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Conserved domains on  [gi|568943134|ref|XP_006506797|]
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cytosolic carboxypeptidase 3 isoform X4 [Mus musculus]

Protein Classification

M14 family cytosolic carboxypeptidase CCP2/3( domain architecture ID 15732948)

M14 family metallopeptidase is a zinc-binding carboxypeptidase which hydrolyzes a single, C-terminal amino acid from a polypeptide chain, and has a recognition site for the free C-terminal carboxyl group

EC:  3.4.17.-
Gene Ontology:  GO:0006508|GO:0008270
PubMed:  7674922|10493853

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
M14_AGBL2-3_like cd06907
Peptidase M14-like domain of ATP/GTP binding protein AGBL-2 and AGBL-3, and related proteins; ...
319-571 9.32e-175

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: 496.82  E-value: 9.32e-175
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568943134 319 RSKFCKIRVLCHTLARNMVYVLTITTPLK--TSDSKRKAVILTARVHPGETNSSWIMKGFLDYILGDSSDARLLRDTFIF 396
Cdd:cd06907    1 RSQYCKRRVLCRTLAGNSVYVLTITSPSSnpEEAKAKKAVVLTARVHPGETNASWMMKGFLDFLTGSSPDAKLLRDNFVF 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568943134 397 KVVPMLNPDGVIVGNYRCSLAGRDLNRNYTSLLKESFPSVWYTRNMINRLMEKREVILYCDLHGHSRKQNIFMYGCDGSS 476
Cdd:cd06907   81 KIVPMLNPDGVIVGNYRCSLAGRDLNRNYKTPLKESFPTIWHTKMMIKRLLEEREVILYCDLHGHSRKQNVFMYGCENRK 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568943134 477 RSKTKglyLQQRIFPLMLSKNCPNIFSFSACKFNVQKSKEGTGRVVMWKMGIRNSFTLEATFCGSTLGNKRGTHFGTKDL 556
Cdd:cd06907  161 NPEKP---LKERVFPLMLSKNAPDKFSFESCKFKVQKSKEGTGRVVMWREGILNSYTLEATFCGSTLGRRKGTHFNTLDF 237
                        250
                 ....*....|....*
gi 568943134 557 ESMGYHFCDSLLDYC 571
Cdd:cd06907  238 EAMGYHFCDTLLDYC 252
Pepdidase_M14_N super family cl39445
Cytosolic carboxypeptidase N-terminal domain; This entry corresponds to the N-terminal domain ...
171-297 3.44e-18

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: 80.41  E-value: 3.44e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568943134  171 FEARFESGNLQKVVKVADHEYELTVRPDlFTNKHTQWYYFQVTNTQAEIvYRFTIVNFTKpaSLYNRGMKPLfysEKEAK 250
Cdd:pfam18027   1 ISSNFDSGNIEVVSASDPDAIRLRIRPD-NGSEHFQWFYFRVSGARGRP-LTFVIENAGE--ASYPDGWTGY---RVVAS 73
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 568943134  251 THNIGWQRIGDQikyYKNNlgqdgrhffslTWTFQFPHSQDTCYFAH 297
Cdd:pfam18027  74 YDRENWFRVPTE---YDGG-----------VLTITHTPEADTVYFAY 106
 
Name Accession Description Interval E-value
M14_AGBL2-3_like cd06907
Peptidase M14-like domain of ATP/GTP binding protein AGBL-2 and AGBL-3, and related proteins; ...
319-571 9.32e-175

