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Conserved domains on  [gi|1021311895|ref|NP_001310502|]
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cytosolic carboxypeptidase 6 isoform 2 [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
M14_AGBL4_like cd06908
Peptidase M14-like domain of ATP/GTP binding protein AGBL-4 and related proteins; Peptidase ...
199-450 0e+00

Peptidase M14-like domain of ATP/GTP binding protein AGBL-4 and related proteins; Peptidase M14-like domain of ATP/GTP binding protein_like (AGBL)-4, and related proteins. The Peptidase M14 family of metallocarboxypeptidases are zinc-binding carboxypeptidases (CPs) which hydrolyze single, C-terminal amino acids from polypeptide chains, and have a recognition site for the free C-terminal carboxyl group, which is a key determinant of specificity. This eukaryotic subgroup includes the human AGBL4 and the mouse cytosolic carboxypeptidase (CCP)-6. ATP/GTP binding protein (AGTPBP-1/Nna1)-like proteins are active metallopeptidases that are thought to act on cytosolic proteins such as alpha-tubulin, to remove a C-terminal tyrosine. Mutations in AGTPBP-1/Nna1 cause Purkinje cell degeneration (pcd). AGTPBP-1/Nna1 however does not belong to this subgroup. AGTPBP-1/Nna1-like proteins from the different phyla are highly diverse, but they all contain a unique N-terminal conserved domain right before the CP domain. It has been suggested that this N-terminal domain might act as a folding domain.


:

Pssm-ID: 349479  Cd Length: 254  Bit Score: 507.22  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021311895 199 DYFFREQLGQSVQQRKLDLLTITSPDNLREG--AEQKVVFITGRVHPGETPSSFVCQGIIDFLVSQHPIACVLREYLVFK 276
Cdd:cd06908     1 NFFTRELLGKSVQQRRLDLLTITDPVNKHLTveKKKKVVFITARVHPGETPSSFVCQGLIDFLVSNHPVAKVLRDHLVFK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021311895 277 IAPMLNPDGVYLGNYRCSLMGFDLNRHWLDPSPWVHPTLHGVKQLIVQMYNDPKTSLEFYIDIHAHSTMMNGFMYGNIFE 356
Cdd:cd06908    81 IVPMLNPDGVFLGNYRCSLMGFDLNRHWHEPSPWAHPTLYAVKNLLRELDNDPTVQLDFYIDIHAHSTLMNGFMYGNIYD 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021311895 357 DEERFQRQAIFPKLLCQNAEDFSYSSTSFNRDAVKAGTGRRFLGGLLDHTSYCYTLEVSFYSYIISGTTAAVPYTEEAYM 436
Cdd:cd06908   161 DVYRFERQAVFPKLLCQNAEDFSLSNTVFNRDPVKAGTGRRFLGGLLDDTANCYTLEVSFYSYRLSDSSSATPYTEEGYM 240
                         250
                  ....*....|....
gi 1021311895 437 KLGRNVARTFLDYY 450
Cdd:cd06908   241 KLGRNMARALLDYY 254
Pepdidase_M14_N super family cl39445
Cytosolic carboxypeptidase N-terminal domain; This entry corresponds to the N-terminal domain ...
46-142 1.68e-10

Cytosolic carboxypeptidase N-terminal domain; This entry corresponds to the N-terminal domain of cytosolic carboxypeptidases. The N-terminal domain folds into a nine-stranded antiparallel beta sandwich. This domain is specific to CCP proteins and is absent in other carboxypeptidases. It has been hypothesized that the N-terminal domain might contribute to folding, might have a regulatory function and/or might be involved in binding other proteins.


The actual alignment was detected with superfamily member pfam18027:

Pssm-ID: 407865  Cd Length: 107  Bit Score: 58.06  E-value: 1.68e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021311895  46 FDACFESGNLGRVDQVSEFEYDLFIRPDTcNPRFRVWFNFTVENVKESQVReivdtfrvvlrviFNIVNFSktKSLYRDG 125
Cdd:pfam18027   1 ISSNFDSGNIEVVSASDPDAIRLRIRPDN-GSEHFQWFYFRVSGARGRPLT-------------FVIENAG--EASYPDG 64
                          90
                  ....*....|....*....
gi 1021311895 126 MAPM--VKSTSRPKWQRLP 142
Cdd:pfam18027  65 WTGYrvVASYDRENWFRVP 83
 
Name Accession Description Interval E-value
M14_AGBL4_like cd06908
Peptidase M14-like domain of ATP/GTP binding protein AGBL-4 and related proteins; Peptidase ...
199-450 0e+00

Peptidase M14-like domain of ATP/GTP binding protein AGBL-4 and related proteins; Peptidase M14-like domain of ATP/GTP binding protein_like (AGBL)-4, and related proteins. The Peptidase M14 family of metallocarboxypeptidases are zinc-binding carboxypeptidases (CPs) which hydrolyze single, C-terminal amino acids from polypeptide chains, and have a recognition site for the free C-terminal carboxyl group, which is a key determinant of specificity. This eukaryotic subgroup includes the human AGBL4 and the mouse cytosolic carboxypeptidase (CCP)-6. ATP/GTP binding protein (AGTPBP-1/Nna1)-like proteins are active metallopeptidases that are thought to act on cytosolic proteins such as alpha-tubulin, to remove a C-terminal tyrosine. Mutations in AGTPBP-1/Nna1 cause Purkinje cell degeneration (pcd). AGTPBP-1/Nna1 however does not belong to this subgroup. AGTPBP-1/Nna1-like proteins from the different phyla are highly diverse, but they all contain a unique N-terminal conserved domain right before the CP domain. It has been suggested that this N-terminal domain might act as a folding domain.


