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Conserved domains on  [gi|767944945|ref|XP_011513464|]
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adipocyte enhancer-binding protein 1 isoform X1 [Homo sapiens]

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 ...
538-877 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: 624.16  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767944945  538 HHSYKDMRQLMKVVNEECPTITRTYSLGKSSRGLKIYAMEISDNPGEHELGEPEFRYTAGIHGNEVLGRELLLLLMQYLC 617
Cdd:cd03869     1 HHNYKDMRQLMKVVNEMCPNITRIYNIGKSYQGLKLYAMEISDNPGEHEVGEPEFRYVAGAHGNEVLGRELLLLLMQFLC 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767944945  618 REYRDGNPRVRSLVQDTRIHLVPSLNPDGYEVAAQMGSEFGNWALGLWTEEGFDIFEDFPDLNSVLWGAEERKWVPYRVP 697
Cdd:cd03869    81 QEYLAGNPRIRHLVEETRIHLLPSVNPDGYEKAYEAGSELGGWSLGRWTSDGIDINHNFPDLNSLLWEAEDRKWVPRKVP 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767944945  698 NNNLPIPERYLSPDATVSTEVRAIIAWMEKNPFVLGANLNGGERLVSYPYDMARTPtqeqllaaamaaargedeDEVSEA 777
Cdd:cd03869   161 NHHIPIPEWYLSENATVAPETRAVIAWMEKIPFVLGGNLQGGELVVSYPYDMTRTP------------------WKTQEY 222
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767944945  778 QETPDHAIFRWLAISFASAHLTLTEPYRGGCQAQDYTGGMGIVNGAKWNPRTGTINDFSYLHTNCLELSFYLGCDKFPHE 857
Cdd:cd03869   223 TPTPDDHVFRWLAYSYASTHRLMTDASRRPCHTEDFQKEDGTVNGASWHTVAGSMNDFSYLHTNCFELSIYLGCDKFPHE 302
                         330       340
                  ....*....|....*....|
gi 767944945  858 SELPREWENNKEALLTFMEQ 877
Cdd:cd03869   303 SELPEEWENNRESLLVFMEQ 322
FA58C cd00057
Coagulation factor 5/8 C-terminal domain, discoidin domain; Cell surface-attached ...
360-513 1.15e-56

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: 192.18  E-value: 1.15e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767944945  360 PPIGMESHRiEDNQIRASSMLRHGLGAQRGRLNmqtgateddyYDGAWCAEDDARTQWIEVDTRRTTRFTGVITQGRDSS 439
Cdd:cd00057     1 EPLGMESGL-ADDQITASSSYSSGWEASRARLN----------SDNAWTPAVNDPPQWLQVDLGKTRRVTGIQTQGRKGG 69
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767944945  440 IHDDFVTTFFVGFSNDSQTWVMYTNGYEEMTFHGNVDKDTPVLSELPEPVVARFIRIYPLTWNGSLCMRLEVLG 513
Cdd:cd00057    70 GSSEWVTSYKVQYSLDGETWTTYKDKGEEKVFTGNSDGSTPVTNDFPPPIVARYIRILPTTWNGNISLRLELYG 143
Peptidase_M14NE-CP-C_like cd11308
Peptidase associated domain: C-terminal domain of M14 N/E carboxypeptidase; putative folding, ...
881-956 1.51e-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: 129.57  E-value: 1.51e-35
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767944945  881 GIKGVVTDEQGIPIANATISVSGINHGVKTASGGDYWRILNPGEYRVTAHAEGYTPSAKTCNVDYDIGATQCNFIL 956
Cdd:cd11308     1 GIKGFVTDATGNPIANATISVEGINHDVTTAKDGDYWRLLLPGTYNVTASAPGYQPVTKTVTVPNNFSATVVNFTL 76
 
Name Accession Description Interval E-value
M14_CPX_like cd03869
Peptidase M14 carboxypeptidase subfamily N/E-like; Carboxypeptidase X subgroup; Peptidase ...
538-877 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: 624.16  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767944945  538 HHSYKDMRQLMKVVNEECPTITRTYSLGKSSRGLKIYAMEISDNPGEHELGEPEFRYTAGIHGNEVLGRELLLLLMQYLC 617
Cdd:cd03869     1 HHNYKDMRQLMKVVNEMCPNITRIYNIGKSYQGLKLYAMEISDNPGEHEVGEPEFRYVAGAHGNEVLGRELLLLLMQFLC 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767944945  618 REYRDGNPRVRSLVQDTRIHLVPSLNPDGYEVAAQMGSEFGNWALGLWTEEGFDIFEDFPDLNSVLWGAEERKWVPYRVP 697
Cdd:cd03869    81 QEYLAGNPRIRHLVEETRIHLLPSVNPDGYEKAYEAGSELGGWSLGRWTSDGIDINHNFPDLNSLLWEAEDRKWVPRKVP 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767944945  698 NNNLPIPERYLSPDATVSTEVRAIIAWMEKNPFVLGANLNGGERLVSYPYDMARTPtqeqllaaamaaargedeDEVSEA 777
Cdd:cd03869   161 NHHIPIPEWYLSENATVAPETRAVIAWMEKIPFVLGGNLQGGELVVSYPYDMTRTP------------------WKTQEY 222
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767944945  778 QETPDHAIFRWLAISFASAHLTLTEPYRGGCQAQDYTGGMGIVNGAKWNPRTGTINDFSYLHTNCLELSFYLGCDKFPHE 857
Cdd:cd03869   223 TPTPDDHVFRWLAYSYASTHRLMTDASRRPCHTEDFQKEDGTVNGASWHTVAGSMNDFSYLHTNCFELSIYLGCDKFPHE 302
                         330       340
                  ....*....|....*....|
gi 767944945  858 SELPREWENNKEALLTFMEQ 877
Cdd:cd03869   303 SELPEEWENNRESLLVFMEQ 322
Peptidase_M14 pfam00246
Zinc carboxypeptidase;
544-870 1.24e-67

Zinc carboxypeptidase;


Pssm-ID: 459730 [Multi-domain]  Cd Length: 287  Bit Score: 229.11  E-value: 1.24e-67
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767944945   544 MRQLMKVVNEECPTITRTYSLGKSSRGLKIYAMEISDNPGEHELGEPEFRYTAGIHGNEVLGRELLLLLMQYLCREYRDg 623
Cdd:pfam00246    1 IEAWLDALAARYPDLVRLVSIGKSVEGRPLKVLKISSGPGEHNPGKPAVFIDGGIHAREWIGPATALYLIHQLLTNYGR- 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767944945   624 NPRVRSLVQDTRIHLVPSLNPDGYEVAAQMgseFGNWALGLW-----TEEGFDIFEDFPDlnsvLWGAeerkwvpyrVPN 698
Cdd:pfam00246   80 DPEITELLDDTDIYILPVVNPDGYEYTHTT---DRLWRKNRSnangsSCIGVDLNRNFPD----HWNE---------VGA 143
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767944945   699 NNLPIPERYLSPDATVSTEVRAIIAWM-EKNPFVLGANLNGGERLVSYPYDMARTptqeqllaaamaaargededevsea 777
Cdd:pfam00246  144 SSNPCSETYRGPAPFSEPETRAVADFIrSKKPFVLYISLHSYSQVLLYPYGYTRD------------------------- 198
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767944945   778 QETPDHAIFRWLAISFASAHLTLTepyrggcQAQDYTggMGIVNGAKWNPRTGTINDFSYLHTNC-LELSFYLGCDK--- 853
Cdd:pfam00246  199 EPPPDDEELKSLARAAAKALQKMV-------RGTSYT--YGITNGATIYPASGGSDDWAYGRLGIkYSYTIELRDTGryg 269
                          330
                   ....*....|....*...
gi 767944945   854 -FPHESELPREWENNKEA 870
Cdd:pfam00246  270 fLLPASQIIPTAEETWEA 287
Zn_pept smart00631
Zn_pept domain;
538-863 1.23e-58