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: 496.82  E-value: 9.32e-175
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568943134 319 RSKFCKIRVLCHTLARNMVYVLTITTPLK--TSDSKRKAVILTARVHPGETNSSWIMKGFLDYILGDSSDARLLRDTFIF 396
Cdd:cd06907    1 RSQYCKRRVLCRTLAGNSVYVLTITSPSSnpEEAKAKKAVVLTARVHPGETNASWMMKGFLDFLTGSSPDAKLLRDNFVF 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568943134 397 KVVPMLNPDGVIVGNYRCSLAGRDLNRNYTSLLKESFPSVWYTRNMINRLMEKREVILYCDLHGHSRKQNIFMYGCDGSS 476
Cdd:cd06907   81 KIVPMLNPDGVIVGNYRCSLAGRDLNRNYKTPLKESFPTIWHTKMMIKRLLEEREVILYCDLHGHSRKQNVFMYGCENRK 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568943134 477 RSKTKglyLQQRIFPLMLSKNCPNIFSFSACKFNVQKSKEGTGRVVMWKMGIRNSFTLEATFCGSTLGNKRGTHFGTKDL 556
Cdd:cd06907  161 NPEKP---LKERVFPLMLSKNAPDKFSFESCKFKVQKSKEGTGRVVMWREGILNSYTLEATFCGSTLGRRKGTHFNTLDF 237
                        250
                 ....*....|....*
gi 568943134 557 ESMGYHFCDSLLDYC 571
Cdd:cd06907  238 EAMGYHFCDTLLDYC 252
MpaA COG2866
Murein tripeptide amidase MpaA [Cell wall/membrane/envelope biogenesis];
301-460 3.99e-24

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


Pssm-ID: 442113 [Multi-domain]  Cd Length: 337  Bit Score: 104.00  E-value: 3.99e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568943134 301 YTYSNLQEYLSGINSdpvRSKFCKIRVLCHTLA-RNMvYVLTITTPlktsDSKRKAVILTARVHPGETNSSWIMKGFLDY 379
Cdd:COG2866   20 YTYEELLALLAKLAA---ASPLVELESIGKSVEgRPI-YLLKIGDP----AEGKPKVLLNAQQHGNEWTGTEALLGLLED 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568943134 380 IL-GDSSDARLLRDTFIFKVVPMLNPDGVIVgNYRCSLAGRDLNRNYtsllkesfPSVWY----TRNMINrLMEKREVIL 454
Cdd:COG2866   92 LLdNYDPLIRALLDNVTLYIVPMLNPDGAER-NTRTNANGVDLNRDW--------PAPWLsepeTRALRD-LLDEHDPDF 161

                 ....*.
gi 568943134 455 YCDLHG 460
Cdd:COG2866  162 VLDLHG 167
Zn_pept smart00631
Zn_pept domain;
301-540 8.07e-19

Zn_pept domain;


Pssm-ID: 214748 [Multi-domain]  Cd Length: 277  Bit Score: 87.01  E-value: 8.07e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568943134   301 YTYSNLQEYLSGINSDpvRSKFCKIRVLCHTLARNMVYVLTITTPLKTSdskRKAVILTARVHPGETNSSWIMKGFLDYI 380
Cdd:smart00631   2 HSYEEIEAWLKELAAR--YPDLVRLVSIGKSVEGRPIWVLKISNGGSHD---KPAIFIDAGIHAREWIGPATALYLINQL 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568943134   381 L---GDSSDARLLRDTFIFKVVPMLNPDGVIVG-----------NYRCSLAGRDLNRNYTSLLKES---FPSVWY----- 438
Cdd:smart00631  77 LenyGRDPRVTNLLDKTDIYIVPVLNPDGYEYThtgdrlwrknrSPNSNCRGVDLNRNFPFHWGETgnpCSETYAgpspf 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568943134   439 ----TRNMINRLMEKREVILYCDLHGHSRKqniFMYGCDGSSRSKTKGLYLQQRIFPLM---LSKNCPNIFSFsACKFNV 511
Cdd:smart00631 157 sepeTKAVRDFIRSNRRFKLYIDLHSYSQL---ILYPYGYTKNDLPPNVDDLDAVAKALakaLASVHGTRYTY-GISNGA 232
                          250       260       270
                   ....*....|....*....|....*....|
gi 568943134   512 QKSKEGTGRV-VMWKMGIRNSFTLEATFCG 540
Cdd:smart00631 233 IYPASGGSDDwAYGVLGIPFSFTLELRDDG 262
Pepdidase_M14_N pfam18027
Cytosolic carboxypeptidase N-terminal domain; This entry corresponds to the N-terminal domain ...
171-297 3.44e-18