Pssm-ID: 349479  Cd Length: 254  Bit Score: 507.22  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021311895 199 DYFFREQLGQSVQQRKLDLLTITSPDNLREG--AEQKVVFITGRVHPGETPSSFVCQGIIDFLVSQHPIACVLREYLVFK 276
Cdd:cd06908     1 NFFTRELLGKSVQQRRLDLLTITDPVNKHLTveKKKKVVFITARVHPGETPSSFVCQGLIDFLVSNHPVAKVLRDHLVFK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021311895 277 IAPMLNPDGVYLGNYRCSLMGFDLNRHWLDPSPWVHPTLHGVKQLIVQMYNDPKTSLEFYIDIHAHSTMMNGFMYGNIFE 356
Cdd:cd06908    81 IVPMLNPDGVFLGNYRCSLMGFDLNRHWHEPSPWAHPTLYAVKNLLRELDNDPTVQLDFYIDIHAHSTLMNGFMYGNIYD 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021311895 357 DEERFQRQAIFPKLLCQNAEDFSYSSTSFNRDAVKAGTGRRFLGGLLDHTSYCYTLEVSFYSYIISGTTAAVPYTEEAYM 436
Cdd:cd06908   161 DVYRFERQAVFPKLLCQNAEDFSLSNTVFNRDPVKAGTGRRFLGGLLDDTANCYTLEVSFYSYRLSDSSSATPYTEEGYM 240
                         250
                  ....*....|....
gi 1021311895 437 KLGRNVARTFLDYY 450
Cdd:cd06908   241 KLGRNMARALLDYY 254
MpaA COG2866
Murein tripeptide amidase MpaA [Cell wall/membrane/envelope biogenesis];
181-340 2.39e-23

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


Pssm-ID: 442113 [Multi-domain]  Cd Length: 337  Bit Score: 100.92  E-value: 2.39e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021311895 181 YTYTRFQHYLDSLQKRNmDYFFREQLGQSVQQRKLDLLTITSPDNlregaEQKVVFITGRVHPGETPSSFVCQGIIDFLV 260
Cdd:COG2866    20 YTYEELLALLAKLAAAS-PLVELESIGKSVEGRPIYLLKIGDPAE-----GKPKVLLNAQQHGNEWTGTEALLGLLEDLL 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021311895 261 S-QHPIACVLREYLVFKIAPMLNPDGVYLgNYRCSLMGFDLNRHWLDP---SPWVhptlhgvkQLIVQMYNdpKTSLEFY 336
Cdd:COG2866    94 DnYDPLIRALLDNVTLYIVPMLNPDGAER-NTRTNANGVDLNRDWPAPwlsEPET--------RALRDLLD--EHDPDFV 162

                  ....
gi 1021311895 337 IDIH 340
Cdd:COG2866   163 LDLH 166
Peptidase_M14 pfam00246
Zinc carboxypeptidase;
189-415 2.18e-22

Zinc carboxypeptidase;


Pssm-ID: 459730 [Multi-domain]  Cd Length: 287  Bit Score: 96.98  E-value: 2.18e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021311895 189 YLDSLQKRNMDYFFREQLGQSVQQRKLDLLTITSPDNLREGAEqKVVFITGRVHPGETPSSFVCQGIIDFLVS---QHPI 265
Cdd:pfam00246   4 WLDALAARYPDLVRLVSIGKSVEGRPLKVLKISSGPGEHNPGK-PAVFIDGGIHAREWIGPATALYLIHQLLTnygRDPE 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021311895 266 ACVLREYLVFKIAPMLNPDGVYLGNY--------RCSLM-----GFDLNRHWLD------------------PSPWVHPT 314
Cdd:pfam00246  83 ITELLDDTDIYILPVVNPDGYEYTHTtdrlwrknRSNANgssciGVDLNRNFPDhwnevgassnpcsetyrgPAPFSEPE 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021311895 315 LHGVKQLIVQMYNdpktsLEFYIDIHAHSTMMNgFMYGNIF----EDEERFQRQA-IFPKLLCQNAEDFSYSSTSFNRDA 389
Cdd:pfam00246 163 TRAVADFIRSKKP-----FVLYISLHSYSQVLL-YPYGYTRdeppPDDEELKSLArAAAKALQKMVRGTSYTYGITNGAT 236
                         250       260       270
                  ....*....|....*....|....*....|..
gi 1021311895 390 VKAGTgrrflGGLLDHTS------YCYTLEVS 415
Cdd:pfam00246 237 IYPAS-----GGSDDWAYgrlgikYSYTIELR 263
Zn_pept smart00631
Zn_pept domain;
181-353 5.68e-22

Zn_pept domain;


Pssm-ID: 214748 [Multi-domain]  Cd Length: 277  Bit Score: 95.48  E-value: 5.68e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021311895  181 YTYTRFQHYLDSLQKRNMDYFFREQLGQSVQQRKLDLLTITSPDnlreGAEQKVVFITGRVHPGETPSSFVCQGIIDFLV 260
Cdd:smart00631   2 HSYEEIEAWLKELAARYPDLVRLVSIGKSVEGRPIWVLKISNGG----SHDKPAIFIDAGIHAREWIGPATALYLINQLL 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021311895  261 SQH---PIACVLREYLVFKIAPMLNPDGVYLG-----------NYRCSLMGFDLNR----HWLDPSPWVHPTLHG----- 317
Cdd:smart00631  78 ENYgrdPRVTNLLDKTDIYIVPVLNPDGYEYThtgdrlwrknrSPNSNCRGVDLNRnfpfHWGETGNPCSETYAGpspfs 157
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|..
gi 1021311895  318 ------VKQLIVQMYNdpktsLEFYIDIHAHSTMMNgFMYGN 353
Cdd:smart00631 158 epetkaVRDFIRSNRR-----FKLYIDLHSYSQLIL-YPYGY 193
Pepdidase_M14_N pfam18027
Cytosolic carboxypeptidase N-terminal domain; This entry corresponds to the N-terminal domain ...
46-142 1.68e-10

Cytosolic carboxypeptidase N-terminal domain; This entry corresponds to the N-terminal domain of cytosolic carboxypeptidases. The N-terminal domain folds into a nine-stranded antiparallel beta sandwich. This domain is specific to CCP proteins and is absent in other carboxypeptidases. It has been hypothesized that the N-terminal domain might contribute to folding, might have a regulatory function and/or might be involved in binding other proteins.


