide chains, and have a recognition site for the free C-terminal carboxyl group, which is a key determinant of specificity. CPD is a single-chain protein containing a signal peptide, three tandem repeats of CP-like domains separated by short bridge regions, followed by a transmembrane domain, and a C-terminal cytosolic tail. The first two CP-like domains of CPD contain all of the essential active site and substrate-binding residues, the third CP-like domain lacks critical residues necessary for enzymatic activity and is inactive towards standard CP substrates. Domain I is optimally active at pH 6.3-7.5 and prefers substrates with C-terminal Arg, whereas domain II is active at pH 5.0-6.5 and prefers substrates with C-terminal Lys. This Domain I family contains two contiguous surface cysteines that may become palmitoylated and target the enzyme to membranes, thus regulating intracellular trafficking. CPD functions in the processing of proteins that transit the secretory pathway, and is present in all vertebrates as well as Drosophila. It is broadly distributed in all tissue types. Within cells, CPD is present in the trans Golgi network and immature secretory vesicles, but is excluded from mature vesicles. It is thought to play a role in the processing of proteins that are initially processed by furin or related endopeptidases present in the trans Golgi network, such as growth factors and receptors. CPD is implicated in the pathogenesis of lupus erythematosus (LE), it is regulated by TGF-beta in various cell types of murine and human origin and is significantly down-regulated in CD14 positive cells isolated from patients with LE. As down-regulation of CPD leads to down-modulation of TGF-beta, CPD may have a role in a positive feedback loop. In D. melanogaster, the CPD variant 1B short (DmCPD1Bs) is necessary and sufficient for viability of the fruit fly.


Pssm-ID: 349440  Cd Length: 294  Bit Score: 343.07  E-value: 7.36e-113
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126920918 296 HDYKAMRKLMKQVNEQCPNITRIYSIGKSHQGLKLYVMEMSDQPGEHELGEPEVRYVAGMHGNEALGRELLLLLMQFLCH 375
Cdd:cd03868    2 HNYDELTDLLHKLAETYPNIAKLHSIGKSVQGRELWVLEISDNVNRREPGKPMFKYVANMHGDETVGRQLLIYLAQYLLE 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126920918 376 EFLRgDPRVTRLLTETRIHLLPSMNPDGYETAfRRGS-ELVGWAEGRWNHQGIDLNHNFADlntplweaEDEGLVPDTVP 454
Cdd:cd03868   82 NYGK-DERVTRLVNSTDIHLMPSMNPDGFENS-KEGDcSGDPGYGGRENANNVDLNRNFPD--------QFEDSDDRLLE 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126920918 455 NHhlplptyytlpnatvAPETWAVIKWMQRIPFVLSANLHGGELVVSYPFDMTRTPWAARELTPTPDEAVFRWLSTVYAG 534
Cdd:cd03868  152 GR---------------QPETLAMMKWIVENPFVLSANLHGGSVVASYPFDDSPSHIECGVYSKSPDDAVFRHLAHTYAD 216
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126920918 535 TNRAMqdPDRRPCHSQDFSlyGSIINGADWHTVPGSMNDFSYLHTNCFEVTVELSCDKFPHENELPQEWENNKDALLTYL 614
Cdd:cd03868  217 NHPTM--HKGNNCCEDSFK--DGITNGAEWYDVPGGMQDFNYVHSNCFEITLELSCCKYPPASELPKEWDNNKEALLSYM 292

                 ..
gi 126920918 615 EQ 616
Cdd:cd03868  293 EQ 294
M14_CPD_II cd03863
Peptidase M14 carboxypeptidase subfamily N/E-like; Carboxypeptidase D, domain II subgroup; The ...
292-616 7.04e-96

Peptidase M14 carboxypeptidase subfamily N/E-like; Carboxypeptidase D, domain II subgroup; The second carboxypeptidase (CP)-like domain of Carboxypeptidase D (CPD; EC 3.4.17.22), domain II. CPD differs from all other metallocarboxypeptidases in that it contains multiple CP-like domains. CPD belongs to the N/E-like subfamily of the M14 family of metallocarboxypeptidases (MCPs).The M14 family are zinc-binding CPs which hydrolyze single, C-terminal amino acids from polypeptide chains, and have a recognition site for the free C-terminal carboxyl group, which is a key determinant of specificity. CPD is a single-chain protein containing a signal peptide, three tandem repeats of CP-like domains separated by short bridge regions, followed by a transmembrane domain, and a C-terminal cytosolic tail. The first two CP-like domains of CPD contain all of the essential active site and substrate-binding residues, while the third CP-like domain lacks critical residues necessary for enzymatic activity and is inactive towards standard CP substrates. Domain I is optimally active at pH 6.3-7.5 and prefers substrates with C-terminal Arg, whereas domain II is active at pH 5.0-6.5 and prefers substrates with C-terminal Lys. CPD functions in the processing of proteins that transit the secretory pathway, and is present in all vertebrates as well as Drosophila. It is broadly distributed in all tissue types. Within cells, CPD is present in the trans-Golgi network and immature secretory vesicles, but is excluded from mature vesicles. It is thought to play a role in the processing of proteins that are initially processed by furin or related endopeptidases present in the trans-Golgi network, such as growth factors and receptors. CPD is implicated in the pathogenesis of lupus erythematosus (LE), it is regulated by TGF-beta in various cell types of murine and human origin and is significantly down-regulated in CD14 positive cells isolated from patients with LE. As down -regulation of CPD leads to down-modulation of TGF-beta, CPD may have a role in a positive feedback loop.


Pssm-ID: 349435 [Multi-domain]  Cd Length: 296  Bit Score: 299.17  E-value: 7.04e-96
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126920918 292 DFRHHDYKAMRKLMKQVNEQCPNITRIYSIGKSHQGLKLYVMEMSDQPGEHELGEPEVRYVAGMHGNEALGRELLLLLMQ 371
Cdd:cd03863    5 DFRHHHFSDMEIFLRRYANEYPSITRLYSVGKSVELRELYVMEISDNPGVHEPGEPEFKYIGNMHGNEVVGRELLLNLIE 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126920918 372 FLCHEFlRGDPRVTRLLTETRIHLLPSMNPDGYETAfRRGSelVGWAEGRWNHQGIDLNHNFadlntplweaedeglvpd 451
Cdd:cd03863   85 YLCKNF-GTDPEVTDLVQNTRIHIMPSMNPDGYEKS-QEGD--RGGTVGRNNSNNYDLNRNF------------------ 142
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126920918 452 tvpnhhlplPTYYTLPNATVAPETWAVIKWMQRIPFVLSANLHGGELVVSYPFDMTRTPWAAreLTPTPDEAVFRWLSTV 531
Cdd:cd03863  143 ---------PDQFFQITDPPQPETLAVMSWLKTYPFVLSANLHGGSLVVNYPFDDDEQGLAT--YSKSPDDAVFQQLALS 211
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126920918 532 YAGTNRAMQDPdrRPCHSQDFSLY--GSIINGADWHTVPGSMNDFSYLHTNCFEVTVELSCDKFPHENELPQEWENNKDA 609
Cdd:cd03863  212 YSKENSKMYQG--SPCKELYPNEYfpHGITNGAQWYNVPGGMQDWNYLNTNCFEVTIELGCVKYPKAEELPKYWEQNRRS 289

                 ....*..
gi 126920918 610 LLTYLEQ 616
Cdd:cd03863  290 LLQFIKQ 296
Peptidase_M14 pfam00246
Zinc carboxypeptidase;
301-609 2.80e-81

Zinc carboxypeptidase;


Pssm-ID: 459730 [Multi-domain]  Cd Length: 287  Bit Score: 260.31  E-value: 2.80e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126920918  301 MRKLMKQVNEQCPNITRIYSIGKSHQGLKLYVMEMSDQPGEHELGEPEVRYVAGMHGNEALGRELLLLLMQFLCHEFLRg 380
Cdd:pfam00246   1 IEAWLDALAARYPDLVRLVSIGKSVEGRPLKVLKISSGPGEHNPGKPAVFIDGGIHAREWIGPATALYLIHQLLTNYGR- 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126920918  381 DPRVTRLLTETRIHLLPSMNPDGYETAFrrgSELVGWAEGRWNHQ-----GIDLNHNFADlntpLWeaedeglvpDTVPN 455
Cdd:pfam00246  80 DPEITELLDDTDIYILPVVNPDGYEYTH---TTDRLWRKNRSNANgssciGVDLNRNFPD----HW---------NEVGA 143
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126920918  456 HHLPLPTYYTLPNATVAPETWAVIKWMQR-IPFVLSANLHGGELVVSYPFDMTRTpwaarelTPTPDEAVFRWLSTVYAG 534
Cdd:pfam00246 144 SSNPCSETYRGPAPFSEPETRAVADFIRSkKPFVLYISLHSYSQVLLYPYGYTRD-------EPPPDDEELKSLARAAAK 216
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126920918  535 TNRAMqdpdrrpCHSQDFSlYGsIINGADWHTVPGSMNDFSYLHTNC-FEVTVELSCDK----FPHENELPQEWENNKDA 609
Cdd:pfam00246 217 ALQKM-------VRGTSYT-YG-ITNGATIYPASGGSDDWAYGRLGIkYSYTIELRDTGrygfLLPASQIIPTAEETWEA 287
M14_CPM cd03866
Peptidase M14 carboxypeptidase subfamily N/E-like; Carboxypeptidase M subgroup; Peptidase M14 ...
295-616 2.02e-80

Peptidase M14 carboxypeptidase subfamily N/E-like; Carboxypeptidase M subgroup; Peptidase M14 Carboxypeptidase (CP) M (CPM) belongs to the N/E subfamily of the M14 family of metallocarboxypeptidases (MCPs).The M14 family are zinc-binding CPs which hydrolyze single, C-terminal amino acids from polypeptide chains, and have a recognition site for the free C-terminal carboxyl group, which is a key determinant of specificity. CPM is an extracellular glycoprotein, bound to cell membranes via a glycosyl-phosphatidylinositol on the C-terminus of the protein. It specifically removes C-terminal basic residues such as lysine and arginine from peptides and proteins. The highest levels of CPM have been found in human lung and placenta, but significant amounts are present in kidney, blood vessels, intestine, brain, and peripheral nerves. CPM has also been found in soluble form in various body fluids, including amniotic fluid, seminal plasma and urine. Due to its wide distribution in a variety of tissues, it is believed that it plays an important role in the control of peptide hormones and growth factor activity on the cell surface and in the membrane-localized degradation of extracellular proteins, for example it hydrolyses the C-terminal arginine of epidermal growth factor (EGF) resulting in des-Arg-EGF which binds to the EGF receptor (EGFR) with an equal or greater affinity than native EGF. CPM is a required processing enzyme that generates specific agonists for the B1 receptor.