Zn_pept domain;


Pssm-ID: 214748 [Multi-domain]  Cd Length: 277  Bit Score: 203.34  E-value: 1.23e-58
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767944945    538 HHSYKDMRQLMKVVNEECPTITRTYSLGKSSRGLKIYAMEISDNPGEhelGEPEFRYTAGIHGNEVLGRELLLLLMQYLC 617
Cdd:smart00631    1 YHSYEEIEAWLKELAARYPDLVRLVSIGKSVEGRPIWVLKISNGGSH---DKPAIFIDAGIHAREWIGPATALYLINQLL 77
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767944945    618 REYRDgNPRVRSLVQDTRIHLVPSLNPDGYEVAAQmGSEFgnWALGLW---TEEGFDIFEDFPDlnsvLWGAeerkwvpy 694
Cdd:smart00631   78 ENYGR-DPRVTNLLDKTDIYIVPVLNPDGYEYTHT-GDRL--WRKNRSpnsNCRGVDLNRNFPF----HWGE-------- 141
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767944945    695 rvpnNNLPIPERYLSPDATVSTEVRAIIAWMEKN-PFVLGANLNGGERLVSYPYDMARTPTQeqllaaamaaargEDEDE 773
Cdd:smart00631  142 ----TGNPCSETYAGPSPFSEPETKAVRDFIRSNrRFKLYIDLHSYSQLILYPYGYTKNDLP-------------PNVDD 204
                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767944945    774 vseaqetpDHAIFRWLAISFASAHLTltepyrggcqaqDYTGgmGIVNGAKWnPRTGTINDFSYLHTN-CLELSFYLGCD 852
Cdd:smart00631  205 --------LDAVAKALAKALASVHGT------------RYTY--GISNGAIY-PASGGSDDWAYGVLGiPFSFTLELRDD 261
                           330
                    ....*....|....*.
gi 767944945    853 -----KFPHESELPRE 863
Cdd:smart00631  262 grygfLLPPSQIIPTG 277
FA58C cd00057
Coagulation factor 5/8 C-terminal domain, discoidin domain; Cell surface-attached ...
360-513 1.15e-56

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: 192.18  E-value: 1.15e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767944945  360 PPIGMESHRiEDNQIRASSMLRHGLGAQRGRLNmqtgateddyYDGAWCAEDDARTQWIEVDTRRTTRFTGVITQGRDSS 439
Cdd:cd00057     1 EPLGMESGL-ADDQITASSSYSSGWEASRARLN----------SDNAWTPAVNDPPQWLQVDLGKTRRVTGIQTQGRKGG 69
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767944945  440 IHDDFVTTFFVGFSNDSQTWVMYTNGYEEMTFHGNVDKDTPVLSELPEPVVARFIRIYPLTWNGSLCMRLEVLG 513
Cdd:cd00057    70 GSSEWVTSYKVQYSLDGETWTTYKDKGEEKVFTGNSDGSTPVTNDFPPPIVARYIRILPTTWNGNISLRLELYG 143
FA58C smart00231
Coagulation factor 5/8 C-terminal domain, discoidin domain; Cell surface-attached ...
358-514 1.83e-39

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: 143.03  E-value: 1.83e-39
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767944945    358 KCP-PIGMEShrieDNQIRASSmlrHGLGAQRGRLNMQTgateddyyDGAWCAEDDARTQWIEVDTRRTTRFTGVITQGR 436
Cdd:smart00231    1 PCNePLGLES----DSQITASS---SYWAAKIARLNGGS--------DGGWCPAKNDLPPWIQVDLGRLRTVTGVITGRR 65
                            90       100       110       120       130       140       150
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767944945    437 DSsiHDDFVTTFFVgFSNDSQTWVMYtNGYEEMTFHGNVDKDTPVLSELPEPVVARFIRIYPLTWNGSLCMRLEVLGC 514
Cdd:smart00231   66 HG--NGDWVTYKLE-YSDDGVNWTTY-KDGNSKVFPGNSDAGTVVLNDFPPPIVARYVRILPTGWNGNIILRVELLGC 139
Peptidase_M14NE-CP-C_like cd11308
Peptidase associated domain: C-terminal domain of M14 N/E carboxypeptidase; putative folding, ...
881-956 1.51e-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: 129.57  E-value: 1.51e-35
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767944945  881 GIKGVVTDEQGIPIANATISVSGINHGVKTASGGDYWRILNPGEYRVTAHAEGYTPSAKTCNVDYDIGATQCNFIL 956
Cdd:cd11308     1 GIKGFVTDATGNPIANATISVEGINHDVTTAKDGDYWRLLLPGTYNVTASAPGYQPVTKTVTVPNNFSATVVNFTL 76
F5_F8_type_C pfam00754
F5/8 type C domain; This domain is also known as the discoidin (DS) domain family.
373-511 5.03e-27

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: 107.15  E-value: 5.03e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767944945   373 QIRASSMlRHGLGAQRGRLnmqtgateDDYYDGAWCAEDDARTQWIEVDTRRTTRFTGVITQGRDSSiHDDFVTTFFVGF 452
Cdd:pfam00754    1 QITASSS-YSGEGPAAAAL--------DGDPNTAWSAWSGDDPQWIQVDLGKPKKITGVVTQGRQDG-SNGYVTSYKIEY 70
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767944945   453 SNDSQTWVMYTNGyeemTFHGNVDKDTPVLSELPEPVVARFIRIYPLTWNGS--LCMRLEV 511
Cdd:pfam00754   71 SLDGENWTTVKDE----KIPGNNDNNTPVTNTFDPPIKARYVRIVPTSWNGGngIALRAEL 127
MpaA COG2866
Murein tripeptide amidase MpaA [Cell wall/membrane/envelope biogenesis];
537-748 9.84e-19

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


Pssm-ID: 442113 [Multi-domain]  Cd Length: 337  Bit Score: 88.98  E-value: 9.84e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767944945  537 RHHSYKDMRQLMKVVnEECPTITRTYSLGKSSRGLKIYAMEISDNPGehelGEPEFRYTAGIHGNEVLGRELLLLLMQYL 616
Cdd:COG2866    18 RYYTYEELLALLAKL-AAASPLVELESIGKSVEGRPIYLLKIGDPAE----GKPKVLLNAQQHGNEWTGTEALLGLLEDL 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767944945  617 CREYrdgNPRVRSLVQDTRIHLVPSLNPDGYEVaaqmgsefgNW---ALGLwteegfdifedfpDLNsvlwgaeeRKWvp 693
Cdd:COG2866    93 LDNY---DPLIRALLDNVTLYIVPMLNPDGAER---------NTrtnANGV-------------DLN--------RDW-- 137
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 767944945  694 yrvpnnnlpiPERYLSpdatvSTEVRAIIAWMEKNPFVLGANLNGGERLVSYPYD 748
Cdd:COG2866   138 ----------PAPWLS-----EPETRALRDLLDEHDPDFVLDLHGQGELFYWFVG 177
CarboxypepD_reg pfam13620
Carboxypeptidase regulatory-like domain;
881-940 3.08e-14