Pssm-ID: 407865  Cd Length: 107  Bit Score: 58.06  E-value: 1.68e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021311895  46 FDACFESGNLGRVDQVSEFEYDLFIRPDTcNPRFRVWFNFTVENVKESQVReivdtfrvvlrviFNIVNFSktKSLYRDG 125
Cdd:pfam18027   1 ISSNFDSGNIEVVSASDPDAIRLRIRPDN-GSEHFQWFYFRVSGARGRPLT-------------FVIENAG--EASYPDG 64
                          90
                  ....*....|....*....
gi 1021311895 126 MAPM--VKSTSRPKWQRLP 142
Cdd:pfam18027  65 WTGYrvVASYDRENWFRVP 83
 
Name Accession Description Interval E-value
M14_AGBL4_like cd06908
Peptidase M14-like domain of ATP/GTP binding protein AGBL-4 and related proteins; Peptidase ...
199-450 0e+00

Peptidase M14-like domain of ATP/GTP binding protein AGBL-4 and related proteins; Peptidase M14-like domain of ATP/GTP binding protein_like (AGBL)-4, and related proteins. The Peptidase M14 family of metallocarboxypeptidases are zinc-binding carboxypeptidases (CPs) which hydrolyze single, C-terminal amino acids from polypeptide chains, and have a recognition site for the free C-terminal carboxyl group, which is a key determinant of specificity. This eukaryotic subgroup includes the human AGBL4 and the mouse cytosolic carboxypeptidase (CCP)-6. ATP/GTP binding protein (AGTPBP-1/Nna1)-like proteins are active metallopeptidases that are thought to act on cytosolic proteins such as alpha-tubulin, to remove a C-terminal tyrosine. Mutations in AGTPBP-1/Nna1 cause Purkinje cell degeneration (pcd). AGTPBP-1/Nna1 however does not belong to this subgroup. AGTPBP-1/Nna1-like proteins from the different phyla are highly diverse, but they all contain a unique N-terminal conserved domain right before the CP domain. It has been suggested that this N-terminal domain might act as a folding domain.


Pssm-ID: 349479  Cd Length: 254  Bit Score: 507.22  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021311895 199 DYFFREQLGQSVQQRKLDLLTITSPDNLREG--AEQKVVFITGRVHPGETPSSFVCQGIIDFLVSQHPIACVLREYLVFK 276
Cdd:cd06908     1 NFFTRELLGKSVQQRRLDLLTITDPVNKHLTveKKKKVVFITARVHPGETPSSFVCQGLIDFLVSNHPVAKVLRDHLVFK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021311895 277 IAPMLNPDGVYLGNYRCSLMGFDLNRHWLDPSPWVHPTLHGVKQLIVQMYNDPKTSLEFYIDIHAHSTMMNGFMYGNIFE 356
Cdd:cd06908    81 IVPMLNPDGVFLGNYRCSLMGFDLNRHWHEPSPWAHPTLYAVKNLLRELDNDPTVQLDFYIDIHAHSTLMNGFMYGNIYD 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021311895 357 DEERFQRQAIFPKLLCQNAEDFSYSSTSFNRDAVKAGTGRRFLGGLLDHTSYCYTLEVSFYSYIISGTTAAVPYTEEAYM 436
Cdd:cd06908   161 DVYRFERQAVFPKLLCQNAEDFSLSNTVFNRDPVKAGTGRRFLGGLLDDTANCYTLEVSFYSYRLSDSSSATPYTEEGYM 240
                         250
                  ....*....|....
gi 1021311895 437 KLGRNVARTFLDYY 450
Cdd:cd06908   241 KLGRNMARALLDYY 254
M14_AGTPBP-like cd06235
Peptidase M14-like domain of human Nna1/AGTPBP-1, AGBL2 -5, and related proteins; Subgroup of ...
199-448 6.52e-143

Peptidase M14-like domain of human Nna1/AGTPBP-1, AGBL2 -5, and related proteins; Subgroup of the Peptidase M14-like domain of Nna-1 (Nervous system Nuclear protein induced by Axotomy), also known as ATP/GTP binding protein (AGTPBP-1) and cytosolic carboxypeptidase (CCP), and related proteins. The Peptidase M14 family of metallocarboxypeptidases are zinc-binding carboxypeptidases (CPs) which hydrolyze single, C-terminal amino acids from polypeptide chains, and have a recognition site for the free C-terminal carboxyl group, which is a key determinant of specificity. This eukaryotic subgroup includes the human Nna1/AGTPBP-1 and AGBL -2, -3, -4, and -5, and the mouse Nna1/CCP-1 and CCP -2 through -6. Nna1-like proteins are active metallopeptidases that are thought to act on cytosolic proteins such as alpha-tubulin, to remove a C-terminal tyrosine. Nna1 is widely expressed in the developing and adult nervous systems, including cerebellar Purkinje and granule neurons, miral cells of the olfactory bulb and retinal photoreceptors. Nna1 is also induced in axotomized motor neurons. Mutations in Nna1 cause Purkinje cell degeneration (pcd). The Nna1 CP domain is required to prevent the retinal photoreceptor loss and cerebellar ataxia phenotypes of pcd mice, and a functional zinc-binding domain is needed for Nna-1 to support neuron survival in these mice. Nna1-like proteins from the different phyla are highly diverse, but they all contain a unique N-terminal conserved domain right before the CP domain. It has been suggested that this N-terminal domain might act as a folding domain.


Pssm-ID: 349454  Cd Length: 256  Bit Score: 410.70  E-value: 6.52e-143
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021311895 199 DYFFREQLGQSVQQRKLDLLTITSPDNL------REGAEQKVVFITGRVHPGETPSSFVCQGIIDFLVSQHPIACVLREY 272
Cdd:cd06235     1 IYFEREVLCHSLDGRKLDLLTITSPNNKklgpypREFAGKKVVFLSGRVHPGETPASFVMKGFLDFLLSNDPRAQLLREH 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021311895 273 LVFKIAPMLNPDGVYLGNYRCSLMGFDLNRHWLDPSPWVHPTLHGVKQLIVQMYNDPKTSLEFYIDIHAHSTMMNGFMYG 352
Cdd:cd06235    81 FVFKIVPMLNPDGVIRGNYRCSLNGFNLNRHYKNPDPELHPTIYGAKKVIDYLQKTYKRRVLMYCDFHGHSSKSNGFMYG 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021311895 353 NIFEDEERFQRQAIFPKLLCQNAEDFSYSST-SFNRDAVKAGTGRRFLGGLLDHtSYCYTLEVSFYSYIISGTTAAVPYT 431
Cdd:cd06235   161 NSFPDTVQFHWNMVFPKILSLNAPDFFSSSCcSFGVMKSKEGTGRVVFGRRLIH-SHSYTLESTFFSNNRGNIDGACGYT 239
                         250
                  ....*....|....*..
gi 1021311895 432 EEAYMKLGRNVARTFLD 448
Cdd:cd06235   240 EENLEDLGYSVASTLLD 256
M14_AGBL5_like cd06236
Peptidase M14-like domain of ATP/GTP binding protein (AGBL)-5 and related proteins; Peptidase ...
200-454 3.21e-64