Pssm-ID: 349438  Cd Length: 289  Bit Score: 258.19  E-value: 2.02e-80
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126920918 295 HHDYKAMRKLMKQVNEQCPNITRIYSIGKSHQGLKLYVMEMSDQPGEHELGEPEVRYVAGMHGNEALGRELLLLLMQFLC 374
Cdd:cd03866    1 YHNQEQMETYLKDVNKNYPSITHLHSIGKSVEGRDLWVLVLGRFPTKHRIGIPEFKYVANMHGDEVVGRELLLHLIEFLV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126920918 375 HEFlRGDPRVTRLLTETRIHLLPSMNPDGYETAFRRGSElvgWAEGRWNHQGIDLNHNFADlntplweAEDEGLVPdtvp 454
Cdd:cd03866   81 TSY-GSDPVITRLINSTRIHIMPSMNPDGFEATKKPDCY---YTKGRYNKNGYDLNRNFPD-------AFEENNVQ---- 145
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126920918 455 nhhlplptyytlpnatVAPETWAVIKWMQRIPFVLSANLHGGELVVSYPFDMTRT-PWAARELTPTPDEAVFRWLSTVYA 533
Cdd:cd03866  146 ----------------RQPETRAVMDWIKNETFVLSANLHGGALVASYPFDNGNSgTGQLGYYSVSPDDDVFIYLAKTYS 209
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126920918 534 GTNRAMQDPDRRPcHSQDFSlyGSIINGADWHTVPGSMNDFSYLHTNCFEVTVELSCDKFPHENELPQEWENNKDALLTY 613
Cdd:cd03866  210 YNHTNMYKGIECS-NSQSFP--GGITNGYQWYPLQGGMQDYNYVWGQCFEITLELSCCKYPPEETLPQFWNDNRVALIEY 286

                 ...
gi 126920918 614 LEQ 616
Cdd:cd03866  287 IKQ 289
M14_CP_bacteria cd18173
bacterial peptidase M14 carboxypeptidase, uncharacterized; This family contains only bacterial ...
296-616 1.87e-74

bacterial peptidase M14 carboxypeptidase, uncharacterized; This family contains only bacterial carboxypeptidase (CP) members of the M14 family of metallocarboxypeptidases (MCPs), mostly of which have yet to be characterized. The M14 family are zinc-binding CPs which hydrolyze single, C-terminal amino acids from polypeptide chains, and have a recognition site for the free C-terminal carboxyl group, which is a key determinant of specificity. The N/E subfamily includes eight members, of which five (CPN, CPE, CPM, CPD, CPZ) are considered enzymatically active, while the other three are non-active (CPX1, PCX2, ACLP/AEBP1) and lack the critical active site and substrate-binding residues considered necessary for CP activity. These non-active members may function as binding proteins or display catalytic activity towards other substrates. Unlike the A/B CP subfamily, enzymes belonging to the N/E subfamily are not produced as inactive precursors that require proteolysis to produce the active form; rather, they rely on their substrate specificity and subcellular compartmentalization to prevent inappropriate cleavages that would otherwise damage the cell. In addition, all members of the N/E subfamily contain an extra C-terminal domain that is not present in the A/B subfamily. This domain has structural homology to transthyretin and other proteins and has been proposed to function as a folding domain. The active N/E enzymes fulfill a variety of cellular functions, including prohormone processing, regulation of peptide hormone activity, alteration of protein-protein or protein-cell interactions and transcriptional regulation.


Pssm-ID: 349483 [Multi-domain]  Cd Length: 281  Bit Score: 242.10  E-value: 1.87e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126920918 296 HDYKAMRKLMKQVNEQCPNITRIYSIGKSHQGLKLYVMEMSDQPGEHElGEPEVRYVAGMHGNEALGRELllllMQFLCH 375
Cdd:cd18173    5 PTYEEYEAMMQSFAANYPNICRLVSIGTSVQGRKLLALKISDNVNTEE-AEPEFKYTSTMHGDETTGYEL----MLRLID 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126920918 376 EFLRG---DPRVTRLLTETRIHLLPSMNPDGYetaFRRGSELVGWAEgRWNHQGIDLNHNFADlntplweaedeglvPDT 452
Cdd:cd18173   80 YLLTNygtDPRITNLVDNTEIWINPLANPDGT---YAGGNNTVSGAT-RYNANGVDLNRNFPD--------------PVD 141
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126920918 453 VPNhhlplPTYYTLPnatvaPETWAVIKWMQRIPFVLSANLHGGELVVSYPFDMTRTPwaareltpTPDEAVFRWLSTVY 532
Cdd:cd18173  142 GDH-----PDGNGWQ-----PETQAMMNFADEHNFVLSANFHGGAEVVNYPWDTWYSR--------HPDDDWFQDISREY 203
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126920918 533 AGTNRAMQDPDRrpchsqdFSLYGS-IINGADWHTVPGSMNDFSYLHTNCFEVTVELSCDKFPHENELPQEWENNKDALL 611
Cdd:cd18173  204 ADTNQANSPPMY-------MSEFNNgITNGYDWYEVYGGRQDYMYYWHGCREVTIELSNTKWPPASQLPTYWNYNRESLL 276

                 ....*
gi 126920918 612 TYLEQ 616
Cdd:cd18173  277 NYIEQ 281
M14_CPD_III cd06245
Peptidase M14 carboxypeptidase subfamily N/E-like; Carboxypeptidase D, domain III subgroup; ...
295-616 1.88e-68

Peptidase M14 carboxypeptidase subfamily N/E-like; Carboxypeptidase D, domain III subgroup; The third carboxypeptidase (CP)-like domain of Carboxypeptidase D (CPD; EC 3.4.17.22), domain III. CPD differs from all other metallocarboxypeptidases in that it contains multiple CP-like domains. CPD belongs to the N/E-like subfamily of the M14 family of metallocarboxypeptidases (MCPs).The M14 family are zinc-binding CPs which hydrolyze single, C-terminal amino acids from polypeptide chains, and have a recognition site for the free C-terminal carboxyl group, which is a key determinant of specificity. CPD is a single-chain protein containing a signal peptide, three tandem repeats of CP-like domains separated by short bridge regions, followed by a transmembrane domain, and a C-terminal cytosolic tail. The first two CP-like domains of CPD contain all of the essential active site and substrate-binding residues, the third CP-like domain lacks critical residues necessary for enzymatic activity and is inactive towards standard CP substrates. Domain I is optimally active at pH 6.3-7.5 and prefers substrates with C-terminal Arg, whereas domain II is active at pH 5.0-6.5 and prefers substrates with C-terminal Lys. CPD functions in the processing of proteins that transit the secretory pathway, and is present in all vertebrates as well as Drosophila. It is broadly distributed in all tissue types. Within cells, CPD is present in the trans-Golgi network and immature secretory vesicles, but is excluded from mature vesicles. It is thought to play a role in the processing of proteins that are initially processed by furin or related endopeptidases present in the trans-Golgi network, such as growth factors and receptors. CPD is implicated in the pathogenesis of lupus erythematosus (LE), it is regulated by TGF-beta in various cell types of murine and human origin and is significantly down-regulated in CD14 positive cells isolated from patients with LE. As down -regulation of CPD leads to down-modulation of TGF-beta, CPD may have a role in a positive feedback loop.


Pssm-ID: 349464 [Multi-domain]  Cd Length: 283  Bit Score: 226.56  E-value: 1.88e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126920918 295 HHDYKAMRKLMKQVNEQCPNITRIYSIGKSHQGLKLYVMEMSDQPGEHELGEPEVRYVAGMHGNEALGRELLLLLMQFLC 374
Cdd:cd06245    1 YHSYKQLSKFLRGLNSNYPTITNLTSLGQSVEKRDIWVLEIGNKPNESEPSEPKILFVGGIHGNAPVGTELLLLLAHFLC 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126920918 375 HeFLRGDPRVTRLLTETRIHLLPSMNPDGYETAFRRGSElvgWAEGRWNHQGIDLNHNFadlntplweaedeglvpdtvp 454
Cdd:cd06245   81 H-NYKKDSAITKLLNRTRIHIVPSLNPDGAEKAEEKKCT---SKIGEKNANGVDLDTDF--------------------- 135
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126920918 455 nhhlplPTYYTLPNATVAPETWAVIKWMQRIPFVLSANLHGGELVVSYPFDMTRtpwaarelTPTPDEAVFRWLSTVYAG 534
Cdd:cd06245  136 ------ESNANNRSGAAQPETKAIMDWLKEKDFTLSVALDGGSLVVTYPYDKPV--------QTVENKETLKHLAKVYAN 201
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126920918 535 TNRAMQDPDRRPCHSQDFSLYGSIINGADWHTVPGSMNDFSYLHTNCFEVTVELSCDKFPHENELPQEWENNKDALLTYL 614
Cdd:cd06245  202 NHPTMHAGDPGCCSNSDENFTNGVIRASEWHSHKGSMLDFSYKFGSCPEITVYTSCCYFPPAEELLTLWAEHKKSLLSMI 281

                 ..
gi 126920918 615 EQ 616
Cdd:cd06245  282 VE 283
M14_CP_plant cd18172
Zinc carboxypeptidase, including SOL1, a carboxypeptidase D in plant; This family includes ...
295-615 7.92e-68

Zinc carboxypeptidase, including SOL1, a carboxypeptidase D in plant; This family includes only plant members of the carboxypeptidase (CP) N/E-like subfamily of the M14 family of metallocarboxypeptidases (MCPs). It includes Arabidopsis thaliana SOL1 carboxypeptidase D which is known to possess enzymatic activity to remove the C-terminal arginine residue of CLE19 proprotein in vitro, and SOL1-dependent cleavage of the C-terminal arginine residue is necessary for CLE19 activity in vivo. The M14 family are zinc-binding CPs which hydrolyze single, C-terminal amino acids from polypeptide chains, and have a recognition site for the free C-terminal carboxyl group, which is a key determinant of specificity. The N/E subfamily includes eight members, of which five (CPN, CPE, CPM, CPD, CPZ) are considered enzymatically active, while the other three are non-active (CPX1, PCX2, ACLP/AEBP1) and lack the critical active site and substrate-binding residues considered necessary for CP activity. These non-active members may function as binding proteins or display catalytic activity towards other substrates. Unlike the A/B CP subfamily, enzymes belonging to the N/E subfamily are not produced as inactive precursors that require proteolysis to produce the active form; rather, they rely on their substrate specificity and subcellular compartmentalization to prevent inappropriate cleavages that would otherwise damage the cell. In addition, all members of the N/E subfamily contain an extra C-terminal domain that is not present in the A/B subfamily. This domain has structural homology to transthyretin and other proteins and has been proposed to function as a folding domain. The active N/E enzymes fulfill a variety of cellular functions, including prohormone processing, regulation of peptide hormone activity, alteration of protein-protein or protein-cell interactions and transcriptional regulation.


Pssm-ID: 349482 [Multi-domain]  Cd Length: 276  Bit Score: 224.60  E-value: 7.92e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126920918 295 HHDYKAMRKLMKQVNEQCPNITRIYSIGKSHQGLKLYVMEMSDQPGEHElGEPEVRYVAGMHGNEALGRELLLLLMQFLC 374
Cdd:cd18172    1 YHSNAELEDALKAFTRRCGAISRLIVIGSSVNGFPLWALEISDGPGEDE-TEPAFKFVGNMHGDEPVGRELLLRLADWLC 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126920918 375 HEFLRGDPRVTRLLTETRIHLLPSMNPDGYEtafrrgselvgwAEGRWNHQGIDLNHNFADLNTPLWEAEDEGLvpdtvp 454
Cdd:cd18172   80 ANYKAKDPLAAKIVENAHLHLVPTMNPDGFA------------RRRRNNANNVDLNRDFPDQFFPKNLRNDLAA------ 141
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126920918 455 nhhlplptyytlpnatVAPETWAVIKWMQRIPFVLSANLHGGELVVSYPFDMT---RTPWAAreltpTPDEAVFRWLSTV 531
Cdd:cd18172  142 ----------------RQPETLAVMNWSRSVRFTASANLHEGALVANYPWDGNadgRTKYSA-----SPDDATFRRLASV 200
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126920918 532 YAGTNRAMQDPDRRPchsqdfslyGSIINGADWHTVPGSMNDFSYLHTNCFEVTVELSCDKFPHENELPQEWENNKDALL 611
Cdd:cd18172  201 YAQAHPNMAKSKEFP---------GGITNGAQWYPLYGGMQDWNYLHTGCMDLTLEVNDNKWPPEDRLVQIWAEHRKAML 271

                 ....
gi 126920918 612 TYLE 615
Cdd:cd18172  272 ALAA 275
Zn_pept smart00631
Zn_pept domain;
295-602 1.47e-66

Zn_pept domain;