Carboxypeptidase regulatory-like domain;


Pssm-ID: 433354 [Multi-domain]  Cd Length: 81  Bit Score: 68.85  E-value: 3.08e-14
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767944945   881 GIKGVVTDEQGIPIANATISV----SGINHGVKTASGGDYW-RILNPGEYRVTAHAEGYTPSAKT 940
Cdd:pfam13620    1 TISGTVTDPSGAPVPGATVTVtntdTGTVRTTTTDADGRYRfPGLPPGTYTVTVSAPGFKTATRT 65
 
Name Accession Description Interval E-value
M14_CPX_like cd03869
Peptidase M14 carboxypeptidase subfamily N/E-like; Carboxypeptidase X subgroup; Peptidase ...
538-877 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: 624.16  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767944945  538 HHSYKDMRQLMKVVNEECPTITRTYSLGKSSRGLKIYAMEISDNPGEHELGEPEFRYTAGIHGNEVLGRELLLLLMQYLC 617
Cdd:cd03869     1 HHNYKDMRQLMKVVNEMCPNITRIYNIGKSYQGLKLYAMEISDNPGEHEVGEPEFRYVAGAHGNEVLGRELLLLLMQFLC 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767944945  618 REYRDGNPRVRSLVQDTRIHLVPSLNPDGYEVAAQMGSEFGNWALGLWTEEGFDIFEDFPDLNSVLWGAEERKWVPYRVP 697
Cdd:cd03869    81 QEYLAGNPRIRHLVEETRIHLLPSVNPDGYEKAYEAGSELGGWSLGRWTSDGIDINHNFPDLNSLLWEAEDRKWVPRKVP 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767944945  698 NNNLPIPERYLSPDATVSTEVRAIIAWMEKNPFVLGANLNGGERLVSYPYDMARTPtqeqllaaamaaargedeDEVSEA 777
Cdd:cd03869   161 NHHIPIPEWYLSENATVAPETRAVIAWMEKIPFVLGGNLQGGELVVSYPYDMTRTP------------------WKTQEY 222
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767944945  778 QETPDHAIFRWLAISFASAHLTLTEPYRGGCQAQDYTGGMGIVNGAKWNPRTGTINDFSYLHTNCLELSFYLGCDKFPHE 857
Cdd:cd03869   223 TPTPDDHVFRWLAYSYASTHRLMTDASRRPCHTEDFQKEDGTVNGASWHTVAGSMNDFSYLHTNCFELSIYLGCDKFPHE 302
                         330       340
                  ....*....|....*....|
gi 767944945  858 SELPREWENNKEALLTFMEQ 877
Cdd:cd03869   303 SELPEEWENNRESLLVFMEQ 322
M14_CP_N-E_like cd03858
Peptidase M14 carboxypeptidase subfamily N/E-like; Carboxypeptidase (CP) N/E-like subfamily of ...
538-877 4.03e-117

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: 363.90  E-value: 4.03e-117
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767944945  538 HHSYKDMRQLMKVVNEECPTITRTYSLGKSSRGLKIYAMEISDNPGEHELGEPEFRYTAGIHGNEVLGRELLLLLMQYLC 617
Cdd:cd03858     1 HHNYEELEEFLKQVAKRYPNITRLYSIGKSVEGRELWVLEISDNPGVHEPGEPEFKYVANMHGNEVVGRELLLLLAEYLC 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767944945  618 REYRdGNPRVRSLVQDTRIHLVPSLNPDGYEVAAQMGSefgNWALGLWTEEGFDIFEDFPDLNSVLWgaeerkwvpyrvP 697
Cdd:cd03858    81 ENYG-KDPRVTQLVNSTRIHIMPSMNPDGYEKAQEGDC---GGLIGRNNANGVDLNRNFPDQFFQVY------------S 144
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767944945  698 NNNLPIPerylspdatvstEVRAIIAWMEKNPFVLGANLNGGERLVSYPYDMARTPTQeqllaaamaaargededevSEA 777
Cdd:cd03858   145 DNNPRQP------------ETKAVMNWLESIPFVLSANLHGGALVANYPYDDTRSGKS-------------------TEY 193
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767944945  778 QETPDHAIFRWLAISFASAHLTLTEPYRGGCQAQDYTGGmGIVNGAKWNPRTGTINDFSYLHTNCLELSFYLGCDKFPHE 857
Cdd:cd03858   194 SPSPDDAVFRMLARSYSDAHPTMSMGKPCCCDDDENFPN-GITNGAAWYSVSGGMQDFNYLHTNCFEITLELGCCKYPPA 272
                         330       340
                  ....*....|....*....|
gi 767944945  858 SELPREWENNKEALLTFMEQ 877
Cdd:cd03858   273 SELPKYWEDNKRSLLNFLEQ 292
M14_CPN cd03864
Peptidase M14 carboxypeptidase subfamily N/E-like; Carboxypeptidase N subgroup; Peptidase M14 ...
538-877 2.65e-98

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: 314.56  E-value: 2.65e-98
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767944945  538 HHSYKDMRQLMKVVNEECPTITRTYSLGKSSRGLKIYAMEISDNPGEHELGEPEFRYTAGIHGNEVLGRELLLLLMQYLC 617
Cdd:cd03864     1 HHRYDDLVRALYAVQNECPYITRIYSIGRSVEGRHLYVLEFSDNPGIHEPLEPEFKYVGNMHGNEVLGRELLIQLSEFLC 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767944945  618 REYRDGNPRVRSLVQDTRIHLVPSLNPDGYEVAAQMGSEFGNWALGLWTEEGFDIFEDFPDLNSVLWGAEErkwvpYRVP 697
Cdd:cd03864    81 EEYRNGNERITRLIQDTRIHILPSMNPDGYEVAARQGPEFNGYLVGRNNANGVDLNRNFPDLNTLMYYNEK-----YGGP 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767944945  698 NNNLPIPERYLSpdaTVSTEVRAIIAWMEKNPFVLGANLNGGERLVSYPYDMARTPtqeqllaaamaAARGEDEdevSEA 777
Cdd:cd03864   156 NHHLPLPDNWKS---QVEPETLAVIQWMQNYNFVLSANLHGGAVVANYPYDKSREP-----------RVRGFRR---TAY 218
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767944945  778 QETPDHAIFRWLAISFASAHLTLTEpyrgGCQAQDYTGGmGIVNGAKWNPRTGTINDFSYLHTNCLELSFYLGCDKFPHE 857
Cdd:cd03864   219 SPTPDDKLFQKLAKTYSYAHGWMHK----GWNCGDYFDE-GITNGASWYSLSKGMQDFNYLHTNCFEITLELSCDKFPPE 293
                         330       340
                  ....*....|....*....|
gi 767944945  858 SELPREWENNKEALLTFMEQ 877
Cdd:cd03864   294 EELEREWLGNREALISYMEQ 313
M14_CPZ cd03867
Peptidase M14 carboxypeptidase subfamily N/E-like; Carboxypeptidase Z subgroup; Peptidase ...
538-876 7.68e-97