Peptidase M14-like domain of ATP/GTP binding protein (AGBL)-5 and related proteins; Peptidase M14-like domain of ATP/GTP binding protein_like (AGBL)-5, and related proteins. The Peptidase M14 family of metallocarboxypeptidases are zinc-binding carboxypeptidases (CPs) which hydrolyze single, C-terminal amino acids from polypeptide chains, and have a recognition site for the free C-terminal carboxyl group, which is a key determinant of specificity. This eukaryotic subgroup includes the human AGBL5 and the mouse cytosolic carboxypeptidase (CCP)-5. ATP/GTP binding protein (AGTPBP-1/Nna1)-like proteins are active metallopeptidases that are thought to act on cytosolic proteins such as alpha-tubulin, to remove a C-terminal tyrosine. Mutations in AGTPBP-1/Nna1 cause Purkinje cell degeneration (pcd). AGTPBP-1/Nna1 however does not belong to this subgroup. AGTPBP-1/Nna1-like proteins from the different phyla are highly diverse, but they all contain a unique N-terminal conserved domain right before the CP domain. It has been suggested that this N-terminal domain might act as a folding domain.


Pssm-ID: 349455  Cd Length: 263  Bit Score: 209.43  E-value: 3.21e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021311895 200 YFFREQLGQSVQQRKLDLLTITSPDNLREGAE--------------------QKVVFITGRVHPGETPSSFVCQGIIDFL 259
Cdd:cd06236     8 YYHRELLCYSLEGRRVDLLTITSCHGVTEEREerlpnlfpdtskprphkfegKKVVFISARVHPGETPSSFVFNGFLEFL 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021311895 260 VSQ-HPIACVLREYLVFKIAPMLNPDGVYLGNYRCSLMGFDLNRHWLDPSPWVHPTLHGVKQLIvqmyndpktsleFYID 338
Cdd:cd06236    88 LRPdDPRAIALRRLFVFKLIPMLNPDGVARGHYRTDTRGVNLNRVYLNPDPELHPSIYAAKALL------------FYID 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021311895 339 IHAHSTMMNGFMYGNIFEDEERFQRQAIFPKLLCQNAEDFSYSSTSFN---------RD-AVKAGTGRRFL---GGLldh 405
Cdd:cd06236   156 LHAHASKRGCFIYGNALEDEEQQVENLLYPKLISLNSAHFDFDACNFSeknmysrdkRDgLSKEGSGRVALykaTGI--- 232
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 1021311895 406 tSYCYTLEVSFYsyiisgttaavpyteeaYMKLGRNVARTFLDYYRLNP 454
Cdd:cd06236   233 -VHSYTLECNYH-----------------FEDVGRALAVALLDMLGCNP 263
M14_AGBL2-3_like cd06907
Peptidase M14-like domain of ATP/GTP binding protein AGBL-2 and AGBL-3, and related proteins; ...
216-449 9.09e-62

Peptidase M14-like domain of ATP/GTP binding protein AGBL-2 and AGBL-3, and related proteins; Peptidase M14-like domain of ATP/GTP binding protein_like (AGBL)-2, and related proteins. The Peptidase M14 family of metallocarboxypeptidases are zinc-binding carboxypeptidases (CPs) which hydrolyze single, C-terminal amino acids from polypeptide chains, and have a recognition site for the free C-terminal carboxyl group, which is a key determinant of specificity. This subgroup includes the human AGBL-2, and -3, and the mouse cytosolic carboxypeptidase (CCPs)-2, and -3. ATP/GTP binding protein (AGTPBP-1/Nna1)-like proteins are active metallopeptidases that are thought to act on cytosolic proteins such as alpha-tubulin, to remove a C-terminal tyrosine. Mutations in AGTPBP-1/Nna1 cause Purkinje cell degeneration (pcd). AGTPBP-1/Nna1 however does not belong to this subgroup. AGTPBP-1/Nna1-like proteins from the different phyla are highly diverse, but they all contain a unique N-terminal conserved domain right before the CP domain. It has been suggested that this N-terminal domain might act as a folding domain.


Pssm-ID: 349478  Cd Length: 252  Bit Score: 202.53  E-value: 9.09e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021311895 216 DLLTITSP-DNLREGAEQKVVFITGRVHPGETPSSFVCQGIIDFLVSQHPIACVLREYLVFKIAPMLNPDGVYLGNYRCS 294
Cdd:cd06907    20 YVLTITSPsSNPEEAKAKKAVVLTARVHPGETNASWMMKGFLDFLTGSSPDAKLLRDNFVFKIVPMLNPDGVIVGNYRCS 99
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021311895 295 LMGFDLNRHWLDPSPWVHPTLHGVKQLIVQMYNDPKTSLefYIDIHAHSTMMNGFMYGNIFED-EERFQRQAIFPKLLCQ 373
Cdd:cd06907   100 LAGRDLNRNYKTPLKESFPTIWHTKMMIKRLLEEREVIL--YCDLHGHSRKQNVFMYGCENRKnPEKPLKERVFPLMLSK 177
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021311895 374 NAED-FSYSSTSFNRDAVKAGTGRRF---LGGLldhtsYCYTLEVSFysyiiSGTT----AAVPYTEEAYMKLGRNVART 445
Cdd:cd06907   178 NAPDkFSFESCKFKVQKSKEGTGRVVmwrEGIL-----NSYTLEATF-----CGSTlgrrKGTHFNTLDFEAMGYHFCDT 247