Pssm-ID: 214748 [Multi-domain]  Cd Length: 277  Bit Score: 221.06  E-value: 1.47e-66
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126920918   295 HHDYKAMRKLMKQVNEQCPNITRIYSIGKSHQGLKLYVMEMSDQPGEhelGEPEVRYVAGMHGNEALGRELLLLLMQFLC 374
Cdd:smart00631   1 YHSYEEIEAWLKELAARYPDLVRLVSIGKSVEGRPIWVLKISNGGSH---DKPAIFIDAGIHAREWIGPATALYLINQLL 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126920918   375 HEFLRgDPRVTRLLTETRIHLLPSMNPDGYEtaFRRGSElVGWAEGRWNHQ---GIDLNHNFADlntpLWEAedeglvpd 451
Cdd:smart00631  78 ENYGR-DPRVTNLLDKTDIYIVPVLNPDGYE--YTHTGD-RLWRKNRSPNSncrGVDLNRNFPF----HWGE-------- 141
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126920918   452 tvpnHHLPLPTYYTLPNATVAPETWAVIKWM-QRIPFVLSANLHGGELVVSYPFDMTRTpwaarELTPTPDE--AVFRWL 528
Cdd:smart00631 142 ----TGNPCSETYAGPSPFSEPETKAVRDFIrSNRRFKLYIDLHSYSQLILYPYGYTKN-----DLPPNVDDldAVAKAL 212
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126920918   529 STVYAgtnramqdpdrrpchsqdfSLYGS-----IINGADWHtVPGSMNDFSYLHTN-CFEVTVELSCD-----KFPHEN 597
Cdd:smart00631 213 AKALA-------------------SVHGTrytygISNGAIYP-ASGGSDDWAYGVLGiPFSFTLELRDDgrygfLLPPSQ 272

                   ....*
gi 126920918   598 ELPQE 602
Cdd:smart00631 273 IIPTG 277
FA58C cd00057
Coagulation factor 5/8 C-terminal domain, discoidin domain; Cell surface-attached ...
112-269 2.31e-46

Coagulation factor 5/8 C-terminal domain, discoidin domain; Cell surface-attached carbohydrate-binding domain, present in eukaryotes and assumed to have horizontally transferred to eubacterial genomes.


Pssm-ID: 238014 [Multi-domain]  Cd Length: 143  Bit Score: 161.37  E-value: 2.31e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126920918 112 PPLGLESLRvSDNQLDASSSQSFGLGPHRGRLNIqsgledgdlfDGAWCAEQQDAEPWLQVDARHPTRFSGIITQGRNSI 191
Cdd:cd00057    1 EPLGMESGL-ADDQITASSSYSSGWEASRARLNS----------DNAWTPAVNDPPQWLQVDLGKTRRVTGIQTQGRKGG 69
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 126920918 192 WRYDWVTSYKVQFSNDSRTWWGSKNRssGMDAVFPANSDPETPVLNLLPEPQVARFIRLLPQTWlqGGASCLRAEILA 269
Cdd:cd00057   70 GSSEWVTSYKVQYSLDGETWTTYKDK--GEEKVFTGNSDGSTPVTNDFPPPIVARYIRILPTTW--NGNISLRLELYG 143
Peptidase_M14NE-CP-C_like cd11308
Peptidase associated domain: C-terminal domain of M14 N/E carboxypeptidase; putative folding, ...
620-696 2.63e-35

Peptidase associated domain: C-terminal domain of M14 N/E carboxypeptidase; putative folding, regulation, or interaction domain; This domain is found C-terminal to the M14 carboxypeptidase (CP) N/E subfamily containing zinc-binding enzymes that hydrolyze single C-terminal amino acids from polypeptide chains, and have a recognition site for the free C-terminal carboxyl group, which is a key determinant of specificity. The N/E subfamily includes enzymatically active members (carboxypeptidase N, E, M, D, and Z), as well as non-active members (carboxypeptidase-like protein 1, -2, aortic CP-like protein, and adipocyte enhancer binding protein-1) which lack the critical active site and substrate-binding residues considered necessary for activity. The active N/E enzymes fulfill a variety of cellular functions, including prohormone processing, regulation of peptide hormone activity, alteration of protein-protein or protein-cell interactions and transcriptional regulation. For M14 CPs, it has been suggested that this domain may assist in folding of the CP domain, regulate enzyme activity, or be involved in interactions with other proteins or with membranes; for carboxypeptidase M, it may interact with the bradykinin 1 receptor at the cell surface. This domain may also be found in other peptidase families.


Pssm-ID: 200604 [Multi-domain]  Cd Length: 76  Bit Score: 128.03  E-value: 2.63e-35
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 126920918 620 GIAGVVRDKDTElGIADAVISVDGINHDVTTAWGGDYWRLLTPGDYMVTASAEGYHTVTRSCRVTFEEGPVPCNFRL 696
Cdd:cd11308    1 GIKGFVTDATGN-PIANATISVEGINHDVTTAKDGDYWRLLLPGTYNVTASAPGYQPVTKTVTVPNNFSATVVNFTL 76
M14_CPT cd03859
Peptidase M14 Carboxypeptidase T subfamily; Peptidase M14-like domain of carboxypeptidase (CP) ...
296-610 3.37e-35

Peptidase M14 Carboxypeptidase T subfamily; Peptidase M14-like domain of carboxypeptidase (CP) T (CPT), CPT belongs to the M14 family of metallocarboxypeptidases (MCPs). The M14 family are zinc-binding CPs which hydrolyze single, C-terminal amino acids from polypeptide chains, and have a recognition site for the free C-terminal carboxyl group, which is a key determinant of specificity. CPT has moderate similarity to CPA and CPB, and exhibits dual-substrate specificity by cleaving C-terminal hydrophobic amino acid residues like CPA and C-terminal positively charged residues like CPB. CPA and CPB are M14 family peptidases but do not belong to this CPT group. The substrate specificity difference between CPT and CPA and CPB is ascribed to a few amino acid substitutions at the substrate-binding pocket while the spatial organization of the binding site remains the same as in all Zn-CPs. CPT has increased thermal stability in presence of Ca2+ ions, and two disulfide bridges which give an additional stabilization factor.


Pssm-ID: 349432 [Multi-domain]  Cd Length: 292  Bit Score: 135.46  E-value: 3.37e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126920918 296 HDYKAMRKLMKQVNEQCPNITRIYSIGKSHQGLKLYVMEMSDQPGEHElGEPEVRYVAGMHGNEALGRELLLLLMQFLCH 375
Cdd:cd03859    5 HTYAELVAELDQLAAEYPEITKLISIGKSVEGRPIWAVKISDNPDEDE-DEPEVLFMGLHHAREWISLEVALYFADYLLE 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126920918 376 EFLRgDPRVTRLLTETRIHLLPSMNPDGYETAFRRGSElVGW-------AEGRWNHQGIDLNHNFADlntpLWEAEDEGL 448
Cdd:cd03859   84 NYGT-DPRITNLVDNREIWIIPVVNPDGYEYNRETGGG-RLWrknrrpnNGNNPGSDGVDLNRNYGY----HWGGDNGGS 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126920918 449 VPDtvpnhhlPLPTYYTLPNATVAPETWAVIKWMQRIPFVLSANLHG-GELVVSypfdmtrtPWAARELTPTPDEAVFRW 527
Cdd:cd03859  158 SPD-------PSSETYRGPAPFSEPETQAIRDLVESHDFKVAISYHSyGELVLY--------PWGYTSDAPTPDEDVFEE 222
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126920918 528 LSTVYAGTNRAMQDPdrrpchSQDFSLYgsiingadwhTVPGSMNDFSYLHTNCFEVTVEL---SCDKFPHENELPQEWE 604
Cdd:cd03859  223 LAEEMASYNGGGYTP------QQSSDLY----------PTNGDTDDWMYGEKGIIAFTPELgpeFYPFYPPPSQIDPLAE 286

                 ....*.
gi 126920918 605 NNKDAL 610
Cdd:cd03859  287 ENLPAA 292
F5_F8_type_C pfam00754
F5/8 type C domain; This domain is also known as the discoidin (DS) domain family.
129-267 9.40e-31

F5/8 type C domain; This domain is also known as the discoidin (DS) domain family.


Pssm-ID: 459925 [Multi-domain]  Cd Length: 127  Bit Score: 117.16  E-value: 9.40e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126920918  129 SSSQSFGLGPHRGRLniqsgleDGDLfDGAWCAEQQDAEPWLQVDARHPTRFSGIITQGRNSIWRYdWVTSYKVQFSNDS 208
Cdd:pfam00754   4 ASSSYSGEGPAAAAL-------DGDP-NTAWSAWSGDDPQWIQVDLGKPKKITGVVTQGRQDGSNG-YVTSYKIEYSLDG 74
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 126920918  209 RTWwgsknrSSGMDAVFPANSDPETPVLNLLPEPQVARFIRLLPQTWLQGGASCLRAEI 267
Cdd:pfam00754  75 ENW------TTVKDEKIPGNNDNNTPVTNTFDPPIKARYVRIVPTSWNGGNGIALRAEL 127
FA58C smart00231
Coagulation factor 5/8 C-terminal domain, discoidin domain; Cell surface-attached ...
113-270 1.92e-30

Coagulation factor 5/8 C-terminal domain, discoidin domain; Cell surface-attached carbohydrate-binding domain, present in eukaryotes and assumed to have horizontally transferred to eubacterial genomes.


Pssm-ID: 214572  Cd Length: 139  Bit Score: 116.45  E-value: 1.92e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126920918   113 PLGLESlrvsDNQLDASSSqsfGLGPHRGRLNIQSgledgdlfDGAWCAEQQDAEPWLQVDARHPTRFSGIITQGRNSiw 192
Cdd:smart00231   5 PLGLES----DSQITASSS---YWAAKIARLNGGS--------DGGWCPAKNDLPPWIQVDLGRLRTVTGVITGRRHG-- 67
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 126920918   193 rYDWVTSYKVQFSNDSRTWWGSKNrssGMDAVFPANSDPETPVLNLLPEPQVARFIRLLPQTWlqGGASCLRAEILAC 270
Cdd:smart00231  68 -NGDWVTYKLEYSDDGVNWTTYKD---GNSKVFPGNSDAGTVVLNDFPPPIVARYVRILPTGW--NGNIILRVELLGC 139
MpaA COG2866
Murein tripeptide amidase MpaA [Cell wall/membrane/envelope biogenesis];
294-527 7.01e-29

Murein tripeptide amidase MpaA [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442113 [Multi-domain]  Cd Length: 337  Bit Score: 118.25  E-value: 7.01e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126920918 294 RHHDYKAMRKLMKQVnEQCPNITRIYSIGKSHQGLKLYVMEMSDQPGehelGEPEVRYVAGMHGNEALGRELllllMQFL 373
Cdd:COG2866   18 RYYTYEELLALLAKL-AAASPLVELESIGKSVEGRPIYLLKIGDPAE----GKPKVLLNAQQHGNEWTGTEA----LLGL 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126920918 374 CHEFLRG-DPRVTRLLTETRIHLLPSMNPDGYETAFRRgselvgwaegrwNHQGIDLNHNFADlntpLWEAEdeglvpdt 452
Cdd:COG2866   89 LEDLLDNyDPLIRALLDNVTLYIVPMLNPDGAERNTRT------------NANGVDLNRDWPA----PWLSE-------- 144
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 126920918 453 vpnhhlplptyytlpnatvaPETWAVIKWMQRIPFVLSANLHGGELVVSYPFDMTRTPWAarELTPTPDEAVFRW 527
Cdd:COG2866  145 --------------------PETRALRDLLDEHDPDFVLDLHGQGELFYWFVGTTEPTGS--FLAPSYDEEREAF 197
Peptidase_M14_like cd00596
M14 family of metallocarboxypeptidases and related proteins; The M14 family of ...
351-606 7.84e-27