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: 310.66  E-value: 7.68e-97
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767944945  538 HHSYKDMRQLMKVVNEECPTITRTYSLGKSSRGLKIYAMEISDNPGEHELGEPEFRYTAGIHGNEVLGRELLLLLMQYLC 617
Cdd:cd03867     1 HHSYSQMVRVLKKTAARCAHIARTYSIGRSFEGKDLLVIEFSSNPGQHELLEPEVKYIGNMHGNEVVGREMLIYLAQYLC 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767944945  618 REYRDGNPRVRSLVQDTRIHLVPSLNPDGYEVAAQMGSEFGNWALGLWTEEGFDIFEDFPDLNSVLWGAEERKWvpYRVp 697
Cdd:cd03867    81 SEYLLGNPRIQTLINTTRIHLLPSMNPDGYEVAAEEGAGYNGWTSGRQNAQNLDLNRNFPDLTSEAYRLARTRG--ARL- 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767944945  698 nNNLPIPERYLspDATVSTEVRAIIAWMEKNPFVLGANLNGGERLVSYPYDMARTPTQEQLLaaamaaargededevsea 777
Cdd:cd03867   158 -DHIPIPQSYW--WGKVAPETKAVMKWMRSIPFVLSASLHGGDLVVSYPYDFSKHPLEEKMF------------------ 216
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767944945  778 QETPDHAIFRWLAISFASAHLTLTEPYRGGCQAQDYTGGmGIVNGAKWNPRTGTINDFSYLHTNCLELSFYLGCDKFPHE 857
Cdd:cd03867   217 SPTPDEKMFKLLAKAYADAHPMMSDRSENRCGGNFLKRG-GIINGAEWYSFTGGMADFNYLHTNCFEVTVELGCEKFPPE 295
                         330
                  ....*....|....*....
gi 767944945  858 SELPREWENNKEALLTFME 876
Cdd:cd03867   296 EELYTIWQENKEALLNFME 314
M14_CPE cd03865
Peptidase M14 carboxypeptidase subfamily N/E-like; Carboxypeptidase E subgroup; Peptidase M14 ...
538-877 1.61e-85

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: 279.94  E-value: 1.61e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767944945  538 HHSYKDMRQLMKVVNEECPTITRTYSLGKSSRGLKIYAMEISDNPGEHELGEPEFRYTAGIHGNEVLGRELLLLLMQYLC 617
Cdd:cd03865     1 YHRYPELREALVSVWLQCPAISRIYTVGRSFEGRELLVIEVSDNPGEHEPGEPEFKYVGNMHGNEAVGRELLIFLAQYLC 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767944945  618 REYRDGNPRVRSLVQDTRIHLVPSLNPDGYEVAAQMGSEFGNWALGLWTEEGFDIFEDFPDLNSVLWGAEERKWvpyrvP 697
Cdd:cd03865    81 NEYQKGNETIINLIHSTRIHIMPSLNPDGFEKAASQPGELKDWFVGRSNAQGIDLNRNFPDLDRIVYVNEKEGG-----P 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767944945  698 NNNL-PIPERYLSPDATVSTEVRAIIAWMEKNPFVLGANLNGGERLVSYPYDMARTPTQEqllaaamaaargededevsE 776
Cdd:cd03865   156 NNHLlKNMKKAVDQNTKLAPETKAVIHWIMDIPFVLSANLHGGDLVANYPYDETRSGSAH-------------------E 216
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767944945  777 AQETPDHAIFRWLAISFASAHLTLTEPYRGGCQAQDYTGGM--GIVNGAKWNPRTGTINDFSYLHTNCLELSFYLGCDKF 854
Cdd:cd03865   217 YSSCPDDAIFQSLARAYSSLNPAMSDPNRPPCRKNDDDSSFvdGTTNGGAWYSVPGGMQDFNYLSSNCFEITVELSCEKF 296
                         330       340
                  ....*....|....*....|...
gi 767944945  855 PHESELPREWENNKEALLTFMEQ 877
Cdd:cd03865   297 PPEETLKGYWEDNKNSLINYIEQ 319
M14_CPD_I cd03868
Peptidase M14 carboxypeptidase subfamily N/E-like; Carboxypeptidase D, domain I subgroup; The ...
539-877 8.04e-81

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: 266.03  E-value: 8.04e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767944945  539 HSYKDMRQLMKVVNEECPTITRTYSLGKSSRGLKIYAMEISDNPGEHELGEPEFRYTAGIHGNEVLGRELLLLLMQYLCR 618
Cdd:cd03868     2 HNYDELTDLLHKLAETYPNIAKLHSIGKSVQGRELWVLEISDNVNRREPGKPMFKYVANMHGDETVGRQLLIYLAQYLLE 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767944945  619 EY-RDgnPRVRSLVQDTRIHLVPSLNPDGYEvAAQMGSEFG-NWALGLWTEEGFDIFEDFPD-LNSVLWGAEERkwvpyR 695
Cdd:cd03868    82 NYgKD--ERVTRLVNSTDIHLMPSMNPDGFE-NSKEGDCSGdPGYGGRENANNVDLNRNFPDqFEDSDDRLLEG-----R 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767944945  696 VPnnnlpiperylspdatvstEVRAIIAWMEKNPFVLGANLNGGERLVSYPYDMARTptqeqllaaamaaargedEDEVS 775
Cdd:cd03868   154 QP-------------------ETLAMMKWIVENPFVLSANLHGGSVVASYPFDDSPS------------------HIECG 196
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767944945  776 EAQETPDHAIFRWLAISFASAHLTLtePYRGGCQAQDYTGgmGIVNGAKWNPRTGTINDFSYLHTNCLELSFYLGCDKFP 855
Cdd:cd03868   197 VYSKSPDDAVFRHLAHTYADNHPTM--HKGNNCCEDSFKD--GITNGAEWYDVPGGMQDFNYVHSNCFEITLELSCCKYP 272
                         330       340
                  ....*....|....*....|..
gi 767944945  856 HESELPREWENNKEALLTFMEQ 877
Cdd:cd03868   273 PASELPKEWDNNKEALLSYMEQ 294
M14_CPD_II cd03863
Peptidase M14 carboxypeptidase subfamily N/E-like; Carboxypeptidase D, domain II subgroup; The ...
535-877 6.14e-78

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: 258.34  E-value: 6.14e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767944945  535 DFRHHSYKDMRQLMKVVNEECPTITRTYSLGKSSRGLKIYAMEISDNPGEHELGEPEFRYTAGIHGNEVLGRELLLLLMQ 614
Cdd:cd03863     5 DFRHHHFSDMEIFLRRYANEYPSITRLYSVGKSVELRELYVMEISDNPGVHEPGEPEFKYIGNMHGNEVVGRELLLNLIE 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767944945  615 YLCREYrDGNPRVRSLVQDTRIHLVPSLNPDGYEVaAQMGSEFGnwALGLWTEEGFDIFEDFPDlnsvlwgaeerkwvpy 694
Cdd:cd03863    85 YLCKNF-GTDPEVTDLVQNTRIHIMPSMNPDGYEK-SQEGDRGG--TVGRNNSNNYDLNRNFPD---------------- 144
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767944945  695 rvpnnnlpipeRYLSPDATVSTEVRAIIAWMEKNPFVLGANLNGGERLVSYPYDmartptqeqllaaamaaargEDEDEV 774
Cdd:cd03863   145 -----------QFFQITDPPQPETLAVMSWLKTYPFVLSANLHGGSLVVNYPFD--------------------DDEQGL 193
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767944945  775 SEAQETPDHAIFRWLAISFASAHltlTEPYRGG-CQAQDYTGGM--GIVNGAKWNPRTGTINDFSYLHTNCLELSFYLGC 851
Cdd:cd03863   194 ATYSKSPDDAVFQQLALSYSKEN---SKMYQGSpCKELYPNEYFphGITNGAQWYNVPGGMQDWNYLNTNCFEVTIELGC 270
                         330       340
                  ....*....|....*....|....*.
gi 767944945  852 DKFPHESELPREWENNKEALLTFMEQ 877
Cdd:cd03863   271 VKYPKAEELPKYWEQNRRSLLQFIKQ 296
Peptidase_M14 pfam00246
Zinc carboxypeptidase;
544-870 1.24e-67