                  ....
gi 1021311895 446 FLDY 449
Cdd:cd06907   248 LLDY 251
M14_Nna1 cd06906
Peptidase M14-like domain of ATP/GTP binding proteins and cytosolic carboxypeptidases; ...
200-409 2.14e-52

Peptidase M14-like domain of ATP/GTP binding proteins and cytosolic carboxypeptidases; Peptidase M14-like domain of Nna-1 (Nervous system Nuclear protein induced by Axotomy), also known as ATP/GTP binding protein (AGTPBP-1) and cytosolic carboxypeptidase (CCP), and related proteins. The Peptidase M14 family of metallocarboxypeptidases are zinc-binding carboxypeptidases (CPs) which hydrolyze single, C-terminal amino acids from polypeptide chains, and have a recognition site for the free C-terminal carboxyl group, which is a key determinant of specificity. This eukaryotic subgroup includes the mouse Nna1/CCP-1, and -4 proteins, and the human Nna1/AGTPBP-1 protein. Nna1-like proteins are active metallopeptidases that are thought to act on cytosolic proteins such as alpha-tubulin, to remove a C-terminal tyrosine. Nna1 is widely expressed in the developing and adult nervous systems, including cerebellar Purkinje and granule neurons, miral cells of the olfactory bulb and retinal photoreceptors. Nna1 is also induced in axotomized motor neurons. Mutations in Nna1 cause Purkinje cell degeneration (pcd). The Nna1 CP domain is required to prevent the retinal photoreceptor loss and cerebellar ataxia phenotypes of pcd mice, and a functional zinc-binding domain is needed for Nna-1 to support neuron survival in these mice. Nna1-like proteins from the different phyla are highly diverse, but they all contain a unique N-terminal conserved domain right before the CP domain. It has been suggested that this N-terminal domain might act as a folding domain.


Pssm-ID: 349477  Cd Length: 271  Bit Score: 178.73  E-value: 2.14e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021311895 200 YFFREQLGQSVQQRKLDLLTITSPD--NLREGAEQ----KVVFITGRVHPGETPSSFVCQGIIDFLVSQHPIACVLREYL 273
Cdd:cd06906     4 YYRQQTLCETLGGNSCPVLTITAMPesNNEEHICQfrnrPYIFLSARVHPGESNASWVMKGTLDFLLSSSPAAQSLRESY 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021311895 274 VFKIAPMLNPDGVYLGNYRCSLMGFDLNRHWLDPSPWVHPTLHGVKQLIVQMYNDPKTSLeFYIDIHAHSTMMNGFMYG- 352
Cdd:cd06906    84 IFKIVPMLNPDGVINGNHRCSLSGEDLNRRWLNPNPELHPTIYHTKGLLQYLRSIGRLPL-VYCDYHGHSRKKNVFMYGc 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021311895 353 ----------------NIFEDeerfQRQAIFPKLLCQNAEDFSYSSTSFNRDAVKAGTGR----RFLGGLLDHT---SYC 409
Cdd:cd06906   163 spkeswshgdtnnpsgDIVED----LGYRTLPKLLSHFAPAFSLSSCSFVVEKSKESTARvvvwREIGVLRSYTmesTYC 238
M14_Nna1-like cd03856
Peptidase M14-like domain of ATP/GTP binding proteins, cytosolic carboxypeptidases and related ...
204-419 1.58e-35

Peptidase M14-like domain of ATP/GTP binding proteins, cytosolic carboxypeptidases and related proteins; Peptidase M14-like domain of Nna-1 (Nervous system Nuclear protein induced by Axotomy), also known as ATP/GTP binding protein (AGTPBP-1) and cytosolic carboxypeptidase (CCP), and related proteins. The Peptidase M14 family of metallocarboxypeptidases are zinc-binding carboxypeptidases (CPs) which hydrolyze single, C-terminal amino acids from polypeptide chains, and have a recognition site for the free C-terminal carboxyl group, which is a key determinant of specificity. This subfamily includes the human AGTPBP-1 and AGBL -2, -3, -4, and -5, and the mouse Nna1/CCP-1 and CCP -2 through -6. Nna1-like proteins are active metallopeptidases that are thought to act on cytosolic proteins such as alpha-tubulin, to remove a C-terminal tyrosine. Nna1 is widely expressed in the developing and adult nervous systems, including cerebellar Purkinje and granule neurons, miral cells of the olfactory bulb and retinal photoreceptors. Nna1 is also induced in axotomized motor neurons. Mutations in Nna1 cause Purkinje cell degeneration (pcd). The Nna1 CP domain is required to prevent the retinal photoreceptor loss and cerebellar ataxia phenotypes of pcd mice, and a functional zinc-binding domain is needed for Nna-1 to support neuron survival in these mice. Nna1-like proteins from the different phyla are highly diverse, but they all contain a characteristic N-terminal conserved domain right before the CP domain. It has been suggested that this N-terminal domain might act as a folding domain.


Pssm-ID: 349429  Cd Length: 252  Bit Score: 133.09  E-value: 1.58e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021311895 204 EQLGQSVQQRKLDLLTITSPDnlrEGAEQKVVFITGRVHPGETPSSFVCQGIIDFLVSQHPIACVLREYLVFKIAPMLNP 283
Cdd:cd03856    18 LEIGVTEQGREIQALQSLRTE---RSDDKSWLFLIARQHPGETTGAWVFFGFLDQLLSDDDPAQQLRAEYNFYIIPMVNP 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021311895 284 DGVYLGNYRCSLMGFDLNRHWLDPSPWVHPTLHGVKQLIVQMYNDPKtSLEFYIDIHAHSTmmNGFMYGNIFEDEerfQR 363
Cdd:cd03856    95 DGVARGHWRTNSRGMDLNRDWHAPDALLSPETYAVAAALAERVQSPE-GVVLALDLHGDNR--NVFLTGPDNKDE---ST 168
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021311895 364 QAIFPKLLCQNAEDFSYSS---TSFNRDAVKAGT-GRRFLGGLLDHTsYCYTLEVSFYSY 419
Cdd:cd03856   169 NHNPDKLNSLLTETDRRLPdynTEASPGDNPGGTvGKQWIADVYQIT-HSVTLEVGDNTD 227
M14_PaCCP-like cd06234
Peptidase M14-like domain of ATP/GTP binding proteins and cytosolic carboxypeptidases similar ...
181-341 3.12e-31