M14 family of metallocarboxypeptidases and related proteins; The M14 family of metallocarboxypeptidases (MCPs), also known as funnelins, are zinc-binding carboxypeptidases (CPs) which hydrolyze single, C-terminal amino acids from polypeptide chains, and have a recognition site for the free C-terminal carboxyl group, which is a key determinant of specificity. Two major subfamilies of the M14 family, defined based on sequence and structural homology, are the A/B and N/E subfamilies. Enzymes belonging to the A/B subfamily are normally synthesized as inactive precursors containing preceding signal peptide, followed by an N-terminal pro-region linked to the enzyme; these proenzymes are called procarboxypeptidases. The A/B enzymes can be further divided based on their substrate specificity; Carboxypeptidase A-like (CPA-like) enzymes favor hydrophobic residues while carboxypeptidase B-like (CPB-like) enzymes only cleave the basic residues lysine or arginine. The A forms have slightly different specificities, with Carboxypeptidase A1 (CPA1) preferring aliphatic and small aromatic residues, and CPA2 preferring the bulky aromatic side chains. Enzymes belonging to the N/E subfamily enzymes are not produced as inactive precursors and instead rely on their substrate specificity and subcellular compartmentalization to prevent inappropriate cleavage. They contain an extra C-terminal transthyretin-like domain, thought to be involved in folding or formation of oligomers. MCPs can also be classified based on their involvement in specific physiological processes; the pancreatic MCPs participate only in alimentary digestion and include carboxypeptidase A and B (A/B subfamily), while others, namely regulatory MCPs or the N/E subfamily, are involved in more selective reactions, mainly in non-digestive tissues and fluids, acting on blood coagulation/fibrinolysis, inflammation and local anaphylaxis, pro-hormone and neuropeptide processing, cellular response and others. Another MCP subfamily, is that of succinylglutamate desuccinylase /aspartoacylase, which hydrolyzes N-acetyl-L-aspartate (NAA), and deficiency in which is the established cause of Canavan disease. Another subfamily (referred to as subfamily C) includes an exceptional type of activity in the MCP family, that of dipeptidyl-peptidase activity of gamma-glutamyl-(L)-meso-diaminopimelate peptidase I which is involved in bacterial cell wall metabolism.


Pssm-ID: 349427 [Multi-domain]  Cd Length: 216  Bit Score: 109.09  E-value: 7.84e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126920918 351 YVAGMHGNEALGRELLLLLMQFLCHEFLRGDprVTRLLTETRIHLLPSMNPDGYETAFRRGselvgwaeGRWNHQGIDLN 430
Cdd:cd00596    3 ITGGIHGNEVIGVELALALIEYLLENYGNDP--LKRLLDNVELWIVPLVNPDGFARVIDSG--------GRKNANGVDLN 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126920918 431 HNFadlntPLWEAEDEGlvpdtvpnhHLPLPTYYTLPNATVAPETWAVIKWMQRIPFVLSANLHGGELVVSYPFdmtrtp 510
Cdd:cd00596   73 RNF-----PYNWGKDGT---------SGPSSPTYRGPAPFSEPETQALRDLAKSHRFDLAVSYHSSSEAILYPY------ 132
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126920918 511 waARELTPTPDEAVFRWLSTVYAGTNramqdpdrrpchsqdFSLYGSIINGADWHTVPGSMNDFSYLHTNCFEVTVELSC 590
Cdd:cd00596  133 --GYTNEPPPDFSEFQELAAGLARAL---------------GAGEYGYGYSYTWYSTTGTADDWLYGELGILAFTVELGT 195
                        250
                 ....*....|....*.
gi 126920918 591 DKFPHENELPQEWENN 606
Cdd:cd00596  196 ADYPLPGTLLDRRLER 211
M14-like cd06905
Peptidase M14-like domain; uncharacterized subfamily; A functionally uncharacterized subgroup ...
291-410 6.39e-20

Peptidase M14-like domain; uncharacterized subfamily; A functionally uncharacterized subgroup of the M14 family of metallocarboxypeptidases (MCPs). The M14 family are zinc-binding carboxypeptidases (CPs) which hydrolyze single, C-terminal amino acids from polypeptide chains, and have a recognition site for the free C-terminal carboxyl group, which is a key determinant of specificity. Two major subfamilies of the M14 family, defined based on sequence and structural homology, are the A/B and N/E subfamilies. Enzymes belonging to the A/B subfamily are normally synthesized as inactive precursors containing preceding signal peptide, followed by an N-terminal pro-region linked to the enzyme; these proenzymes are called procarboxypeptidases. The A/B enzymes can be further divided based on their substrate specificity; Carboxypeptidase A-like (CPA-like) enzymes favor hydrophobic residues while carboxypeptidase B-like (CPB-like) enzymes only cleave the basic residues lysine or arginine. The A forms have slightly different specificities, with Carboxypeptidase A1 (CPA1) preferring aliphatic and small aromatic residues, and CPA2 preferring the bulky aromatic side chains. Enzymes belonging to the N/E subfamily enzymes are not produced as inactive precursors and instead rely on their substrate specificity and subcellular compartmentalization to prevent inappropriate cleavages. They contain an extra C-terminal transthyretin-like domain, thought to be involved in folding or formation of oligomers. MCPs can also be classified based on their involvement in specific physiological processes; the pancreatic MCPs participate only in alimentary digestion and include carboxypeptidase A and B (A/B subfamily), while others, namely regulatory MCPs or the N/E subfamily, are involved in more selective reactions, mainly in non-digestive tissues and fluids, acting on blood coagulation/fibrinolysis, inflammation and local anaphylaxis, pro-hormone and neuropeptide processing, cellular response and others. Another MCP subfamily, is that of succinylglutamate desuccinylase /aspartoacylase, which hydrolyzes N-acetyl-L-aspartate (NAA), and deficiency in which is the established cause of Canavan disease. Another subfamily (referred to as subfamily C) includes an exceptional type of activity in the MCP family, that of dipeptidyl-peptidase activity of gamma-glutamyl-(L)-meso-diaminopimelate peptidase I which is involved in bacterial cell wall metabolism.


Pssm-ID: 349476 [Multi-domain]  Cd Length: 359  Bit Score: 91.91  E-value: 6.39e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126920918 291 LDFRH-HDYKAMRKLMKQVNEQCPNITRIYSIGKSHQGLKLYVMEMSDQPGEHELGEPEVRYVAGMHGNEALGRELLLLL 369
Cdd:cd06905    1 LAFDRyYTYAELTARLKALAEAYPNLVRLESIGKSYEGRDIWLLTITNGETGPADEKPALWVDGNIHGNEVTGSEVALYL 80
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 126920918 370 MQFLCHEFLRgDPRVTRLLTETRIHLLPSMNPDGYETAFRR 410
Cdd:cd06905   81 AEYLLTNYGK-DPEITRLLDTRTFYILPRLNPDGAEAYKLK 120
M14_CP_A-B_like cd03860
Peptidase M14 carboxypeptidase subfamily A/B-like; The Peptidase M14 Carboxypeptidase (CP) A/B ...
296-434 4.85e-11

Peptidase M14 carboxypeptidase subfamily A/B-like; The Peptidase M14 Carboxypeptidase (CP) A/B subfamily is one of two main M14 CP subfamilies defined by sequence and structural homology, the other being the N/E subfamily. CPs hydrolyze single, C-terminal amino acids from polypeptide chains. They have a recognition site for the free C-terminal carboxyl group, which is a key determinant of specificity. Enzymes belonging to the A/B subfamily are normally synthesized as inactive precursors containing preceding signal peptide, followed by a globular N-terminal pro-region linked to the enzyme; these proenzymes are called procarboxypeptidases. The A/B enzymes can be further divided based on their substrate specificity; Carboxypeptidase A-like (CPA-like) enzymes favor hydrophobic residues while carboxypeptidase B-like (CPB-like) enzymes only cleave the basic residues lysine or arginine. There are nine members in the A/B family: CPA1, CPA2, CPA3, CPA4, CPA5, CPA6, CPB, CPO and CPU. CPA1, CPA2 and CPB are produced by the pancreas. The A forms have slightly different specificities, with CPA1 preferring aliphatic and small aromatic residues, and CPA2 preferring the bulkier aromatic side chains. CPA3 is found in secretory granules of mast cells and functions in inflammatory processes. CPA4 is detected in hormone-regulated tissues, and is thought to play a role in prostate cancer. CPA5 is present in discrete regions of pituitary and other tissues, and cleaves aliphatic C-terminal residues. CPA6 is highly expressed in embryonic brain and optic muscle, suggesting that it may play a specific role in cell migration and axonal guidance. CPU (also called CPB2) is produced and secreted by the liver as the inactive precursor, PCPU, commonly referred to as thrombin-activatable fibrinolysis inhibitor (TAFI). Little is known about CPO but it has been suggested to have specificity for acidic residues.


Pssm-ID: 349433 [Multi-domain]  Cd Length: 300  Bit Score: 64.47  E-value: 4.85e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126920918 296 HDYKAMRKLMKQVNEQCPNITRIYSIGKSHQGLKLYVMEMSDQPGEHelGEPEVRYVAGMHGnealgRE-LLLLLMQFLC 374
Cdd:cd03860    2 HPLDDIVQWLDDLAAAFPDNVEIFTIGKSYEGRDITGIHIWGSGGKG--GKPAIVIHGGQHA-----REwISTSTVEYLA 74
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 126920918 375 HEFLRG---DPRVTRLLTETRIHLLPSMNPDGYE-TafrrgselvgWAEGR-W--NHQ--------GIDLNHNFA 434
Cdd:cd03860   75 HQLLSGygsDATITALLDKFDFYIIPVVNPDGYVyT----------WTTDRlWrkNRQptggsscvGIDLNRNWG 139
M14-like cd03857
Peptidase M14-like domain; uncharacterized subfamily; Peptidase M14-like domain of a ...
351-509 5.28e-11

Peptidase M14-like domain; uncharacterized subfamily; Peptidase M14-like domain of a functionally uncharacterized subgroup of the M14 family of metallocarboxypeptidases (MCPs). The M14 family are zinc-binding carboxypeptidases (CPs) which hydrolyze single, C-terminal amino acids from polypeptide chains, and have a recognition site for the free C-terminal carboxyl group, which is a key determinant of specificity. Two major subfamilies of the M14 family, defined based on sequence and structural homology, are the A/B and N/E subfamilies. Enzymes belonging to the A/B subfamily are normally synthesized as inactive precursors containing preceding signal peptide, followed by an N-terminal pro-region linked to the enzyme; these proenzymes are called procarboxypeptidases. The A/B enzymes can be further divided based on their substrate specificity; Carboxypeptidase A-like (CPA-like) enzymes favor hydrophobic residues while carboxypeptidase B-like (CPB-like) enzymes only cleave the basic residues lysine or arginine. The A forms have slightly different specificities, with Carboxypeptidase A1 (CPA1) preferring aliphatic and small aromatic residues, and CPA2 preferring the bulky aromatic side chains. Enzymes belonging to the N/E subfamily enzymes are not produced as inactive precursors and instead rely on their substrate specificity and subcellular compartmentalization to prevent inappropriate cleavage. They contain an extra C-terminal transthyretin-like domain, thought to be involved in folding or formation of oligomers. MCPs can also be classified based on their involvement in specific physiological processes; the pancreatic MCPs participate only in alimentary digestion and include carboxypeptidase A and B (A/B subfamily), while others, namely regulatory MCPs or the N/E subfamily, are involved in more selective reactions, mainly in non-digestive tissues and fluids, acting on blood coagulation/fibrinolysis, inflammation and local anaphylaxis, pro-hormone and neuropeptide processing, cellular response and others. Another MCP subfamily, is that of succinylglutamate desuccinylase /aspartoacylase, which hydrolyzes N-acetyl-L-aspartate (NAA), and deficiency in which is the established cause of Canavan disease. Another subfamily (referred to as subfamily C) includes an exceptional type of activity in the MCP family, that of dipeptidyl-peptidase activity of gamma-glutamyl-(L)-meso-diaminopimelate peptidase I which is involved in bacterial cell wall metabolism.