Zinc carboxypeptidase;


Pssm-ID: 459730 [Multi-domain]  Cd Length: 287  Bit Score: 229.11  E-value: 1.24e-67
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767944945   544 MRQLMKVVNEECPTITRTYSLGKSSRGLKIYAMEISDNPGEHELGEPEFRYTAGIHGNEVLGRELLLLLMQYLCREYRDg 623
Cdd:pfam00246    1 IEAWLDALAARYPDLVRLVSIGKSVEGRPLKVLKISSGPGEHNPGKPAVFIDGGIHAREWIGPATALYLIHQLLTNYGR- 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767944945   624 NPRVRSLVQDTRIHLVPSLNPDGYEVAAQMgseFGNWALGLW-----TEEGFDIFEDFPDlnsvLWGAeerkwvpyrVPN 698
Cdd:pfam00246   80 DPEITELLDDTDIYILPVVNPDGYEYTHTT---DRLWRKNRSnangsSCIGVDLNRNFPD----HWNE---------VGA 143
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767944945   699 NNLPIPERYLSPDATVSTEVRAIIAWM-EKNPFVLGANLNGGERLVSYPYDMARTptqeqllaaamaaargededevsea 777
Cdd:pfam00246  144 SSNPCSETYRGPAPFSEPETRAVADFIrSKKPFVLYISLHSYSQVLLYPYGYTRD------------------------- 198
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767944945   778 QETPDHAIFRWLAISFASAHLTLTepyrggcQAQDYTggMGIVNGAKWNPRTGTINDFSYLHTNC-LELSFYLGCDK--- 853
Cdd:pfam00246  199 EPPPDDEELKSLARAAAKALQKMV-------RGTSYT--YGITNGATIYPASGGSDDWAYGRLGIkYSYTIELRDTGryg 269
                          330
                   ....*....|....*...
gi 767944945   854 -FPHESELPREWENNKEA 870
Cdd:pfam00246  270 fLLPASQIIPTAEETWEA 287
M14_CPM cd03866
Peptidase M14 carboxypeptidase subfamily N/E-like; Carboxypeptidase M subgroup; Peptidase M14 ...
538-877 6.33e-59

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: 204.64  E-value: 6.33e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767944945  538 HHSYKDMRQLMKVVNEECPTITRTYSLGKSSRGLKIYAMEISDNPGEHELGEPEFRYTAGIHGNEVLGRELLLLLMQYLC 617
Cdd:cd03866     1 YHNQEQMETYLKDVNKNYPSITHLHSIGKSVEGRDLWVLVLGRFPTKHRIGIPEFKYVANMHGDEVVGRELLLHLIEFLV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767944945  618 REYRDgNPRVRSLVQDTRIHLVPSLNPDGYEVAAQMGSefgNWALGLWTEEGFDIFEDFPDlnsvlwgAEERKWVPyrvp 697
Cdd:cd03866    81 TSYGS-DPVITRLINSTRIHIMPSMNPDGFEATKKPDC---YYTKGRYNKNGYDLNRNFPD-------AFEENNVQ---- 145
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767944945  698 nnnlpiperylspdatVSTEVRAIIAWMEKNPFVLGANLNGGERLVSYPYDMARTPTQEQllaaamaaargededevSEA 777
Cdd:cd03866   146 ----------------RQPETRAVMDWIKNETFVLSANLHGGALVASYPFDNGNSGTGQL-----------------GYY 192
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767944945  778 QETPDHAIFRWLAISFASAHLTLtepYRG-GC-QAQDYTGgmGIVNGAKWNPRTGTINDFSYLHTNCLELSFYLGCDKFP 855
Cdd:cd03866   193 SVSPDDDVFIYLAKTYSYNHTNM---YKGiECsNSQSFPG--GITNGYQWYPLQGGMQDYNYVWGQCFEITLELSCCKYP 267
                         330       340
                  ....*....|....*....|..
gi 767944945  856 HESELPREWENNKEALLTFMEQ 877
Cdd:cd03866   268 PEETLPQFWNDNRVALIEYIKQ 289
Zn_pept smart00631
Zn_pept domain;
538-863 1.23e-58

Zn_pept domain;


Pssm-ID: 214748 [Multi-domain]  Cd Length: 277  Bit Score: 203.34  E-value: 1.23e-58
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767944945    538 HHSYKDMRQLMKVVNEECPTITRTYSLGKSSRGLKIYAMEISDNPGEhelGEPEFRYTAGIHGNEVLGRELLLLLMQYLC 617
Cdd:smart00631    1 YHSYEEIEAWLKELAARYPDLVRLVSIGKSVEGRPIWVLKISNGGSH---DKPAIFIDAGIHAREWIGPATALYLINQLL 77
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767944945    618 REYRDgNPRVRSLVQDTRIHLVPSLNPDGYEVAAQmGSEFgnWALGLW---TEEGFDIFEDFPDlnsvLWGAeerkwvpy 694
Cdd:smart00631   78 ENYGR-DPRVTNLLDKTDIYIVPVLNPDGYEYTHT-GDRL--WRKNRSpnsNCRGVDLNRNFPF----HWGE-------- 141
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767944945    695 rvpnNNLPIPERYLSPDATVSTEVRAIIAWMEKN-PFVLGANLNGGERLVSYPYDMARTPTQeqllaaamaaargEDEDE 773
Cdd:smart00631  142 ----TGNPCSETYAGPSPFSEPETKAVRDFIRSNrRFKLYIDLHSYSQLILYPYGYTKNDLP-------------PNVDD 204
                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767944945    774 vseaqetpDHAIFRWLAISFASAHLTltepyrggcqaqDYTGgmGIVNGAKWnPRTGTINDFSYLHTN-CLELSFYLGCD 852
Cdd:smart00631  205 --------LDAVAKALAKALASVHGT------------RYTY--GISNGAIY-PASGGSDDWAYGVLGiPFSFTLELRDD 261
                           330
                    ....*....|....*.
gi 767944945    853 -----KFPHESELPRE 863
Cdd:smart00631  262 grygfLLPPSQIIPTG 277
FA58C cd00057
Coagulation factor 5/8 C-terminal domain, discoidin domain; Cell surface-attached ...
360-513 1.15e-56