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


Pssm-ID: 349453 [Multi-domain]  Cd Length: 256  Bit Score: 121.13  E-value: 3.12e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021311895 181 YTYTRFQHYLDSLQKRnmDYFFREQLGQSVQQRKLDLLTITSPDNLRegaeqKVVFITGRVHPGETPSSFVCQGIIDFLV 260
Cdd:cd06234     1 YSYERHLDLVARAQAS--PGVRLEVLGQTLDGRDIDLLTIGDPGTGK-----KKVWIIARQHPGETMAEWFMEGLLDRLL 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021311895 261 SQH-PIACVLREYLVFKIAPMLNPDGVYLGNYRCSLMGFDLNRHWLDPSPWVHPTLHGVKQlivQMyndPKTSLEFYIDI 339
Cdd:cd06234    74 DEDdPVSRALLEKAVFYVVPNMNPDGSVRGNLRTNAAGVNLNREWANPSLERSPEVFAVRQ---AM---DATGVDFFLDV 147

                  ..
gi 1021311895 340 HA 341
Cdd:cd06234   148 HG 149
MpaA COG2866
Murein tripeptide amidase MpaA [Cell wall/membrane/envelope biogenesis];
181-340 2.39e-23

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


Pssm-ID: 442113 [Multi-domain]  Cd Length: 337  Bit Score: 100.92  E-value: 2.39e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021311895 181 YTYTRFQHYLDSLQKRNmDYFFREQLGQSVQQRKLDLLTITSPDNlregaEQKVVFITGRVHPGETPSSFVCQGIIDFLV 260
Cdd:COG2866    20 YTYEELLALLAKLAAAS-PLVELESIGKSVEGRPIYLLKIGDPAE-----GKPKVLLNAQQHGNEWTGTEALLGLLEDLL 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021311895 261 S-QHPIACVLREYLVFKIAPMLNPDGVYLgNYRCSLMGFDLNRHWLDP---SPWVhptlhgvkQLIVQMYNdpKTSLEFY 336
Cdd:COG2866    94 DnYDPLIRALLDNVTLYIVPMLNPDGAER-NTRTNANGVDLNRDWPAPwlsEPET--------RALRDLLD--EHDPDFV 162

                  ....
gi 1021311895 337 IDIH 340
Cdd:COG2866   163 LDLH 166
Peptidase_M14 pfam00246
Zinc carboxypeptidase;
189-415 2.18e-22

Zinc carboxypeptidase;


Pssm-ID: 459730 [Multi-domain]  Cd Length: 287  Bit Score: 96.98  E-value: 2.18e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021311895 189 YLDSLQKRNMDYFFREQLGQSVQQRKLDLLTITSPDNLREGAEqKVVFITGRVHPGETPSSFVCQGIIDFLVS---QHPI 265
Cdd:pfam00246   4 WLDALAARYPDLVRLVSIGKSVEGRPLKVLKISSGPGEHNPGK-PAVFIDGGIHAREWIGPATALYLIHQLLTnygRDPE 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021311895 266 ACVLREYLVFKIAPMLNPDGVYLGNY--------RCSLM-----GFDLNRHWLD------------------PSPWVHPT 314
Cdd:pfam00246  83 ITELLDDTDIYILPVVNPDGYEYTHTtdrlwrknRSNANgssciGVDLNRNFPDhwnevgassnpcsetyrgPAPFSEPE 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021311895 315 LHGVKQLIVQMYNdpktsLEFYIDIHAHSTMMNgFMYGNIF----EDEERFQRQA-IFPKLLCQNAEDFSYSSTSFNRDA 389
Cdd:pfam00246 163 TRAVADFIRSKKP-----FVLYISLHSYSQVLL-YPYGYTRdeppPDDEELKSLArAAAKALQKMVRGTSYTYGITNGAT 236
                         250       260       270
                  ....*....|....*....|....*....|..
gi 1021311895 390 VKAGTgrrflGGLLDHTS------YCYTLEVS 415
Cdd:pfam00246 237 IYPAS-----GGSDDWAYgrlgikYSYTIELR 263
Zn_pept smart00631
Zn_pept domain;
181-353 5.68e-22

Zn_pept domain;


Pssm-ID: 214748 [Multi-domain]  Cd Length: 277  Bit Score: 95.48  E-value: 5.68e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021311895  181 YTYTRFQHYLDSLQKRNMDYFFREQLGQSVQQRKLDLLTITSPDnlreGAEQKVVFITGRVHPGETPSSFVCQGIIDFLV 260
Cdd:smart00631   2 HSYEEIEAWLKELAARYPDLVRLVSIGKSVEGRPIWVLKISNGG----SHDKPAIFIDAGIHAREWIGPATALYLINQLL 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021311895  261 SQH---PIACVLREYLVFKIAPMLNPDGVYLG-----------NYRCSLMGFDLNR----HWLDPSPWVHPTLHG----- 317
Cdd:smart00631  78 ENYgrdPRVTNLLDKTDIYIVPVLNPDGYEYThtgdrlwrknrSPNSNCRGVDLNRnfpfHWGETGNPCSETYAGpspfs 157
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|..
gi 1021311895  318 ------VKQLIVQMYNdpktsLEFYIDIHAHSTMMNgFMYGN 353
Cdd:smart00631 158 epetkaVRDFIRSNRR-----FKLYIDLHSYSQLIL-YPYGY 193
M14_Nna1-like cd06237
Peptidase M14-like domain of ATP/GTP binding proteins and cytosolic carboxypeptidases; ...
185-344 3.28e-19