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: 80.41  E-value: 3.44e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568943134  171 FEARFESGNLQKVVKVADHEYELTVRPDlFTNKHTQWYYFQVTNTQAEIvYRFTIVNFTKpaSLYNRGMKPLfysEKEAK 250
Cdd:pfam18027   1 ISSNFDSGNIEVVSASDPDAIRLRIRPD-NGSEHFQWFYFRVSGARGRP-LTFVIENAGE--ASYPDGWTGY---RVVAS 73
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 568943134  251 THNIGWQRIGDQikyYKNNlgqdgrhffslTWTFQFPHSQDTCYFAH 297
Cdd:pfam18027  74 YDRENWFRVPTE---YDGG-----------VLTITHTPEADTVYFAY 106
Peptidase_M14 pfam00246
Zinc carboxypeptidase;
334-486 2.42e-13

Zinc carboxypeptidase;


Pssm-ID: 459730 [Multi-domain]  Cd Length: 287  Bit Score: 70.79  E-value: 2.42e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568943134  334 RNMvYVLTITTPLKTSDSKRKAVILTARVHPGETNSSWIMKGFLDYIL---GDSSDARLLRDTFIFKVVPMLNPDGVIVG 410
Cdd:pfam00246  28 RPL-KVLKISSGPGEHNPGKPAVFIDGGIHAREWIGPATALYLIHQLLtnyGRDPEITELLDDTDIYILPVVNPDGYEYT 106
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568943134  411 ------------NYRCSLA-GRDLNRNYTSLLKESFP---------------SVWYTRNMINRLMEKREVILYCDLHGHS 462
Cdd:pfam00246 107 httdrlwrknrsNANGSSCiGVDLNRNFPDHWNEVGAssnpcsetyrgpapfSEPETRAVADFIRSKKPFVLYISLHSYS 186
                         170       180
                  ....*....|....*....|....
gi 568943134  463 RKQNiFMYGCDGSSRSKTKGLYLQ 486
Cdd:pfam00246 187 QVLL-YPYGYTRDEPPPDDEELKS 209
 
Name Accession Description Interval E-value
M14_AGBL2-3_like cd06907
Peptidase M14-like domain of ATP/GTP binding protein AGBL-2 and AGBL-3, and related proteins; ...
319-571 9.32e-175

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: 496.82  E-value: 9.32e-175
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568943134 319 RSKFCKIRVLCHTLARNMVYVLTITTPLK--TSDSKRKAVILTARVHPGETNSSWIMKGFLDYILGDSSDARLLRDTFIF 396
Cdd:cd06907    1 RSQYCKRRVLCRTLAGNSVYVLTITSPSSnpEEAKAKKAVVLTARVHPGETNASWMMKGFLDFLTGSSPDAKLLRDNFVF 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568943134 397 KVVPMLNPDGVIVGNYRCSLAGRDLNRNYTSLLKESFPSVWYTRNMINRLMEKREVILYCDLHGHSRKQNIFMYGCDGSS 476
Cdd:cd06907   81 KIVPMLNPDGVIVGNYRCSLAGRDLNRNYKTPLKESFPTIWHTKMMIKRLLEEREVILYCDLHGHSRKQNVFMYGCENRK 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568943134 477 RSKTKglyLQQRIFPLMLSKNCPNIFSFSACKFNVQKSKEGTGRVVMWKMGIRNSFTLEATFCGSTLGNKRGTHFGTKDL 556
Cdd:cd06907  161 NPEKP---LKERVFPLMLSKNAPDKFSFESCKFKVQKSKEGTGRVVMWREGILNSYTLEATFCGSTLGRRKGTHFNTLDF 237
                        250
                 ....*....|....*
gi 568943134 557 ESMGYHFCDSLLDYC 571
Cdd:cd06907  238 EAMGYHFCDTLLDYC 252
M14_AGTPBP-like cd06235
Peptidase M14-like domain of human Nna1/AGTPBP-1, AGBL2 -5, and related proteins; Subgroup of ...
322-569 5.91e-108