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: 192.18  E-value: 1.15e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767944945  360 PPIGMESHRiEDNQIRASSMLRHGLGAQRGRLNmqtgateddyYDGAWCAEDDARTQWIEVDTRRTTRFTGVITQGRDSS 439
Cdd:cd00057     1 EPLGMESGL-ADDQITASSSYSSGWEASRARLN----------SDNAWTPAVNDPPQWLQVDLGKTRRVTGIQTQGRKGG 69
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767944945  440 IHDDFVTTFFVGFSNDSQTWVMYTNGYEEMTFHGNVDKDTPVLSELPEPVVARFIRIYPLTWNGSLCMRLEVLG 513
Cdd:cd00057    70 GSSEWVTSYKVQYSLDGETWTTYKDKGEEKVFTGNSDGSTPVTNDFPPPIVARYIRILPTTWNGNISLRLELYG 143
M14_CPD_III cd06245
Peptidase M14 carboxypeptidase subfamily N/E-like; Carboxypeptidase D, domain III subgroup; ...
538-877 1.25e-56

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: 197.67  E-value: 1.25e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767944945  538 HHSYKDMRQLMKVVNEECPTITRTYSLGKSSRGLKIYAMEISDNPGEHELGEPEFRYTAGIHGNEVlGRELLLLLMQYLC 617
Cdd:cd06245     1 YHSYKQLSKFLRGLNSNYPTITNLTSLGQSVEKRDIWVLEIGNKPNESEPSEPKILFVGGIHGNAP-VGTELLLLLAHFL 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767944945  618 REYRDGNPRVRSLVQDTRIHLVPSLNPDGYEVAAQMGSefgNWALGLWTEEGFDIFEDFpdlnsvlwgaeerkwvpyrvp 697
Cdd:cd06245    80 CHNYKKDSAITKLLNRTRIHIVPSLNPDGAEKAEEKKC---TSKIGEKNANGVDLDTDF--------------------- 135
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767944945  698 nnnlpiPERYLSPDATVSTEVRAIIAWMEKNPFVLGANLNGGERLVSYPYDmartptqeqllaaamaaargeDEDEVSEA 777
Cdd:cd06245   136 ------ESNANNRSGAAQPETKAIMDWLKEKDFTLSVALDGGSLVVTYPYD---------------------KPVQTVEN 188
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767944945  778 QETPDHaifrwLAISFASAHLTLTEPYRGGCQAQDYTGGMGIVNGAKWNPRTGTINDFSYLHTNCLELSFYLGCDKFPHE 857
Cdd:cd06245   189 KETLKH-----LAKVYANNHPTMHAGDPGCCSNSDENFTNGVIRASEWHSHKGSMLDFSYKFGSCPEITVYTSCCYFPPA 263
                         330       340
                  ....*....|....*....|
gi 767944945  858 SELPREWENNKEALLTFMEQ 877
Cdd:cd06245   264 EELLTLWAEHKKSLLSMIVE 283
M14_CP_bacteria cd18173
bacterial peptidase M14 carboxypeptidase, uncharacterized; This family contains only bacterial ...
539-877 2.48e-52

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: 185.09  E-value: 2.48e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767944945  539 HSYKDMRQLMKVVNEECPTITRTYSLGKSSRGLKIYAMEISDNPGEHElGEPEFRYTAGIHGNEVLGRELLLLLMQYLCR 618
Cdd:cd18173     5 PTYEEYEAMMQSFAANYPNICRLVSIGTSVQGRKLLALKISDNVNTEE-AEPEFKYTSTMHGDETTGYELMLRLIDYLLT 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767944945  619 EYRDgNPRVRSLVQDTRIHLVPSLNPDGYeVAAQMGSEFGNW---ALGLwteegfdifedfpDLNsvlwgaeeRkwvpyr 695
Cdd:cd18173    84 NYGT-DPRITNLVDNTEIWINPLANPDGT-YAGGNNTVSGATrynANGV-------------DLN--------R------ 134
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767944945  696 vpnnNLPIPERYLSPDATVS-TEVRAIIAWMEKNPFVLGANLNGGERLVSYPYDMARTPtqeqllaaamaaargededev 774
Cdd:cd18173   135 ----NFPDPVDGDHPDGNGWqPETQAMMNFADEHNFVLSANFHGGAEVVNYPWDTWYSR--------------------- 189
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767944945  775 seaqeTPDHAIFRWLAISFASAhltltepyrggCQAQDYTGGM-----GIVNGAKWNPRTGTINDFSYLHTNCLELSFYL 849
Cdd:cd18173   190 -----HPDDDWFQDISREYADT-----------NQANSPPMYMsefnnGITNGYDWYEVYGGRQDYMYYWHGCREVTIEL 253
                         330       340
                  ....*....|....*....|....*...
gi 767944945  850 GCDKFPHESELPREWENNKEALLTFMEQ 877
Cdd:cd18173   254 SNTKWPPASQLPTYWNYNRESLLNYIEQ 281
M14_CP_plant cd18172
Zinc carboxypeptidase, including SOL1, a carboxypeptidase D in plant; This family includes ...
538-872 6.12e-48

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: 172.60  E-value: 6.12e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767944945  538 HHSYKDMRQLMKVVNEECPTITRTYSLGKSSRGLKIYAMEISDNPGEHElGEPEFRYTAGIHGNEVLGRELLLLLMQYLC 617
Cdd:cd18172     1 YHSNAELEDALKAFTRRCGAISRLIVIGSSVNGFPLWALEISDGPGEDE-TEPAFKFVGNMHGDEPVGRELLLRLADWLC 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767944945  618 REYRDGNPRVRSLVQDTRIHLVPSLNPDGYevaAQMGSEFGNwalglwteeGFDIFEDFPDlnsvlwgaeerkwvpyRVP 697
Cdd:cd18172    80 ANYKAKDPLAAKIVENAHLHLVPTMNPDGF---ARRRRNNAN---------NVDLNRDFPD----------------QFF 131
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767944945  698 NNNLPIPERYLSPdatvstEVRAIIAWMEKNPFVLGANLNGGERLVSYPYDmartptqeqllaaamaaargEDEDEVSEA 777
Cdd:cd18172   132 PKNLRNDLAARQP------ETLAVMNWSRSVRFTASANLHEGALVANYPWD--------------------GNADGRTKY 185
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767944945  778 QETPDHAIFRWLAISFASAHLTLTEPyrggcqaQDYTGgmGIVNGAKWNPRTGTINDFSYLHTNCLELSFYLGCDKFPHE 857
Cdd:cd18172   186 SASPDDATFRRLASVYAQAHPNMAKS-------KEFPG--GITNGAQWYPLYGGMQDWNYLHTGCMDLTLEVNDNKWPPE 256
                         330
                  ....*....|....*
gi 767944945  858 SELPREWENNKEALL 872
Cdd:cd18172   257 DRLVQIWAEHRKAML 271
FA58C smart00231
Coagulation factor 5/8 C-terminal domain, discoidin domain; Cell surface-attached ...
358-514 1.83e-39