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


Pssm-ID: 349456 [Multi-domain]  Cd Length: 239  Bit Score: 86.85  E-value: 3.28e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021311895 185 RFQHYLDSLQKRnmDYFFREQLGQSVQQRKLDLLTITSPDNlregaeQKVVFITGRVHPGETPSSFVCQGIIDFLVSQHP 264
Cdd:cd06237     2 DYDAWIDSLAKK--PFVKRSTIGKSVEGRPIEALTIGNPDS------KELVVLLGRQHPPEVTGALAMQAFVETLLADTE 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021311895 265 IACVLRE-YLVFkIAPMLNPDGVYLGNYRCSLMGFDLNRHWldpSPWVHPTLHGVKQLIVQMYNDPKTSLEFYIDIhaHS 343
Cdd:cd06237    74 LAKAFRArFRVL-VVPLLNPDGVDLGHWRHNAGGVDLNRDW---GPFTQPETRAVRDFLLELVEEPGGKVVFGLDF--HS 147

                  .
gi 1021311895 344 T 344
Cdd:cd06237   148 T 148
M14_Nna1-like cd18429
Peptidase M14-like domain of ATP/GTP binding proteins and cytosolic carboxypeptidases; ...
204-340 5.42e-14

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


Pssm-ID: 349485  Cd Length: 253  Bit Score: 71.72  E-value: 5.42e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021311895 204 EQLGQSVQQRKLDLLTITSPDnlregaEQKVVFITGRVHPGETPSSFVCQGIIDFLVSQHPIACVLREYLVFKIAPMLNP 283
Cdd:cd18429    18 TTIGKTVEGRPLEIIRIGNES------APHRVFLRARAHPWEAGGNWVVEGLVERLLQNDEEAKRFLKRYCVYILPMANK 91
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1021311895 284 DGVYLGNYRCSLMGFDLNRHWLDPS-PWVHPTLHGVKQLIVQMYNDPKTSlEFYIDIH 340
Cdd:cd18429    92 DGVARGRTRFNANGKDLNREWDKPAdPVLAPENFALEKWLEEMIKAGKKP-DLAIELH 148
Pepdidase_M14_N pfam18027
Cytosolic carboxypeptidase N-terminal domain; This entry corresponds to the N-terminal domain ...
46-142 1.68e-10

Cytosolic carboxypeptidase N-terminal domain; This entry corresponds to the N-terminal domain of cytosolic carboxypeptidases. The N-terminal domain folds into a nine-stranded antiparallel beta sandwich. This domain is specific to CCP proteins and is absent in other carboxypeptidases. It has been hypothesized that the N-terminal domain might contribute to folding, might have a regulatory function and/or might be involved in binding other proteins.


Pssm-ID: 407865  Cd Length: 107  Bit Score: 58.06  E-value: 1.68e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021311895  46 FDACFESGNLGRVDQVSEFEYDLFIRPDTcNPRFRVWFNFTVENVKESQVReivdtfrvvlrviFNIVNFSktKSLYRDG 125
Cdd:pfam18027   1 ISSNFDSGNIEVVSASDPDAIRLRIRPDN-GSEHFQWFYFRVSGARGRPLT-------------FVIENAG--EASYPDG 64
                          90
                  ....*....|....*....
gi 1021311895 126 MAPM--VKSTSRPKWQRLP 142
Cdd:pfam18027  65 WTGYrvVASYDRENWFRVP 83
M14_CP_bacteria cd18173
bacterial peptidase M14 carboxypeptidase, uncharacterized; This family contains only bacterial ...
179-314 3.38e-08

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: 54.89  E-value: 3.38e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021311895 179 YPyTYTRFQHYLDSLQKRNMDYFFREQLGQSVQQRKLDLLTITspDNLREGAEQKVVFITGRVHPGETPSSFVCQGIIDF 258
Cdd:cd18173     4 YP-TYEEYEAMMQSFAANYPNICRLVSIGTSVQGRKLLALKIS--DNVNTEEAEPEFKYTSTMHGDETTGYELMLRLIDY 80
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1021311895 259 LVSQHPIACVLReYLVFK----IAPMLNPDGVYLGNYRCSLM-------GFDLNRHWLDPSPWVHPT 314
Cdd:cd18173    81 LLTNYGTDPRIT-NLVDNteiwINPLANPDGTYAGGNNTVSGatrynanGVDLNRNFPDPVDGDHPD 146
Peptidase_M14_like cd00596
M14 family of metallocarboxypeptidases and related proteins; The M14 family of ...
235-424 2.67e-07

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: 51.31  E-value: 2.67e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021311895 235 VFITGRVHPGETPSSFVCQGIIDFLVS---QHPIACVLREYLVFkIAPMLNPDGVYLGNYRCS---LMGFDLNRHWldPS 308
Cdd:cd00596     1 ILITGGIHGNEVIGVELALALIEYLLEnygNDPLKRLLDNVELW-IVPLVNPDGFARVIDSGGrknANGVDLNRNF--PY 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021311895 309 PWVHPTLHGVKQLI-----------VQMYNDPKTSLEF--YIDIH--AHSTMMNGFMYGNIFEDEERFQRQA-IFPKLLC 372
Cdd:cd00596    78 NWGKDGTSGPSSPTyrgpapfsepeTQALRDLAKSHRFdlAVSYHssSEAILYPYGYTNEPPPDFSEFQELAaGLARALG 157
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1021311895 373 QNAEDFSYSSTSFNRDavkaGTGRRFLGGllDHTSYCYTLEVSFYSYIISGT 424
Cdd:cd00596   158 AGEYGYGYSYTWYSTT----GTADDWLYG--ELGILAFTVELGTADYPLPGT 203
M14-like cd06905
Peptidase M14-like domain; uncharacterized subfamily; A functionally uncharacterized subgroup ...
181-285 3.19e-07

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: 52.23  E-value: 3.19e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021311895 181 YTYTRFQHYLDSLQKRNMDYFFREQLGQSVQQRKLDLLTITSPDNlREGAEQKVVFITGRVHPGETPSSFVCQGIIDFLV 260
Cdd:cd06905     7 YTYAELTARLKALAEAYPNLVRLESIGKSYEGRDIWLLTITNGET-GPADEKPALWVDGNIHGNEVTGSEVALYLAEYLL 85
                          90       100
                  ....*....|....*....|....*...
gi 1021311895 261 SQHPIACVLREYL---VFKIAPMLNPDG 285
Cdd:cd06905    86 TNYGKDPEITRLLdtrTFYILPRLNPDG 113
M14_CP_A-B_like cd03860
Peptidase M14 carboxypeptidase subfamily A/B-like; The Peptidase M14 Carboxypeptidase (CP) A/B ...
182-351 8.05e-07