Pssm-ID: 349430 [Multi-domain]  Cd Length: 203  Bit Score: 62.48  E-value: 5.28e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126920918 351 YVAGMHGNEALGRELLlllMQFLCHEFLRGDPrVTRLLTETRIHLLPSMNPDGYE-TAFRRGSELVGWAEGRWNHQGIDL 429
Cdd:cd03857    4 LAAQIHGNETTGTEAL---MELIRDLASESDE-AAKLLDNIVILLVPQLNPDGAElFVNFYLDSMNGLPGTRYNANGIDL 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126920918 430 NHNFADLNTPLWEAEDE---GLVPDTVPNHH------LPLPTYYTLPNATVAPEtwAVIKWMQRIPFVLSANLHGGELVV 500
Cdd:cd03857   80 NRDHVKLTQPETQAVAEnfiHWWPDIFIDLHeqvgasIPYPTPPDAPNYNLVDL--RSDAENGQEHIRLIAGEGSGELGK 157

                 ....*....
gi 126920918 501 SYPFDMTRT 509
Cdd:cd03857  158 YFSPMRGGF 166
CarboxypepD_reg pfam13620
Carboxypeptidase regulatory-like domain;
620-696 5.29e-11

Carboxypeptidase regulatory-like domain;


Pssm-ID: 433354 [Multi-domain]  Cd Length: 81  Bit Score: 59.22  E-value: 5.29e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126920918  620 GIAGVVRDKDTElGIADAVISV----DGINHDVTTAWGGDYW-RLLTPGDYMVTASAEGYHTVTRScRVTFEEG-PVPCN 693
Cdd:pfam13620   1 TISGTVTDPSGA-PVPGATVTVtntdTGTVRTTTTDADGRYRfPGLPPGTYTVTVSAPGFKTATRT-GVTVTAGqTTTLD 78

                  ...
gi 126920918  694 FRL 696
Cdd:pfam13620  79 VTL 81
M14_Endopeptidase_I cd06229
Peptidase M14 carboxypeptidase family-like domain of Endopeptidase I; Peptidase M14-like ...
349-494 8.92e-10

Peptidase M14 carboxypeptidase family-like domain of Endopeptidase I; Peptidase M14-like domain of Gamma-D-glutamyl-L-diamino acid endopeptidase 1 (also known as Gamma-D-glutamyl-meso-diaminopimelate peptidase I, and Endopeptidase I (ENP1); EC 3.4.19.11). ENP1 is a member of the M14 family of metallocarboxypeptidases (MCPs), and is classified as belonging to subfamily C. However it has an exceptional type of activity of hydrolyzing the gamma-D-Glu-(L)meso-diaminopimelic acid (gamma-D-Glu-Dap) bond of L-Ala-gamma-D-Glu-(L)meso-diaminopimelic acid and L-Ala-gamma-D-Glu-(L)meso-diaminopimelic acid(L)-D-Ala peptides. ENP1 has a different substrate specificity and cellular role than MpaA (MpaA does not belong to this group). ENP1 hydrolyzes the gamma-D-Glu-Dap bond of MurNAc-tripeptide and MurNAc-tetrapeptide, as well as the amide bond of free tripeptide and tetrapeptide. ENP1 is active on spore cortex peptidoglycan, and is produced at stage IV of sporulation in forespore and spore integuments.


Pssm-ID: 349448 [Multi-domain]  Cd Length: 238  Bit Score: 59.66  E-value: 8.92e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126920918 349 VRYVAGMHGNEALgreLLLLLMQFLcHEFLRG--------DPRVTRLLTETRIHLLPSMNPDGYE------TAFR-RGSE 413
Cdd:cd06229    1 VLYNASFHAREYI---TTLLLMKFI-EDYAKAyvnksyirGKDVGELLNKVTLHIVPMVNPDGVEisqngsNAINpYYLR 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126920918 414 LVGWAEG-----RW--NHQGIDLNHNFADlntpLWEAEDEglvpdtvPNHHLPLPTYYTLPNATVAPETWAVIKWMQRIP 486
Cdd:cd06229   77 LVAWNKKgtdftGWkaNIRGVDLNRNFPA----GWEKEKR-------LGPKAPGPRDYPGKEPLSEPETKAMAALTRQND 145

                 ....*...
gi 126920918 487 FVLSANLH 494
Cdd:cd06229  146 FDLVLAYH 153
M14_MpaA-like cd06904
Peptidase M14-like domain of Escherichia coli Murein Peptide Amidase A and related proteins; ...
321-614 1.40e-09

Peptidase M14-like domain of Escherichia coli Murein Peptide Amidase A and related proteins; Peptidase M14-like domain of Escherichia coli Murein Peptide Amidase A (MpaA) and related proteins. MpaA is a member of the M14 family of metallocarboxypeptidases (MCPs), however it has an exceptional type of activity, it hydrolyzes the gamma-D-glutamyl-meso-diaminopimelic acid (gamma-D-Glu-Dap) bond in murein peptides. MpaA is specific for cleavage of the gamma-D-Glu-Dap bond of free murein tripeptide; it may also cleave murein tetrapeptide. MpaA has a different substrate specificity and cellular role than endopeptidase I, ENP1 (ENP1 does not belong to this group). MpaA works on free murein peptide in the recycling pathway.


Pssm-ID: 349475 [Multi-domain]  Cd Length: 214  Bit Score: 58.83  E-value: 1.40e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126920918 321 IGKSHQGLKLYVMEMSDQPGehelgePEVRYVAGMHGNEALGrelllllmQFLCHEFLRgdprvtRLLTET-----RIHL 395
Cdd:cd06904    4 YGTSVKGRPILAYKFGPGSR------ARILIIGGIHGDEPEG--------VSLVEHLLR------WLKNHPasgdfHIVV 63
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126920918 396 LPSMNPDGYEtafrRGSelvgwaegRWNHQGIDLNHNFadlNTPLWEAedEGLVPDTvpnhhlplPTYYTLPNATVAPET 475
Cdd:cd06904   64 VPCLNPDGLA----AGT--------RTNANGVDLNRNF---PTKNWEP--DARKPKD--------PRYYPGPKPASEPET 118
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126920918 476 WAVIKWMQRIPFvlsanlhggELVVSypfdmtrtpwaareltptpdeaVFRWLSTVYagtnramqDPDRRPCHSQDFSLY 555
Cdd:cd06904  119 RALVELIERFKP---------DRIIS----------------------LHAPYLVNY--------DGPAKSLLAEKLAQA 159
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 126920918 556 GSIINGADWHTVPGSMNDFSYLHTNCFEVTVELscdkfPHENELPQEWENNKDALLTYL 614
Cdd:cd06904  160 TGYPVVGDVGYTPGSLGTYAGIERNIPVITLEL-----PEAVSIDELWQDLKRALIEAI 213
M14_CP_insect cd06248
Peptidase M14 carboxypeptidase subfamily A/B-like; This family includes peptidase M14 ...
296-588 6.59e-09

Peptidase M14 carboxypeptidase subfamily A/B-like; This family includes peptidase M14 carboxypeptidases found specifically in insects, including B-type carboxypeptidase of H. zea (CPBHz, insect gut carboxypeptidase-3) that is insensitive to potato carboxypeptidase inhibitor (PCI) in corn earworm, and midgut procarboxypeptidase A (PCPAHa, insect gut carboxypeptidase-1) from Helicoverpa armigera larva, a devastating pest of crops. PCPAHa preferentially cleaves aliphatic and aromatic residues. The peptidase M14 Carboxypeptidase (CP) A/B subfamily is one of two main M14 CP subfamilies defined by sequence and structural homology, the other being the N/E subfamily. CPs hydrolyze single, C-terminal amino acids from polypeptide chains. They have a recognition site for the free C-terminal carboxyl group, which is a key determinant of specificity. Enzymes belonging to the A/B subfamily are normally synthesized as inactive precursors containing preceding signal peptide, followed by a globular N-terminal pro-region linked to the enzyme; these proenzymes are called procarboxypeptidases. The A/B enzymes can be further divided based on their substrate specificity; Carboxypeptidase A-like (CPA-like) enzymes favor hydrophobic residues while carboxypeptidase B-like (CPB-like) enzymes only cleave the basic residues lysine or arginine. There are nine members in the A/B family: CPA1, CPA2, CPA3, CPA4, CPA5, CPA6, CPB, CPO and CPU. CPA1, CPA2 and CPB are produced by the pancreas. The A forms have slightly different specificities, with CPA1 preferring aliphatic and small aromatic residues, and CPA2 preferring the bulkier aromatic side chains. CPA3 is found in secretory granules of mast cells and functions in inflammatory processes. CPA4 is detected in hormone-regulated tissues, and is thought to play a role in prostate cancer. CPA5 is present in discrete regions of pituitary and other tissues, and cleaves aliphatic C-terminal residues. CPA6 is highly expressed in embryonic brain and optic muscle, suggesting that it may play a specific role in cell migration and axonal guidance. CPU (also called CPB2) is produced and secreted by the liver as the inactive precursor, PCPU, commonly referred to as thrombin-activatable fibrinolysis inhibitor (TAFI). Little is known about CPO but it has been suggested to have specificity for acidic residues.


Pssm-ID: 349467 [Multi-domain]  Cd Length: 297  Bit Score: 57.85  E-value: 6.59e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126920918 296 HDYKAMRKLMKQVNEQCPNITRIYSIGKSHQGLKLYVMEMSDQPGEHElGEPEVRYVAGMHGNEALgrelLLLLMQFLCH 375
Cdd:cd06248    2 HSLDEIDEYLDGLAEESPDVVTVVEGGYTFEGRPIKYVRIRSTNSEDT-SKPTIMIEGGINPREWI----SPPAALYAIH 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126920918 376 EFLRGDPRVTRLLTETRIHLLPSMNPDGYE---TAFR--RGSELVGWAEGRWNHQGIDLNHNFAdlntplWEAEDEGLVP 450
Cdd:cd06248   77 KLVEDVETQSDLLNNFDWIILPVANPDGYVfthTNDRewTKNRSTNSNPLGQICFGVNINRNFD------YQWNPVLSSE 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126920918 451 DtvpnhhlPLPTYYTLPNATVAPETWAVIKWM--QRIPFVLSANLHGGELVVSYPFDMTRTpwaareltpTPDEAVFRWL 528
Cdd:cd06248  151 S-------PCSELYAGPSAFSEAESRAIRDILheHGNRIHLYISFHSGGSFILYPWGYDGS---------TSSNARQLHL 214
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 126920918 529 STVYAGtnRAMQDPDRRPchsqdfslY----GSIINGAdwhtVPGSMNDFSYLHTNcFEVTVEL 588
Cdd:cd06248  215 AGVAAA--AAISSNNGRP--------YvvgqSSVLLYR----AAGTSSDYAMGIAG-IDYTYEL 263
M14-like cd06242
Peptidase M14-like domain; uncharacterized subgroup; Peptidase M14-like domain of a ...
347-439 4.56e-08

Peptidase M14-like domain; uncharacterized subgroup; Peptidase M14-like domain of a functionally uncharacterized subgroup of the M14 family of metallocarboxypeptidases (MCPs). The M14 family are zinc-binding carboxypeptidases (CPs) which hydrolyze single, C-terminal amino acids from polypeptide chains, and have a recognition site for the free C-terminal carboxyl group, which is a key determinant of specificity. Two major subfamilies of the M14 family, defined based on sequence and structural homology, are the A/B and N/E subfamilies. Enzymes belonging to the A/B subfamily are normally synthesized as inactive precursors containing preceding signal peptide, followed by an N-terminal pro-region linked to the enzyme; these proenzymes are called procarboxypeptidases. The A/B enzymes can be further divided based on their substrate specificity; Carboxypeptidase A-like (CPA-like) enzymes favor hydrophobic residues while carboxypeptidase B-like (CPB-like) enzymes only cleave the basic residues lysine or arginine. The A forms have slightly different specificities, with Carboxypeptidase A1 (CPA1) preferring aliphatic and small aromatic residues, and CPA2 preferring the bulky aromatic side chains. Enzymes belonging to the N/E subfamily enzymes are not produced as inactive precursors and instead rely on their substrate specificity and subcellular compartmentalization to prevent inappropriate cleavages. They contain an extra C-terminal transthyretin-like domain, thought to be involved in folding or formation of oligomers. MCPs can also be classified based on their involvement in specific physiological processes; the pancreatic MCPs participate only in alimentary digestion and include carboxypeptidase A and B (A/B subfamily), while others, namely regulatory MCPs or the N/E subfamily, are involved in more selective reactions, mainly in non-digestive tissues and fluids, acting on blood coagulation/fibrinolysis, inflammation and local anaphylaxis, pro-hormone and neuropeptide processing, cellular response and others. Another MCP subfamily, is that of succinylglutamate desuccinylase /aspartoacylase, which hydrolyzes N-acetyl-L-aspartate (NAA), and deficiency in which is the established cause of Canavan disease. Another subfamily (referred to as subfamily C) includes an exceptional type of activity in the MCP family, that of dipeptidyl-peptidase activity of gamma-glutamyl-(L)-meso-diaminopimelate peptidase I which is involved in bacterial cell wall metabolism.