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: 326.34  E-value: 5.91e-108
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568943134 322 FCKIRVLCHTLARNMVYVLTITTPLKTSDSK-------RKAVILTARVHPGETNSSWIMKGFLDYILGDSSDARLLRDTF 394
Cdd:cd06235    2 YFEREVLCHSLDGRKLDLLTITSPNNKKLGPyprefagKKVVFLSGRVHPGETPASFVMKGFLDFLLSNDPRAQLLREHF 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568943134 395 IFKVVPMLNPDGVIVGNYRCSLAGRDLNRNYTSLLKESFPSVWYTRNMINRLME--KREVILYCDLHGHSRKQNIFMYGC 472
Cdd:cd06235   82 VFKIVPMLNPDGVIRGNYRCSLNGFNLNRHYKNPDPELHPTIYGAKKVIDYLQKtyKRRVLMYCDFHGHSSKSNGFMYGN 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568943134 473 DGSSRSKtkglYLQQRIFPLMLSKNCPNIFSFSACKFNVQKSKEGTGRVVMWKM-GIRNSFTLEATFCGSTLGNK-RGTH 550
Cdd:cd06235  162 SFPDTVQ----FHWNMVFPKILSLNAPDFFSSSCCSFGVMKSKEGTGRVVFGRRlIHSHSYTLESTFFSNNRGNIdGACG 237
                        250
                 ....*....|....*....
gi 568943134 551 FGTKDLESMGYHFCDSLLD 569
Cdd:cd06235  238 YTEENLEDLGYSVASTLLD 256
M14_Nna1 cd06906
Peptidase M14-like domain of ATP/GTP binding proteins and cytosolic carboxypeptidases; ...
327-568 4.39e-90

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: 280.42  E-value: 4.39e-90
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568943134 327 VLCHTLARNMVYVLTITTPLKTSDSK-------RKAVILTARVHPGETNSSWIMKGFLDYILGDSSDARLLRDTFIFKVV 399
Cdd:cd06906    9 TLCETLGGNSCPVLTITAMPESNNEEhicqfrnRPYIFLSARVHPGESNASWVMKGTLDFLLSSSPAAQSLRESYIFKIV 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568943134 400 PMLNPDGVIVGNYRCSLAGRDLNRNYTSLLKESFPSVWYTRNMINRL-MEKREVILYCDLHGHSRKQNIFMYGCDGS--- 475
Cdd:cd06906   89 PMLNPDGVINGNHRCSLSGEDLNRRWLNPNPELHPTIYHTKGLLQYLrSIGRLPLVYCDYHGHSRKKNVFMYGCSPKesw 168
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568943134 476 ---SRSKTKGLYLQQ---RIFPLMLSKNCPnIFSFSACKFNVQKSKEGTGRVVMWKM-GIRNSFTLEATFCGSTLGNKRG 548
Cdd:cd06906  169 shgDTNNPSGDIVEDlgyRTLPKLLSHFAP-AFSLSSCSFVVEKSKESTARVVVWREiGVLRSYTMESTYCGCDQGKYKG 247
                        250       260
                 ....*....|....*....|
gi 568943134 549 THFGTKDLESMGYHFCDSLL 568
Cdd:cd06906  248 LHIGTRELEEMGARFCEALL 267
M14_AGBL4_like cd06908
Peptidase M14-like domain of ATP/GTP binding protein AGBL-4 and related proteins; Peptidase ...
327-570 2.79e-62