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: 50.60  E-value: 8.05e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021311895 182 TYTRFQHYLDSLQKRNMDYFFREQLGQSVQQRKLDLLTITSPDNlreGAEQKVVFITGRVHPGE--TPSsfVCQGIIDFL 259
Cdd:cd03860     3 PLDDIVQWLDDLAAAFPDNVEIFTIGKSYEGRDITGIHIWGSGG---KGGKPAIVIHGGQHAREwiSTS--TVEYLAHQL 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021311895 260 VSQHPIACVLREYLV---FKIAPMLNPDG-VY--------------LGNYRCslMGFDLNR----HWLDPSPWVHP---T 314
Cdd:cd03860    78 LSGYGSDATITALLDkfdFYIIPVVNPDGyVYtwttdrlwrknrqpTGGSSC--VGIDLNRnwgyKWGGPGASTNPcseT 155
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1021311895 315 LHG--------VKQLIVQMYNDPKTS-LEFYIDIHAHSTMmngFMY 351
Cdd:cd03860   156 YRGpsafsapeTKALADFINALAAGQgIKGFIDLHSYSQL---ILY 198
M14_REP34-like cd06231
Peptidase M14-like domain similar to rapid encystment phenotype 34 (REP34); This family ...
189-311 7.04e-06

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


Pssm-ID: 349450 [Multi-domain]  Cd Length: 239  Bit Score: 47.30  E-value: 7.04e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021311895 189 YLDSLQKR-NMDYFFREQLGqSVQQRKLDLLTITSPdnlREGAEQKVVFITGRVHpGETPSSfvCQGIIDFLVSQHPIac 267
Cdd:cd06231     2 YLRDVAERlGARRFKVRELG-EVGYQGYPLFALKSP---NPRGDKPRVLISAGIH-GDEPAG--VEALLRFLESLAEK-- 72
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1021311895 268 VLREYlVFKIAPMLNPDGvYLGNYRCSLMGFDLNRHWL--DPSPWV 311
Cdd:cd06231    73 YLRRV-NLLVLPCVNPWG-FERNTRENADGIDLNRSFLkdSPSPEV 116
M14-like cd03857
Peptidase M14-like domain; uncharacterized subfamily; Peptidase M14-like domain of a ...
234-340 2.61e-03

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


Pssm-ID: 349430 [Multi-domain]  Cd Length: 203  Bit Score: 39.37  E-value: 2.61e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021311895 234 VVFITGRVHPGE-TPSSFVCQGIIDFLVSQHPIACVLREyLVFKIAPMLNPDGVYL-GNYRCSLM-----------GFDL 300
Cdd:cd03857     1 TVLLAAQIHGNEtTGTEALMELIRDLASESDEAAKLLDN-IVILLVPQLNPDGAELfVNFYLDSMnglpgtrynanGIDL 79
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1021311895 301 NRHWLDPSpwvHPTLHGVKQLIVQMYndpktsLEFYIDIH 340
Cdd:cd03857    80 NRDHVKLT---QPETQAVAENFIHWW------PDIFIDLH 110
M14_CP_insect cd06248
Peptidase M14 carboxypeptidase subfamily A/B-like; This family includes peptidase M14 ...
189-321 3.11e-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: 3.11e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021311895 189 YLDSLQKRNMDYFFREQLGQSVQQRKLDLLTITSPDNlrEGAEQKVVFITGRVHPGETPSSFVCQGIIDFLV----SQHP 264
Cdd:cd06248    10 YLDGLAEESPDVVTVVEGGYTFEGRPIKYVRIRSTNS--EDTSKPTIMIEGGINPREWISPPAALYAIHKLVedveTQSD 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021311895 265 IACVLREYLVfkiaPMLNPDGV--------------YLGNYRC--SLMGFDLNR----HWLDPSPWVHP---TLHGVKQL 321
Cdd:cd06248    88 LLNNFDWIIL----PVANPDGYvfthtndrewtknrSTNSNPLgqICFGVNINRnfdyQWNPVLSSESPcseLYAGPSAF 163
M14-like cd06239
Peptidase M14-like domain; uncharacterized subgroup; Peptidase M14-like domain of a ...
254-302 3.23e-03

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


Pssm-ID: 349458 [Multi-domain]  Cd Length: 194  Bit Score: 38.94  E-value: 3.23e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 1021311895 254 GIIDFLVSQHPIACVLREYLVFKIAPMLNPDGVYLgNYRCSLMGFDLNR 302
Cdd:cd06239    21 DLISYLRRERQEFEKILERLTLVAIPMLNPDGAEL-FTRHNAEGIDLNR 68
M14-CPA-like cd06227
Peptidase M14 carboxypeptidase A-like domain; uncharacterized subfamily; A functionally ...
269-310 3.47e-03

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


Pssm-ID: 349446 [Multi-domain]  Cd Length: 224  Bit Score: 39.18  E-value: 3.47e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 1021311895 269 LREYLVFKIAPMLNPDG---VYLGNY--RCSLMGFDLNRHWldPSPW 310
Cdd:cd06227    47 ILDNVELKIIPNANPDGrrlVESGDYcwRGNENGVDLNRNW--GVDW 91
M14_CPD_III cd06245
Peptidase M14 carboxypeptidase subfamily N/E-like; Carboxypeptidase D, domain III subgroup; ...
206-285 3.68e-03

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: 39.35  E-value: 3.68e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021311895 206 LGQSVQQRKLDLLTITSPDNLREGAEQKVVFITGrvHPGETPSS---------FVCQ-GIIDFLVSQhpiacvLREYLVF 275
Cdd:cd06245    27 LGQSVEKRDIWVLEIGNKPNESEPSEPKILFVGG--IHGNAPVGtelllllahFLCHnYKKDSAITK------LLNRTRI 98
                          90
                  ....*....|
gi 1021311895 276 KIAPMLNPDG 285
Cdd:cd06245    99 HIVPSLNPDG 108
 
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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