Pssm-ID: 349461 [Multi-domain]  Cd Length: 220  Bit Score: 54.23  E-value: 4.56e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126920918 347 PEVRYVAGMHGNEALGRELLLLLMQFLCheflrGDPRVTRLLTETRIHLLPSMNPDGYEtAFRRGselvgwaegrwNHQG 426
Cdd:cd06242    2 PTVLLVGQQHGNEPAGREAALALARDLA-----FGDDARELLEKVNVLVVPRANPDGRA-ANTRG-----------NANG 64
                         90
                 ....*....|...
gi 126920918 427 IDLNHNFADLNTP 439
Cdd:cd06242   65 VDLNRDHLLLSTP 77
M14_CPA6 cd03872
Peptidase M14 carboxypeptidase subfamily A/B-like; Carboxypeptidase A6 subgroup; ...
295-510 3.93e-06

Peptidase M14 carboxypeptidase subfamily A/B-like; Carboxypeptidase A6 subgroup; Carboxypeptidase (CP) A6 (CPA6, also known as CPAH; EC 3.4.17.1), belongs to the carboxypeptidase A/B subfamily of the M14 family of metallocarboxypeptidases (MCPs). The M14 family are zinc-binding CPs which hydrolyze single, C-terminal amino acids from polypeptide chains, and have a recognition site for the free C-terminal carboxyl group, which is a key determinant of specificity. CPA6 prefers large hydrophobic C-terminal amino acids as well as histidine, while peptides with a penultimate glycine or proline are very poorly cleaved. Several neuropeptides are processed by CPA6, including Met- and Leu-enkephalin, angiotensin I, and neurotensin. CPA6 converts enkephalin and neurotensin into forms known to be inactive toward their receptors, but converts inactive angiotensin I into the biologically active angiotensin II. Thus, CPA6 plays a possible role in the regulation of neuropeptides in the extracellular environment within the olfactory bulb where it is highly expressed. It is also broadly expressed in embryonic tissue, being found in neuronal tissues, bone, skin as well as the lateral rectus eye muscle. A disruption in the CPA6 gene is linked to Duane syndrome, a defect in the abducens nerve/lateral rectus muscle connection.


Pssm-ID: 349444 [Multi-domain]  Cd Length: 300  Bit Score: 49.21  E-value: 3.93e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126920918 295 HHDYKAMRKLMKQVNEQCPNITRIYSIGKSHQGLKLYVMEMSDQPGEHelgEPEVRYVAGMHGNEALGrellLLLMQFLC 374
Cdd:cd03872    2 YHSLEEIESWMFYMNKTHSDLVHMFSIGKSYEGRSLYVLKLGKRSRSY---KKAVWIDCGIHAREWIG----PAFCQWFV 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126920918 375 HEFL---RGDPRVTRLLTETRIHLLPSMNPDGYETA-----FRRGSELvgwAEGRWNHQGIDLNHNfadlntplWEAE-- 444
Cdd:cd03872   75 KEAInsyQTDPAMKKMLNQLYFYVMPVFNVDGYHYSwtndrFWRKTRS---KNSRFQCRGVDANRN--------WKVKwc 143
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126920918 445 DEGlvpdtvPNHHlPLPTYYTLPNATVAPETWAVIKWM----QRIPFVLSANLHGGELVVSYPFDMTRTP 510
Cdd:cd03872  144 DEG------ASLH-PCDDTYCGPFPESEPEVKAVAQFLrkhrKHVRAYLSFHAYAQMLLYPYSYKYATIP 206
M14-like cd06238
Peptidase M14-like domain; uncharacterized subgroup; Peptidase M14-like domain of a ...
356-485 4.28e-06

Peptidase M14-like domain; uncharacterized subgroup; Peptidase M14-like domain of a functionally uncharacterized subgroup of the M14 family of metallocarboxypeptidases (MCPs). The M14 family are zinc-binding carboxypeptidases (CPs) which hydrolyze single, C-terminal amino acids from polypeptide chains, and have a recognition site for the free C-terminal carboxyl group, which is a key determinant of specificity. Two major subfamilies of the M14 family, defined based on sequence and structural homology, are the A/B and N/E subfamilies. Enzymes belonging to the A/B subfamily are normally synthesized as inactive precursors containing preceding signal peptide, followed by an N-terminal pro-region linked to the enzyme; these proenzymes are called procarboxypeptidases. The A/B enzymes can be further divided based on their substrate specificity; Carboxypeptidase A-like (CPA-like) enzymes favor hydrophobic residues while carboxypeptidase B-like (CPB-like) enzymes only cleave the basic residues lysine or arginine. The A forms have slightly different specificities, with Carboxypeptidase A1 (CPA1) preferring aliphatic and small aromatic residues, and CPA2 preferring the bulky aromatic side chains. Enzymes belonging to the N/E subfamily enzymes are not produced as inactive precursors and instead rely on their substrate specificity and subcellular compartmentalization to prevent inappropriate cleavage. They contain an extra C-terminal transthyretin-like domain, thought to be involved in folding or formation of oligomers. MCPs can also be classified based on their involvement in specific physiological processes; the pancreatic MCPs participate only in alimentary digestion and include carboxypeptidase A and B (A/B subfamily), while others, namely regulatory MCPs or the N/E subfamily, are involved in more selective reactions, mainly in non-digestive tissues and fluids, acting on blood coagulation/fibrinolysis, inflammation and local anaphylaxis, pro-hormone and neuropeptide processing, cellular response and others. Another MCP subfamily, is that of succinylglutamate desuccinylase /aspartoacylase, which hydrolyzes N-acetyl-L-aspartate (NAA), and deficiency in which is the established cause of Canavan disease. Another subfamily (referred to as subfamily C) includes an exceptional type of activity in the MCP family, that of dipeptidyl-peptidase activity of gamma-glutamyl-(L)-meso-diaminopimelate peptidase I which is involved in bacterial cell wall metabolism.


Pssm-ID: 349457  Cd Length: 217  Bit Score: 48.51  E-value: 4.28e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126920918 356 HGNEALGRELLlllMQFLCHEFLRGDPRVTRLLTETRIHLLPSMNPDGYEtAF------RRGSELVG----------WAE 419
Cdd:cd06238   11 HGNELSGSEAA---MQVAYHLAAGQDEATRALLENTVIVIDPNQNPDGRE-RFvnwfnqNRGAVGDPdpqsmehnepWPG 86
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 126920918 420 GRWNHQGIDLNHNFADLNTPlweaEDEGLV-------PDTVPNHHL--PLPTYYTLPNA-TVAPETWA-VIKWMQRI 485
Cdd:cd06238   87 GRTNHYLFDLNRDWLAQTQP----ESRARAaaihrwrPQVVVDFHEmgTDQTFFFPPPAePVNPLIPRqQLRWTKRF 159
M14_REP34-like cd06231
Peptidase M14-like domain similar to rapid encystment phenotype 34 (REP34); This family ...
353-434 4.85e-05

Peptidase M14-like domain similar to rapid encystment phenotype 34 (REP34); This family includes Francisella tularensis protein rapid encystment phenotype 34 (REP34) which is a zinc-containing monomeric protein demonstrating carboxypeptidase B-like activity. REP34 possesses a novel topology with its substrate binding pocket deviating from the canonical M14 peptidases with a possible catalytic role for a conserved tyrosine and distinct S1' recognition site. Thus, REP34, identified as an active carboxypeptidase and a potential key F. tularensis effector protein, may help elucidate a mechanistic understanding of F. tularensis infection of phagocytic cells. A functionally uncharacterized subgroup of the M14 family of metallocarboxypeptidases (MCPs). The M14 family are zinc-binding carboxypeptidases (CPs) which hydrolyze single, C-terminal amino acids from polypeptide chains, and have a recognition site for the free C-terminal carboxyl group, which is a key determinant of specificity. Two major subfamilies of the M14 family, defined based on sequence and structural homology, are the A/B and N/E subfamilies. Enzymes belonging to the A/B subfamily are normally synthesized as inactive precursors containing preceding signal peptide, followed by an N-terminal pro-region linked to the enzyme; these proenzymes are called procarboxypeptidases. The A/B enzymes can be further divided based on their substrate specificity; Carboxypeptidase A-like (CPA-like) enzymes favor hydrophobic residues while carboxypeptidase B-like (CPB-like) enzymes only cleave the basic residues lysine or arginine. The A forms have slightly different specificities, with Carboxypeptidase A1 (CPA1) preferring aliphatic and small aromatic residues, and CPA2 preferring the bulky aromatic side chains. Enzymes belonging to the N/E subfamily enzymes are not produced as inactive precursors and instead rely on their substrate specificity and subcellular compartmentalization to prevent inappropriate cleavages. They contain an extra C-terminal transthyretin-like domain, thought to be involved in folding or formation of oligomers. MCPs can also be classified based on their involvement in specific physiological processes; the pancreatic MCPs participate only in alimentary digestion and include carboxypeptidase A and B (A/B subfamily), while others, namely regulatory MCPs or the N/E subfamily, are involved in more selective reactions, mainly in non-digestive tissues and fluids, acting on blood coagulation/fibrinolysis, inflammation and local anaphylaxis, pro-hormone and neuropeptide processing, cellular response and others. Another MCP subfamily, is that of succinylglutamate desuccinylase /aspartoacylase, which hydrolyzes N-acetyl-L-aspartate (NAA), and deficiency in which is the established cause of Canavan disease. Another subfamily (referred to as subfamily C) includes an exceptional type of activity in the MCP family, that of dipeptidyl-peptidase activity of gamma-glutamyl-(L)-meso-diaminopimelate peptidase I which is involved in bacterial cell wall metabolism.


Pssm-ID: 349450 [Multi-domain]  Cd Length: 239  Bit Score: 45.38  E-value: 4.85e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126920918 353 AGMHGNEALGRELllllmqfLCHeFLRGDPRvtRLLTETRIHLLPSMNPDGYEtafrRGSelvgwaegRWNHQGIDLNHN 432
Cdd:cd06231   49 AGIHGDEPAGVEA-------LLR-FLESLAE--KYLRRVNLLVLPCVNPWGFE----RNT--------RENADGIDLNRS 106

                 ..
gi 126920918 433 FA 434
Cdd:cd06231  107 FL 108
M14_PaCCP-like cd06234
Peptidase M14-like domain of ATP/GTP binding proteins and cytosolic carboxypeptidases similar ...
311-556 2.18e-04

Peptidase M14-like domain of ATP/GTP binding proteins and cytosolic carboxypeptidases similar to Pseudomonas aerugnosa CCP (PaCCP); A bacterial subgroup of the Peptidase M14-like domain of Nna-1 (Nervous system Nuclear protein induced by Axotomy), also known as ATP/GTP binding protein (AGTPBP-1) and cytosolic carboxypeptidase (CCP)-like proteins. This subgroup includes PaCCP from Pseudomonas aeruginosa, a carboxypeptidase homologous to M14D subfamily of human CCPs. Structural complexes with well-known inhibitors of metallocarboxypeptidases indicate that PaCCP might only possess C-terminal hydrolase activity against cellular substrates of particular specificity. The Peptidase M14 family of metallocarboxypeptidases are zinc-binding carboxypeptidases (CPs) which hydrolyze single, C-terminal amino acids from polypeptide chains, and have a recognition site for the free C-terminal carboxyl group, which is a key determinant of specificity. Nna1-like proteins are active metallopeptidases that are thought to act on cytosolic proteins (such as alpha-tubulin in eukaryotes) to remove a C-terminal tyrosine. Nna1-like proteins from the different phyla are highly diverse, but they all contain a unique N-terminal conserved domain right before the CP domain. It has been suggested that this N-terminal domain might act as a folding domain.