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: 207.15  E-value: 2.79e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568943134 327 VLCHTLARNMVYVLTITTPL---KTSDSKRKAVILTARVHPGETNSSWIMKGFLDYILGDSSDARLLRDTFIFKVVPMLN 403
Cdd:cd06908    7 LLGKSVQQRRLDLLTITDPVnkhLTVEKKKKVVFITARVHPGETPSSFVCQGLIDFLVSNHPVAKVLRDHLVFKIVPMLN 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568943134 404 PDGVIVGNYRCSLAGRDLNRNYTSLLKESFPSVWYTRNMINRLME--KREVILYCDLHGHSRKQNIFMYGCDGSSRSKtk 481
Cdd:cd06908   87 PDGVFLGNYRCSLMGFDLNRHWHEPSPWAHPTLYAVKNLLRELDNdpTVQLDFYIDIHAHSTLMNGFMYGNIYDDVYR-- 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568943134 482 glYLQQRIFPLMLSKNCPNiFSFSACKFNVQKSKEGTGRVVMWKMGIRNSF--TLEATFCGSTLGNKRG-THFGTKDLES 558
Cdd:cd06908  165 --FERQAVFPKLLCQNAED-FSLSNTVFNRDPVKAGTGRRFLGGLLDDTANcyTLEVSFYSYRLSDSSSaTPYTEEGYMK 241
                        250
                 ....*....|..
gi 568943134 559 MGYHFCDSLLDY 570
Cdd:cd06908  242 LGRNMARALLDY 253
M14_AGBL5_like cd06236
Peptidase M14-like domain of ATP/GTP binding protein (AGBL)-5 and related proteins; Peptidase ...
327-539 1.11e-48

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: 170.91  E-value: 1.11e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568943134 327 VLCHTLARNMVYVLTITTPLKTSDS---------------------KRKAVILTARVHPGETNSSWIMKGFLDYILG-DS 384
Cdd:cd06236   13 LLCYSLEGRRVDLLTITSCHGVTEEreerlpnlfpdtskprphkfeGKKVVFISARVHPGETPSSFVFNGFLEFLLRpDD 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568943134 385 SDARLLRDTFIFKVVPMLNPDGVIVGNYRCSLAGRDLNRNYTSLLKESFPSVWYTrnminrlmekREVILYCDLHGHSRK 464
Cdd:cd06236   93 PRAIALRRLFVFKLIPMLNPDGVARGHYRTDTRGVNLNRVYLNPDPELHPSIYAA----------KALLFYIDLHAHASK 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568943134 465 QNIFMYGcdgsSRSKTKGLYLQQRIFPLMLSKNCPNiFSFSACKFNVQ----------KSKEGTGRVVMWK-MGIRNSFT 533
Cdd:cd06236  163 RGCFIYG----NALEDEEQQVENLLYPKLISLNSAH-FDFDACNFSEKnmysrdkrdgLSKEGSGRVALYKaTGIVHSYT 237

                 ....*.
gi 568943134 534 LEATFC 539
Cdd:cd06236  238 LECNYH 243
M14_Nna1-like cd03856
Peptidase M14-like domain of ATP/GTP binding proteins, cytosolic carboxypeptidases and related ...
349-478 1.56e-32

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: 126.16  E-value: 1.56e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568943134 349 SDSKRKaVILTARVHPGETNSSWIMKGFLDYILGDSSDARLLRDTFIFKVVPMLNPDGVIVGNYRCSLAGRDLNRNYTSL 428
Cdd:cd03856   40 SDDKSW-LFLIARQHPGETTGAWVFFGFLDQLLSDDDPAQQLRAEYNFYIIPMVNPDGVARGHWRTNSRGMDLNRDWHAP 118
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 568943134 429 LKESFPSVWYTRN-MINRLMEKREVILYCDLHGHSRkqNIFMYGCDGSSRS 478
Cdd:cd03856  119 DALLSPETYAVAAaLAERVQSPEGVVLALDLHGDNR--NVFLTGPDNKDES 167
M14_PaCCP-like cd06234
Peptidase M14-like domain of ATP/GTP binding proteins and cytosolic carboxypeptidases similar ...
320-499 8.90e-30