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: 143.03  E-value: 1.83e-39
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767944945    358 KCP-PIGMEShrieDNQIRASSmlrHGLGAQRGRLNMQTgateddyyDGAWCAEDDARTQWIEVDTRRTTRFTGVITQGR 436
Cdd:smart00231    1 PCNePLGLES----DSQITASS---SYWAAKIARLNGGS--------DGGWCPAKNDLPPWIQVDLGRLRTVTGVITGRR 65
                            90       100       110       120       130       140       150
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767944945    437 DSsiHDDFVTTFFVgFSNDSQTWVMYtNGYEEMTFHGNVDKDTPVLSELPEPVVARFIRIYPLTWNGSLCMRLEVLGC 514
Cdd:smart00231   66 HG--NGDWVTYKLE-YSDDGVNWTTY-KDGNSKVFPGNSDAGTVVLNDFPPPIVARYVRILPTGWNGNIILRVELLGC 139
Peptidase_M14NE-CP-C_like cd11308
Peptidase associated domain: C-terminal domain of M14 N/E carboxypeptidase; putative folding, ...
881-956 1.51e-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: 129.57  E-value: 1.51e-35
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767944945  881 GIKGVVTDEQGIPIANATISVSGINHGVKTASGGDYWRILNPGEYRVTAHAEGYTPSAKTCNVDYDIGATQCNFIL 956
Cdd:cd11308     1 GIKGFVTDATGNPIANATISVEGINHDVTTAKDGDYWRLLLPGTYNVTASAPGYQPVTKTVTVPNNFSATVVNFTL 76
F5_F8_type_C pfam00754
F5/8 type C domain; This domain is also known as the discoidin (DS) domain family.
373-511 5.03e-27

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: 107.15  E-value: 5.03e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767944945   373 QIRASSMlRHGLGAQRGRLnmqtgateDDYYDGAWCAEDDARTQWIEVDTRRTTRFTGVITQGRDSSiHDDFVTTFFVGF 452
Cdd:pfam00754    1 QITASSS-YSGEGPAAAAL--------DGDPNTAWSAWSGDDPQWIQVDLGKPKKITGVVTQGRQDG-SNGYVTSYKIEY 70
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767944945   453 SNDSQTWVMYTNGyeemTFHGNVDKDTPVLSELPEPVVARFIRIYPLTWNGS--LCMRLEV 511
Cdd:pfam00754   71 SLDGENWTTVKDE----KIPGNNDNNTPVTNTFDPPIKARYVRIVPTSWNGGngIALRAEL 127
M14_CPT cd03859
Peptidase M14 Carboxypeptidase T subfamily; Peptidase M14-like domain of carboxypeptidase (CP) ...
539-871 2.07e-23

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: 101.95  E-value: 2.07e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767944945  539 HSYKDMRQLMKVVNEECPTITRTYSLGKSSRGLKIYAMEISDNPGEHElGEPEFRYTAGIHGNEVLGRELLLLLMQYLCR 618
Cdd:cd03859     5 HTYAELVAELDQLAAEYPEITKLISIGKSVEGRPIWAVKISDNPDEDE-DEPEVLFMGLHHAREWISLEVALYFADYLLE 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767944945  619 EYrDGNPRVRSLVQDTRIHLVPSLNPDGYEVAAQMGSEfgnwalGLWTEEGFDIFEDFP-----DLN---SVLWGAEErk 690
Cdd:cd03859    84 NY-GTDPRITNLVDNREIWIIPVVNPDGYEYNRETGGG------RLWRKNRRPNNGNNPgsdgvDLNrnyGYHWGGDN-- 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767944945  691 wvpyrVPNNNLPIPERYLSPDATVSTEVRAIIAWMEKNPFVLGANLNGGERLVSYPYDMARTPTqeqllaaamaaarged 770
Cdd:cd03859   155 -----GGSSPDPSSETYRGPAPFSEPETQAIRDLVESHDFKVAISYHSYGELVLYPWGYTSDAP---------------- 213
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767944945  771 edevseaqeTPDHAIFRWLAISFASahlTLTEPYRGGCQAQDYtggmgivngakwnPRTGTINDFSYLHTNCLELSFYLG 850
Cdd:cd03859   214 ---------TPDEDVFEELAEEMAS---YNGGGYTPQQSSDLY-------------PTNGDTDDWMYGEKGIIAFTPELG 268
                         330       340
                  ....*....|....*....|....
gi 767944945  851 ---CDKFPHESELPREWENNKEAL 871
Cdd:cd03859   269 pefYPFYPPPSQIDPLAEENLPAA 292
MpaA COG2866
Murein tripeptide amidase MpaA [Cell wall/membrane/envelope biogenesis];
537-748 9.84e-19

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


Pssm-ID: 442113 [Multi-domain]  Cd Length: 337  Bit Score: 88.98  E-value: 9.84e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767944945  537 RHHSYKDMRQLMKVVnEECPTITRTYSLGKSSRGLKIYAMEISDNPGehelGEPEFRYTAGIHGNEVLGRELLLLLMQYL 616
Cdd:COG2866    18 RYYTYEELLALLAKL-AAASPLVELESIGKSVEGRPIYLLKIGDPAE----GKPKVLLNAQQHGNEWTGTEALLGLLEDL 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767944945  617 CREYrdgNPRVRSLVQDTRIHLVPSLNPDGYEVaaqmgsefgNW---ALGLwteegfdifedfpDLNsvlwgaeeRKWvp 693
Cdd:COG2866    93 LDNY---DPLIRALLDNVTLYIVPMLNPDGAER---------NTrtnANGV-------------DLN--------RDW-- 137
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 767944945  694 yrvpnnnlpiPERYLSpdatvSTEVRAIIAWMEKNPFVLGANLNGGERLVSYPYD 748
Cdd:COG2866   138 ----------PAPWLS-----EPETRALRDLLDEHDPDFVLDLHGQGELFYWFVG 177
M14-like cd06905
Peptidase M14-like domain; uncharacterized subfamily; A functionally uncharacterized subgroup ...
534-680 2.09e-18

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: 88.44  E-value: 2.09e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767944945  534 LDFRH-HSYKDMRQLMKVVNEECPTITRTYSLGKSSRGLKIYAMEISDNPGEHELGEPEFRYTAGIHGNEVLGRELLLLL 612
Cdd:cd06905     1 LAFDRyYTYAELTARLKALAEAYPNLVRLESIGKSYEGRDIWLLTITNGETGPADEKPALWVDGNIHGNEVTGSEVALYL 80
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767944945  613 MQYLCREYrDGNPRVRSLVQDTRIHLVPSLNPDGYEVAAQMGSEFGNWALGLWTEEGfDIFEDFP-DLN 680
Cdd:cd06905    81 AEYLLTNY-GKDPEITRLLDTRTFYILPRLNPDGAEAYKLKTERSGRSSPRDDDRDG-DGDEDGPeDLN 147
Peptidase_M14_like cd00596
M14 family of metallocarboxypeptidases and related proteins; The M14 family of ...
594-871 5.99e-17

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: 80.97  E-value: 5.99e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767944945  594 YTAGIHGNEVLGRELLLLLMQYLCREYrdGNPRVRSLVQDTRIHLVPSLNPDGYEVAAQMGsefgnwalGLWTEEGFDIF 673
Cdd:cd00596     3 ITGGIHGNEVIGVELALALIEYLLENY--GNDPLKRLLDNVELWIVPLVNPDGFARVIDSG--------GRKNANGVDLN 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767944945  674 EDFPDlnsvLWGAEERKWvpyrvpnnnlPIPERYLSPDATVSTEVRAIIAWMEKNPFVLGANLNGGERLVSYPYdmartp 753
Cdd:cd00596    73 RNFPY----NWGKDGTSG----------PSSPTYRGPAPFSEPETQALRDLAKSHRFDLAVSYHSSSEAILYPY------ 132
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767944945  754 tqeqllaaamaaaRGEDEDEvseaqetPDHAIFRWLAISFASAHLTLTEPYRggcqaqdytggmgivNGAKWNPRTGTIN 833
Cdd:cd00596   133 -------------GYTNEPP-------PDFSEFQELAAGLARALGAGEYGYG---------------YSYTWYSTTGTAD 177
                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 767944945  834 DFSYLHTNCLELSFYLGC-DKFPHESELPREWENNKEAL 871
Cdd:cd00596   178 DWLYGELGILAFTVELGTaDYPLPGTLLDRRLERNLAAL 216
CarboxypepD_reg pfam13620
Carboxypeptidase regulatory-like domain;
881-940 3.08e-14