Pssm-ID: 349453 [Multi-domain]  Cd Length: 256  Bit Score: 43.71  E-value: 2.18e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126920918 311 QCPNITRIYSIGKSHQGLKLYVMEMSDQPGehelGEPEVRYVAGMHGNEALGrellLLLMQFLCHEFL-RGDPRVTRLLT 389
Cdd:cd06234   14 QASPGVRLEVLGQTLDGRDIDLLTIGDPGT----GKKKVWIIARQHPGETMA----EWFMEGLLDRLLdEDDPVSRALLE 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126920918 390 ETRIHLLPSMNPDGyetAFRrgselvGWAegRWNHQGIDLNHNFADlntplweaedeglvpdtvpnhhlplptyytlPNA 469
Cdd:cd06234   86 KAVFYVVPNMNPDG---SVR------GNL--RTNAAGVNLNREWAN-------------------------------PSL 123
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126920918 470 TVAPETWAVIKWMQRIPFVLSANLHGGElVVSYPFdmtrtpWAARELTPTPDEAVFRWLSTVYAGTNRAmqDPDRRPCHS 549
Cdd:cd06234  124 ERSPEVFAVRQAMDATGVDFFLDVHGDE-ALPYNF------IAGAEGIPSWTPRLAALEAAFKAALAAA--SPDFQTEHG 194

                 ....*..
gi 126920918 550 QDFSLYG 556
Cdd:cd06234  195 YPPDAPG 201
M14-CPA-like cd06227
Peptidase M14 carboxypeptidase A-like domain; uncharacterized subfamily; A functionally ...
352-523 2.73e-04

Peptidase M14 carboxypeptidase A-like domain; uncharacterized subfamily; A functionally uncharacterized subgroup of the M14 family of metallocarboxypeptidases (MCPs). The M14 family are zinc-binding carboxypeptidases (CPs) which hydrolyze single, C-terminal amino acids from polypeptide chains, and have a recognition site for the free C-terminal carboxyl group, which is a key determinant of specificity. Two major subfamilies of the M14 family, defined based on sequence and structural homology, are the A/B and N/E subfamilies. Enzymes belonging to the A/B subfamily are normally synthesized as inactive precursors containing preceding signal peptide, followed by an N-terminal pro-region linked to the enzyme; these proenzymes are called procarboxypeptidases. The A/B enzymes can be further divided based on their substrate specificity; Carboxypeptidase A-like (CPA-like) enzymes favor hydrophobic residues while carboxypeptidase B-like (CPB-like) enzymes only cleave the basic residues lysine or arginine. The A forms have slightly different specificities, with Carboxypeptidase A1 (CPA1) preferring aliphatic and small aromatic residues, and CPA2 preferring the bulky aromatic side chains. Enzymes belonging to the N/E subfamily enzymes are not produced as inactive precursors and instead rely on their substrate specificity and subcellular compartmentalization to prevent inappropriate cleavages. They contain an extra C-terminal transthyretin-like domain, thought to be involved in folding or formation of oligomers. MCPs can also be classified based on their involvement in specific physiological processes; the pancreatic MCPs participate only in alimentary digestion and include carboxypeptidase A and B (A/B subfamily), while others, namely regulatory MCPs or the N/E subfamily, are involved in more selective reactions, mainly in non-digestive tissues and fluids, acting on blood coagulation/fibrinolysis, inflammation and local anaphylaxis, pro-hormone and neuropeptide processing, cellular response and others. Another MCP subfamily, is that of succinylglutamate desuccinylase /aspartoacylase, which hydrolyzes N-acetyl-L-aspartate (NAA), and deficiency in which is the established cause of Canavan disease. Another subfamily (referred to as subfamily C) includes an exceptional type of activity in the MCP family, that of dipeptidyl-peptidase activity of gamma-glutamyl-(L)-meso-diaminopimelate peptidase I which is involved in bacterial cell wall metabolism.


Pssm-ID: 349446 [Multi-domain]  Cd Length: 224  Bit Score: 43.03  E-value: 2.73e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126920918 352 VAGMHGNEALGRELLLLLMQFLCHE-----FLRGDPRVTRLLTETRIHLLPSMNPDGyetafRRgselvGWAEG----RW 422
Cdd:cd06227    7 VFGEHARELISVESALRLLRQLCGGlqepaASALRELAREILDNVELKIIPNANPDG-----RR-----LVESGdycwRG 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126920918 423 NHQGIDLNHNFADlntpLWEAEDEGLVPDTVPNHHlPLPtyytlpnatvAPETWAVIKWMQRIPFVLSANLHGGELVVsY 502
Cdd:cd06227   77 NENGVDLNRNWGV----DWGKGEKGAPSEEYPGPK-PFS----------EPETRALRDLALSFKPHAFVSVHSGMLAI-Y 140
                        170       180
                 ....*....|....*....|.
gi 126920918 503 pfdmtrTPWAARELTPTPDEA 523
Cdd:cd06227  141 ------TPYAYSASVPRPNRA 155
M14-like cd06239
Peptidase M14-like domain; uncharacterized subgroup; Peptidase M14-like domain of a ...
355-439 5.36e-04

Peptidase M14-like domain; uncharacterized subgroup; Peptidase M14-like domain of a functionally uncharacterized subgroup of the M14 family of metallocarboxypeptidases (MCPs). The M14 family are zinc-binding carboxypeptidases (CPs) which hydrolyze single, C-terminal amino acids from polypeptide chains, and have a recognition site for the free C-terminal carboxyl group, which is a key determinant of specificity. Two major subfamilies of the M14 family, defined based on sequence and structural homology, are the A/B and N/E subfamilies. Enzymes belonging to the A/B subfamily are normally synthesized as inactive precursors containing preceding signal peptide, followed by an N-terminal pro-region linked to the enzyme; these proenzymes are called procarboxypeptidases. The A/B enzymes can be further divided based on their substrate specificity; Carboxypeptidase A-like (CPA-like) enzymes favor hydrophobic residues while carboxypeptidase B-like (CPB-like) enzymes only cleave the basic residues lysine or arginine. The A forms have slightly different specificities, with Carboxypeptidase A1 (CPA1) preferring aliphatic and small aromatic residues, and CPA2 preferring the bulky aromatic side chains. Enzymes belonging to the N/E subfamily enzymes are not produced as inactive precursors and instead rely on their substrate specificity and subcellular compartmentalization to prevent inappropriate cleavage. They contain an extra C-terminal transthyretin-like domain, thought to be involved in folding or formation of oligomers. MCPs can also be classified based on their involvement in specific physiological processes; the pancreatic MCPs participate only in alimentary digestion and include carboxypeptidase A and B (A/B subfamily), while others, namely regulatory MCPs or the N/E subfamily, are involved in more selective reactions, mainly in non-digestive tissues and fluids, acting on blood coagulation/fibrinolysis, inflammation and local anaphylaxis, pro-hormone and neuropeptide processing, cellular response and others. Another MCP subfamily, is that of succinylglutamate desuccinylase /aspartoacylase, which hydrolyzes N-acetyl-L-aspartate (NAA), and deficiency in which is the established cause of Canavan disease. Another subfamily (referred to as subfamily C) includes an exceptional type of activity in the MCP family, that of dipeptidyl-peptidase activity of gamma-glutamyl-(L)-meso-diaminopimelate peptidase I which is involved in bacterial cell wall metabolism.


Pssm-ID: 349458 [Multi-domain]  Cd Length: 194  Bit Score: 41.63  E-value: 5.36e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126920918 355 MHGNEALGRELLLLLMQFLCheflRGDPRVTRLLTETRIHLLPSMNPDGYEtAFRRgselvgwaegrWNHQGIDLNHNFA 434
Cdd:cd06239    8 MHGNEPTGTEALLDLISYLR----RERQEFEKILERLTLVAIPMLNPDGAE-LFTR-----------HNAEGIDLNRDAR 71

                 ....*
gi 126920918 435 DLNTP 439
Cdd:cd06239   72 ALQTP 76
M14_CPA cd03870
Peptidase M14 carboxypeptidase subfamily A/B-like; Carboxypeptidase A subgroup; Peptidase M14 ...
313-433 8.73e-04

Peptidase M14 carboxypeptidase subfamily A/B-like; Carboxypeptidase A subgroup; Peptidase M14 Carboxypeptidase (CP) A (CPA) belongs to the A/B subfamily of the M14 family of metallocarboxypeptidases (MCPs). The M14 family are zinc-binding CPs which hydrolyze single, C-terminal amino acids from polypeptide chains, and have a recognition site for the free C-terminal carboxyl group, which is a key determinant of specificity. CPA enzymes generally favor hydrophobic residues. A/B subfamily enzymes are normally synthesized as inactive precursors containing preceding signal peptide, followed by a globular N-terminal pro-region linked to the enzyme; these proenzymes are called procarboxypeptidases. The procarboxypeptidase A (PCPA) is produced by the exocrine pancreas and stored as a stable zymogen in the pancreatic granules until secretion into the digestive tract occurs. This subfamily includes CPA1, CPA2 and CPA4 forms. Within these A forms, there are slightly different specificities, with CPA1 preferring aliphatic and small aromatic residues, and CPA2 preferring the bulkier aromatic side chains. CPA4, detected in hormone-regulated tissues, is thought to play a role in prostate cancer.


Pssm-ID: 349442 [Multi-domain]  Cd Length: 301  Bit Score: 42.04  E-value: 8.73e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126920918 313 PNITRIYSIGKSHQGLKLYVMEMSDQPGEhelgEPEVRYVAGMHGNEALGRELLLLLMQFLCHEFLRgDPRVTRLLTETR 392
Cdd:cd03870   24 PNLVSKLQIGSSFENRPMYVLKFSTGGEE----RPAIWIDAGIHSREWVTQASAIWTAEKIVSDYGK-DPSITSILDTMD 98
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 126920918 393 IHLLPSMNPDGYetAFRRGSELVgWAEGRWNHQ-----GIDLNHNF 433
Cdd:cd03870   99 IFLEIVTNPDGY--VFTHSSNRL-WRKTRSVNPgslciGVDPNRNW 141
M14_Nna1-like cd06237
Peptidase M14-like domain of ATP/GTP binding proteins and cytosolic carboxypeptidases; ...
297-430 1.05e-03

Peptidase M14-like domain of ATP/GTP binding proteins and cytosolic carboxypeptidases; uncharacterized bacterial subgroup; A bacterial subgroup of the Peptidase M14-like domain of Nna-1 (Nervous system Nuclear protein induced by Axotomy), also known as ATP/GTP binding protein (AGTPBP-1) and cytosolic carboxypeptidase (CCP),-like proteins. The Peptidase M14 family of metallocarboxypeptidases are zinc-binding carboxypeptidases (CPs) which hydrolyze single, C-terminal amino acids from polypeptide chains, and have a recognition site for the free C-terminal carboxyl group, which is a key determinant of specificity. Nna1-like proteins are active metallopeptidases that are thought to act on cytosolic proteins (such as alpha-tubulin in eukaryotes) to remove a C-terminal tyrosine. Nna1-like proteins from the different phyla are highly diverse, but they all contain a unique N-terminal conserved domain right before the CP domain. It has been suggested that this N-terminal domain might act as a folding domain.