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: 118.44  E-value: 8.90e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568943134 320 SKFCKIRVLCHTLA-RNMVyVLTITTPlktsDSKRKAVILTARVHPGETNSSWIMKGFLDYILGDS-SDARLLRDTFIFK 397
Cdd:cd06234   16 SPGVRLEVLGQTLDgRDID-LLTIGDP----GTGKKKVWIIARQHPGETMAEWFMEGLLDRLLDEDdPVSRALLEKAVFY 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568943134 398 VVPMLNPDGVIVGNYRCSLAGRDLNRNYTSLLKESFPSVWYTRNMinrlMEKREVILYCDLHGHSRKQNIFMYGCDGSSr 477
Cdd:cd06234   91 VVPNMNPDGSVRGNLRTNAAGVNLNREWANPSLERSPEVFAVRQA----MDATGVDFFLDVHGDEALPYNFIAGAEGIP- 165
                        170       180
                 ....*....|....*....|..
gi 568943134 478 SKTKGLYLQQRIFPLMLSKNCP 499
Cdd:cd06234  166 SWTPRLAALEAAFKAALAAASP 187
MpaA COG2866
Murein tripeptide amidase MpaA [Cell wall/membrane/envelope biogenesis];
301-460 3.99e-24

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


Pssm-ID: 442113 [Multi-domain]  Cd Length: 337  Bit Score: 104.00  E-value: 3.99e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568943134 301 YTYSNLQEYLSGINSdpvRSKFCKIRVLCHTLA-RNMvYVLTITTPlktsDSKRKAVILTARVHPGETNSSWIMKGFLDY 379
Cdd:COG2866   20 YTYEELLALLAKLAA---ASPLVELESIGKSVEgRPI-YLLKIGDP----AEGKPKVLLNAQQHGNEWTGTEALLGLLED 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568943134 380 IL-GDSSDARLLRDTFIFKVVPMLNPDGVIVgNYRCSLAGRDLNRNYtsllkesfPSVWY----TRNMINrLMEKREVIL 454
Cdd:COG2866   92 LLdNYDPLIRALLDNVTLYIVPMLNPDGAER-NTRTNANGVDLNRDW--------PAPWLsepeTRALRD-LLDEHDPDF 161

                 ....*.
gi 568943134 455 YCDLHG 460
Cdd:COG2866  162 VLDLHG 167
M14_Nna1-like cd06237
Peptidase M14-like domain of ATP/GTP binding proteins and cytosolic carboxypeptidases; ...
319-425 1.54e-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: 88.01  E-value: 1.54e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568943134 319 RSKFCKIRVLCHTLARNMVYVLTITTPlktsdSKRKAVILTARVHPGETNSSWIMKGFLDYILGDSSDARLLRDTFIFKV 398
Cdd:cd06237   12 KKPFVKRSTIGKSVEGRPIEALTIGNP-----DSKELVVLLGRQHPPEVTGALAMQAFVETLLADTELAKAFRARFRVLV 86
                         90       100
                 ....*....|....*....|....*..
gi 568943134 399 VPMLNPDGVIVGNYRCSLAGRDLNRNY 425
Cdd:cd06237   87 VPLLNPDGVDLGHWRHNAGGVDLNRDW 113
Zn_pept smart00631
Zn_pept domain;
301-540 8.07e-19

Zn_pept domain;