Carboxypeptidase regulatory-like domain;


Pssm-ID: 433354 [Multi-domain]  Cd Length: 81  Bit Score: 68.85  E-value: 3.08e-14
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767944945   881 GIKGVVTDEQGIPIANATISV----SGINHGVKTASGGDYW-RILNPGEYRVTAHAEGYTPSAKT 940
Cdd:pfam13620    1 TISGTVTDPSGAPVPGATVTVtntdTGTVRTTTTDADGRYRfPGLPPGTYTVTVSAPGFKTATRT 65
M14_CP_A-B_like cd03860
Peptidase M14 carboxypeptidase subfamily A/B-like; The Peptidase M14 Carboxypeptidase (CP) A/B ...
539-648 1.17e-08

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: 57.92  E-value: 1.17e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767944945  539 HSYKDMRQLMKVVNEECPTITRTYSLGKSSRGLKIYAMEISDNPGEHelGEPEFRYTAGIHGNE------VLgrelllLL 612
Cdd:cd03860     2 HPLDDIVQWLDDLAAAFPDNVEIFTIGKSYEGRDITGIHIWGSGGKG--GKPAIVIHGGQHAREwiststVE------YL 73
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 767944945  613 MQYLCREYrDGNPRVRSLVQDTRIHLVPSLNPDGYE 648
Cdd:cd03860    74 AHQLLSGY-GSDATITALLDKFDFYIIPVVNPDGYV 108
M14_Endopeptidase_I cd06229
Peptidase M14 carboxypeptidase family-like domain of Endopeptidase I; Peptidase M14-like ...
594-736 3.97e-07

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: 52.34  E-value: 3.97e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767944945  594 YTAGIHGNEVLGRELLLLLMQYLCREY----RDGNPRVRSLVQDTRIHLVPSLNPDGYEVaAQMGSEFGN--WALGLWTE 667
Cdd:cd06229     3 YNASFHAREYITTLLLMKFIEDYAKAYvnksYIRGKDVGELLNKVTLHIVPMVNPDGVEI-SQNGSNAINpyYLRLVAWN 81
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767944945  668 EGFDIFEDFP------DLN---SVLWGAEERKWVPYrvpnnnlPIPERYLSPDATVSTEVRAIIAWMEKNPFVLGANL 736
Cdd:cd06229    82 KKGTDFTGWKanirgvDLNrnfPAGWEKEKRLGPKA-------PGPRDYPGKEPLSEPETKAMAALTRQNDFDLVLAY 152
CarbopepD_reg_2 pfam13715
CarboxypepD_reg-like domain; This domain family is found in bacteria, archaea and eukaryotes, ...
882-943 6.45e-05

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: 42.58  E-value: 6.45e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767944945   882 IKGVVTDE-QGIPIANATISVSGINHGVKTASGGDY-WRILNPGEYRVTAHAEGYTPSAKTCNV 943
Cdd:pfam13715    1 ISGTVVDEnTGEPLPGATVYVKGTTKGTVTDADGNFeLKNLPAGTYTLVVSFVGYKTQEKKVTV 64
M14_CPT_like cd06226
Peptidase M14-like domain of an uncharacterized group of Peptidase M14 Carboxypeptidase T (CPT) ...
573-652 3.03e-04

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: 43.98  E-value: 3.03e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767944945  573 IYAMEISDNPGEHELGEPEFRYTAGIHGNEVLGRELLLLLMQYLCREYrDGNPRVRSLVQDTRIHLVPSLNPDGYEVAAQ 652
Cdd:cd06226     2 IRALKLTNKQATPPGEKPKFFMMAAIHAREYTTAELVARFAEDLVAGY-GTDADATWLLDYTELHLVPQVNPDGRKIAET 80
M14-like cd06242
Peptidase M14-like domain; uncharacterized subgroup; Peptidase M14-like domain of a ...
594-648 3.43e-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 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: 43.44  E-value: 3.43e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 767944945  594 YTAGIHGNEVLGRELLLLLMQYLCReyrdgNPRVRSLVQDTRIHLVPSLNPDGYE 648
Cdd:cd06242     6 LVGQQHGNEPAGREAALALARDLAF-----GDDARELLEKVNVLVVPRANPDGRA 55
M14_MpaA-like cd06904
Peptidase M14-like domain of Escherichia coli Murein Peptide Amidase A and related proteins; ...
564-729 3.05e-03

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: 40.34  E-value: 3.05e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767944945  564 LGKSSRGLKIYAMEISDNPGEHELgepefrYTAGIHGNEVLGRELLLLLMQYLCREyrdgnprvrSLVQDTRIHLVPSLN 643
Cdd:cd06904     4 YGTSVKGRPILAYKFGPGSRARIL------IIGGIHGDEPEGVSLVEHLLRWLKNH---------PASGDFHIVVVPCLN 68
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767944945  644 PDGYevaaqmgsefgnwALGLWT-EEGFDIFEDFPdlnSVLWGAEERKwvpyrvpnnnlPIPERYLSPDATVS-TEVRAI 721
Cdd:cd06904    69 PDGL-------------AAGTRTnANGVDLNRNFP---TKNWEPDARK-----------PKDPRYYPGPKPASePETRAL 121

                  ....*...
gi 767944945  722 IAWMEKNP 729
Cdd:cd06904   122 VELIERFK 129
M14_CP_insect cd06248
Peptidase M14 carboxypeptidase subfamily A/B-like; This family includes peptidase M14 ...
539-747 7.85e-03

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: 39.75  E-value: 7.85e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767944945  539 HSYKDMRQLMKVVNEECPTITRTYSLGKSSRGLKIYAMEISDNPGEHElGEPEFRYTAGIHGNEVLgrelLLLLMQYLCR 618
Cdd:cd06248     2 HSLDEIDEYLDGLAEESPDVVTVVEGGYTFEGRPIKYVRIRSTNSEDT-SKPTIMIEGGINPREWI----SPPAALYAIH 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767944945  619 EYRDGNPRVRSLVQDTRIHLVPSLNPDGYEVAAQMGSEF-----GNWALGLWTEEGFDIFEDFpdlnsvlwgaeERKWVP 693
Cdd:cd06248    77 KLVEDVETQSDLLNNFDWIILPVANPDGYVFTHTNDREWtknrsTNSNPLGQICFGVNINRNF-----------DYQWNP 145
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 767944945  694 yrVPNNNLPIPERYLSPDATVSTEVRAIIAWMEK--NPFVLGANLNGGERLVSYPY 747
Cdd:cd06248   146 --VLSSESPCSELYAGPSAFSEAESRAIRDILHEhgNRIHLYISFHSGGSFILYPW 199
 
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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