Pssm-ID: 349456 [Multi-domain]  Cd Length: 239  Bit Score: 41.40  E-value: 1.05e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126920918 297 DYKA-MRKLMKQvneqcPNITRIySIGKSHQGLKLYVMEMSDqPGEHE----LGE---PEVR-YVAGMHGNEALGRELLl 367
Cdd:cd06237    2 DYDAwIDSLAKK-----PFVKRS-TIGKSVEGRPIEALTIGN-PDSKElvvlLGRqhpPEVTgALAMQAFVETLLADTE- 73
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 126920918 368 llmqfLCHEFLRgdprvtrlltETRIHLLPSMNPDGyetafrrgselVgwAEGRWNHQ--GIDLN 430
Cdd:cd06237   74 -----LAKAFRA----------RFRVLVVPLLNPDG-----------V--DLGHWRHNagGVDLN 110
M14-like cd03862
Peptidase M14-like domain; uncharacterized subfamily; A functionally uncharacterized subgroup ...
347-513 2.77e-03

Peptidase M14-like domain; uncharacterized subfamily; A functionally uncharacterized subgroup of the M14 family of metallocarboxypeptidases (MCPs). The M14 family are zinc-binding carboxypeptidases (CPs) which hydrolyze single, C-terminal amino acids from polypeptide chains, and have a recognition site for the free C-terminal carboxyl group, which is a key determinant of specificity. Two major subfamilies of the M14 family, defined based on sequence and structural homology, are the A/B and N/E subfamilies. Enzymes belonging to the A/B subfamily are normally synthesized as inactive precursors containing preceding signal peptide, followed by an N-terminal pro-region linked to the enzyme; these proenzymes are called procarboxypeptidases. The A/B enzymes can be further divided based on their substrate specificity; Carboxypeptidase A-like (CPA-like) enzymes favor hydrophobic residues while carboxypeptidase B-like (CPB-like) enzymes only cleave the basic residues lysine or arginine. The A forms have slightly different specificities, with Carboxypeptidase A1 (CPA1) preferring aliphatic and small aromatic residues, and CPA2 preferring the bulky aromatic side chains. Enzymes belonging to the N/E subfamily enzymes are not produced as inactive precursors and instead rely on their substrate specificity and subcellular compartmentalization to prevent inappropriate cleavages. They contain an extra C-terminal transthyretin-like domain, thought to be involved in folding or formation of oligomers. MCPs can also be classified based on their involvement in specific physiological processes; the pancreatic MCPs participate only in alimentary digestion and include carboxypeptidase A and B (A/B subfamily), while others, namely regulatory MCPs or the N/E subfamily, are involved in more selective reactions, mainly in non-digestive tissues and fluids, acting on blood coagulation/fibrinolysis, inflammation and local anaphylaxis, pro-hormone and neuropeptide processing, cellular response and others. Another MCP subfamily, is that of succinylglutamate desuccinylase /aspartoacylase, which hydrolyzes N-acetyl-L-aspartate (NAA), and deficiency in which is the established cause of Canavan disease. Another subfamily (referred to as subfamily C) includes an exceptional type of activity in the MCP family, that of dipeptidyl-peptidase activity of gamma-glutamyl-(L)-meso-diaminopimelate peptidase I which is involved in bacterial cell wall metabolism.


Pssm-ID: 349434  Cd Length: 245  Bit Score: 40.10  E-value: 2.77e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126920918 347 PEVRYVAGMHGNEALGRELLlllMQFLCHEFLRG--DPRVTRLLTETRIHLLPSMNPDGYetafrrgselvgWAEGRWNH 424
Cdd:cd03862    1 PVVGLVGGVHGLERIGTQVI---LAFLRSLLARLkwDKLLQELLEEVRLVVIPIVNPGGM------------ALKTRSNP 65
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126920918 425 QGIDLNHNfADLNTPlweaedeGLVPDTVPNH----HLPlptyYTLPNATVAPETWAVIKWMQRI----PFVLSANLHGG 496
Cdd:cd03862   66 NGVDLMRN-APVEAV-------EKVPFLVGGQrispHLP----WYRGRNGLETESQALIRYVNEHllesKMSISLDCHSG 133
                        170       180
                 ....*....|....*....|
gi 126920918 497 ELVVS---YPFDMTRTPWAA 513
Cdd:cd03862  134 FGLVDriwFPYAHTTEPFPN 153
M14-like cd06241
Peptidase M14-like domain; uncharacterized subgroup; Peptidase M14-like domain of a ...
353-439 3.51e-03

Peptidase M14-like domain; uncharacterized subgroup; Peptidase M14-like domain of a functionally uncharacterized subgroup of the M14 family of metallocarboxypeptidases (MCPs). The M14 family are zinc-binding carboxypeptidases (CPs) which hydrolyze single, C-terminal amino acids from polypeptide chains, and have a recognition site for the free C-terminal carboxyl group, which is a key determinant of specificity. Two major subfamilies of the M14 family, defined based on sequence and structural homology, are the A/B and N/E subfamilies. Enzymes belonging to the A/B subfamily are normally synthesized as inactive precursors containing preceding signal peptide, followed by an N-terminal pro-region linked to the enzyme; these proenzymes are called procarboxypeptidases. The A/B enzymes can be further divided based on their substrate specificity; Carboxypeptidase A-like (CPA-like) enzymes favor hydrophobic residues while carboxypeptidase B-like (CPB-like) enzymes only cleave the basic residues lysine or arginine. The A forms have slightly different specificities, with Carboxypeptidase A1 (CPA1) preferring aliphatic and small aromatic residues, and CPA2 preferring the bulky aromatic side chains. Enzymes belonging to the N/E subfamily enzymes are not produced as inactive precursors and instead rely on their substrate specificity and subcellular compartmentalization to prevent inappropriate cleavage. They contain an extra C-terminal transthyretin-like domain, thought to be involved in folding or formation of oligomers. MCPs can also be classified based on their involvement in specific physiological processes; the pancreatic MCPs participate only in alimentary digestion and include carboxypeptidase A and B (A/B subfamily), while others, namely regulatory MCPs or the N/E subfamily, are involved in more selective reactions, mainly in non-digestive tissues and fluids, acting on blood coagulation/fibrinolysis, inflammation and local anaphylaxis, pro-hormone and neuropeptide processing, cellular response and others. Another MCP subfamily, is that of succinylglutamate desuccinylase /aspartoacylase, which hydrolyzes N-acetyl-L-aspartate (NAA), and deficiency in which is the established cause of Canavan disease. Another subfamily (referred to as subfamily C) includes an exceptional type of activity in the MCP family, that of dipeptidyl-peptidase activity of gamma-glutamyl-(L)-meso-diaminopimelate peptidase I which is involved in bacterial cell wall metabolism.


Pssm-ID: 349460 [Multi-domain]  Cd Length: 215  Bit Score: 39.55  E-value: 3.51e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126920918 353 AGMHGNEALGRELllllMQFLCHEFLRGDprVTRLLTETRIHLLPSMNPDGYETAFR------RGSELVGWaegRWNHQG 426
Cdd:cd06241    8 AGIHPGEVEGKEA----SLMLLRDIAQGG--KKHLLDNLILLFVPIFNADGNDRRSKgnrpnqNGPLEVGW---RTNAQG 78
                         90
                 ....*....|...
gi 126920918 427 IDLNHNFADLNTP 439
Cdd:cd06241   79 LDLNRDFMKLEAP 91
M14_CPT_like cd06226
Peptidase M14-like domain of an uncharacterized group of Peptidase M14 Carboxypeptidase T (CPT) ...
381-434 4.26e-03

Peptidase M14-like domain of an uncharacterized group of Peptidase M14 Carboxypeptidase T (CPT)-like proteins; Peptidase M14-like domain of an uncharacterized group of Peptidase M14 Carboxypeptidase T (CPT)-like proteins. This group belongs to the M14 family of metallocarboxypeptidases (MCPs). The M14 family are zinc-binding CPs which hydrolyze single, C-terminal amino acids from polypeptide chains, and have a recognition site for the free C-terminal carboxyl group, which is a key determinant of specificity. CPT exhibits dual-substrate specificity by cleaving C-terminal hydrophobic amino acid residues and C-terminal positively charged residues. However, CPT does not belong to this CPT-like group.


Pssm-ID: 349445 [Multi-domain]  Cd Length: 267  Bit Score: 39.74  E-value: 4.26e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 126920918 381 DPRVTRLLTETRIHLLPSMNPDGYETA----FRRGSELVGWAEGRWNHQGIDLNHNFA 434
Cdd:cd06226   52 DADATWLLDYTELHLVPQVNPDGRKIAetglLWRKNTNTTPCPASSPTYGVDLNRNSS 109
M14_CPB2 cd06246
Peptidase M14 carboxypeptidase subfamily A/B-like; Carboxypeptidase B2 subgroup; Peptidase M14 ...
294-434 4.95e-03

Peptidase M14 carboxypeptidase subfamily A/B-like; Carboxypeptidase B2 subgroup; Peptidase M14 Carboxypeptidase (CP) B2 (CPB2, also known as plasma carboxypeptidase B, carboxypeptidase U, and CPU), belongs to the carboxpeptidase A/B subfamily of the M14 family of metallocarboxypeptidases (MCPs). The M14 family are zinc-binding CPs which hydrolyze single, C-terminal amino acids from polypeptide chains, and have a recognition site for the free C-terminal carboxyl group, which is a key determinant of specificity. CPB2 enzyme displays B-like activity; it only cleaves the basic residues lysine or arginine. It is produced and secreted by the liver as the inactive precursor, procarboxypeptidase U or PCPB2, commonly referred to as thrombin-activatable fibrinolysis inhibitor (TAFI). It circulates in plasma as a zymogen bound to plasminogen, and the active enzyme, TAFIa, inhibits fibrinolysis. It is highly regulated, increased TAFI concentrations are thought to increase the risk of thrombosis and coronary artery disease by reducing fibrinolytic activity while low TAFI levels have been correlated with chronic liver disease.


Pssm-ID: 349465 [Multi-domain]  Cd Length: 300  Bit Score: 39.79  E-value: 4.95e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126920918 294 RHHDYKAMRKLMKQVNEQCPNITRIYSIGKSHQGLKLYVMEMSDQpgehelgEPEVRYVAGMH-GNEALGRELLLLLMQF 372
Cdd:cd06246    4 QYHSLNEIYSWIEFITERHPDMLTKIHIGSSFEKYPLYVLKVSGK-------EQTAKNAIWIDcGIHAREWISPAFCLWF 76
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 126920918 373 LCH--EFLRGDPRVTRLLTETRIHLLPSMNPDGYETAFRRGSElvgWAEGRWNHQ-----GIDLNHNFA 434
Cdd:cd06246   77 IGHasYFYGIIGQHTNLLNLVDFYVMPVVNVDGYDYSWKKNRM---WRKNRSKHAnnrciGTDLNRNFD 142
CarbopepD_reg_2 pfam13715
CarboxypepD_reg-like domain; This domain family is found in bacteria, archaea and eukaryotes, ...
621-696 8.43e-03

CarboxypepD_reg-like domain; This domain family is found in bacteria, archaea and eukaryotes, and is approximately 90 amino acids in length. The family is found in association with pfam07715 and pfam00593.


Pssm-ID: 433425 [Multi-domain]  Cd Length: 88  Bit Score: 36.03  E-value: 8.43e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 126920918  621 IAGVVRDKDTELGIADAVISVDGINHDVTTAWGGDY-WRLLTPGDYMVTASAEGYHTVTRScrVTFEEG-PVPCNFRL 696
Cdd:pfam13715   1 ISGTVVDENTGEPLPGATVYVKGTTKGTVTDADGNFeLKNLPAGTYTLVVSFVGYKTQEKK--VTVSNDnTLDVNFLL 76
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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