Pssm-ID: 214748 [Multi-domain]  Cd Length: 277  Bit Score: 87.01  E-value: 8.07e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568943134   301 YTYSNLQEYLSGINSDpvRSKFCKIRVLCHTLARNMVYVLTITTPLKTSdskRKAVILTARVHPGETNSSWIMKGFLDYI 380
Cdd:smart00631   2 HSYEEIEAWLKELAAR--YPDLVRLVSIGKSVEGRPIWVLKISNGGSHD---KPAIFIDAGIHAREWIGPATALYLINQL 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568943134   381 L---GDSSDARLLRDTFIFKVVPMLNPDGVIVG-----------NYRCSLAGRDLNRNYTSLLKES---FPSVWY----- 438
Cdd:smart00631  77 LenyGRDPRVTNLLDKTDIYIVPVLNPDGYEYThtgdrlwrknrSPNSNCRGVDLNRNFPFHWGETgnpCSETYAgpspf 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568943134   439 ----TRNMINRLMEKREVILYCDLHGHSRKqniFMYGCDGSSRSKTKGLYLQQRIFPLM---LSKNCPNIFSFsACKFNV 511
Cdd:smart00631 157 sepeTKAVRDFIRSNRRFKLYIDLHSYSQL---ILYPYGYTKNDLPPNVDDLDAVAKALakaLASVHGTRYTY-GISNGA 232
                          250       260       270
                   ....*....|....*....|....*....|
gi 568943134   512 QKSKEGTGRV-VMWKMGIRNSFTLEATFCG 540
Cdd:smart00631 233 IYPASGGSDDwAYGVLGIPFSFTLELRDDG 262
Pepdidase_M14_N pfam18027
Cytosolic carboxypeptidase N-terminal domain; This entry corresponds to the N-terminal domain ...
171-297 3.44e-18

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: 80.41  E-value: 3.44e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568943134  171 FEARFESGNLQKVVKVADHEYELTVRPDlFTNKHTQWYYFQVTNTQAEIvYRFTIVNFTKpaSLYNRGMKPLfysEKEAK 250
Cdd:pfam18027   1 ISSNFDSGNIEVVSASDPDAIRLRIRPD-NGSEHFQWFYFRVSGARGRP-LTFVIENAGE--ASYPDGWTGY---RVVAS 73
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 568943134  251 THNIGWQRIGDQikyYKNNlgqdgrhffslTWTFQFPHSQDTCYFAH 297
Cdd:pfam18027  74 YDRENWFRVPTE---YDGG-----------VLTITHTPEADTVYFAY 106
Peptidase_M14 pfam00246
Zinc carboxypeptidase;
334-486 2.42e-13

Zinc carboxypeptidase;


Pssm-ID: 459730 [Multi-domain]  Cd Length: 287  Bit Score: 70.79  E-value: 2.42e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568943134  334 RNMvYVLTITTPLKTSDSKRKAVILTARVHPGETNSSWIMKGFLDYIL---GDSSDARLLRDTFIFKVVPMLNPDGVIVG 410
Cdd:pfam00246  28 RPL-KVLKISSGPGEHNPGKPAVFIDGGIHAREWIGPATALYLIHQLLtnyGRDPEITELLDDTDIYILPVVNPDGYEYT 106
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568943134  411 ------------NYRCSLA-GRDLNRNYTSLLKESFP---------------SVWYTRNMINRLMEKREVILYCDLHGHS 462
Cdd:pfam00246 107 httdrlwrknrsNANGSSCiGVDLNRNFPDHWNEVGAssnpcsetyrgpapfSEPETRAVADFIRSKKPFVLYISLHSYS 186
                         170       180
                  ....*....|....*....|....
gi 568943134  463 RKQNiFMYGCDGSSRSKTKGLYLQ 486
Cdd:pfam00246 187 QVLL-YPYGYTRDEPPPDDEELKS 209
M14_Nna1-like cd18429
Peptidase M14-like domain of ATP/GTP binding proteins and cytosolic carboxypeptidases; ...
354-459 5.34e-11

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: 63.25  E-value: 5.34e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568943134 354 KAVILTARVHPGETNSSWIMKGFLDYILGDSSDARLLRDTFIFKVVPMLNPDGVIVGNYRCSLAGRDLNRNY-----TSL 428
Cdd:cd18429   41 HRVFLRARAHPWEAGGNWVVEGLVERLLQNDEEAKRFLKRYCVYILPMANKDGVARGRTRFNANGKDLNREWdkpadPVL 120
                         90       100       110
                 ....*....|....*....|....*....|.
gi 568943134 429 LKESFPSVWYTRNMINRlmeKREVILYCDLH 459
Cdd:cd18429  121 APENFALEKWLEEMIKA---GKKPDLAIELH 148
Peptidase_M14_like cd00596
M14 family of metallocarboxypeptidases and related proteins; The M14 family of ...
356-460 7.51e-10

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: 59.40  E-value: 7.51e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568943134 356 VILTARVHPGETNSSWIMKGFLDYIL---GDSSDARLLRDTFIFkVVPMLNPDGVIVGNYRCS---LAGRDLNRNYTSLL 429
Cdd:cd00596    1 ILITGGIHGNEVIGVELALALIEYLLenyGNDPLKRLLDNVELW-IVPLVNPDGFARVIDSGGrknANGVDLNRNFPYNW 79
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 568943134 430 KE---SFPSVWY-----------TRNMINrLMEKREVILYCDLHG 460
Cdd:cd00596   80 GKdgtSGPSSPTyrgpapfsepeTQALRD-LAKSHRFDLAVSYHS 123
M14-like cd03857
Peptidase M14-like domain; uncharacterized subfamily; Peptidase M14-like domain of a ...
356-460 2.40e-06

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: 48.61  E-value: 2.40e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568943134 356 VILTARVHPGETNSSWIMKGFLDYILGDSSDARLLRDTFIFKVVPMLNPDG-VIVGNYRCSLA-----------GRDLNR 423
Cdd:cd03857    2 VLLAAQIHGNETTGTEALMELIRDLASESDEAAKLLDNIVILLVPQLNPDGaELFVNFYLDSMnglpgtrynanGIDLNR 81
                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 568943134 424 NYTSLLKESfpsvwytRNMINRLMEKREVILYCDLHG 460
Cdd:cd03857   82 DHVKLTQPE-------TQAVAENFIHWWPDIFIDLHE 111
M14_CP_A-B_like cd03860
Peptidase M14 carboxypeptidase subfamily A/B-like; The Peptidase M14 Carboxypeptidase (CP) A/B ...
347-459 8.65e-06

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: 47.91  E-value: 8.65e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568943134 347 KTSDSKRKAVILTARVHPGEtnssWIMKGFLDYIL-------GDSSDARLLRDTFIFKVVPMLNPDGVI----------- 408
Cdd:cd03860   44 SGGKGGKPAIVIHGGQHARE----WISTSTVEYLAhqllsgyGSDATITALLDKFDFYIIPVVNPDGYVytwttdrlwrk 119
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568943134 409 ----VGNYRCSlaGRDLNRNY--------TSllkeSFP-SVWY----------TRNM---INRLMEKREVILYCDLH 459
Cdd:cd03860  120 nrqpTGGSSCV--GIDLNRNWgykwggpgAS----TNPcSETYrgpsafsapeTKALadfINALAAGQGIKGFIDLH 190
M14-CPA-like cd06227
Peptidase M14 carboxypeptidase A-like domain; uncharacterized subfamily; A functionally ...
356-425 1.04e-05

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: 47.27  E-value: 1.04e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568943134 356 VILTARVHPGETNSSWIMKGFLDYILGDSSD---------ARLLRDTFIFKVVPMLNPDG---VIVGNY--RCSLAGRDL 421
Cdd:cd06227    4 VLLVFGEHARELISVESALRLLRQLCGGLQEpaasalrelAREILDNVELKIIPNANPDGrrlVESGDYcwRGNENGVDL 83

                 ....
gi 568943134 422 NRNY 425
Cdd:cd06227   84 NRNW 87
M14_ASTE_ASPA-like cd06251
Peptidase M14 Succinylglutamate desuccinylase (ASTE)/aspartoacylase (ASPA)-like; ...
354-459 2.97e-04

Peptidase M14 Succinylglutamate desuccinylase (ASTE)/aspartoacylase (ASPA)-like; uncharacterized subgroup; A functionally uncharacterized subgroup of the Succinylglutamate desuccinylase (ASTE)/aspartoacylase (ASPA) subfamily which is part of the M14 family of metallocarboxypeptidases. ASTE catalyzes the fifth and last step in arginine catabolism by the arginine succinyltransferase pathway, and aspartoacylase (ASPA, also known as aminoacylase 2, and ACY-2; EC:3.5.1.15) cleaves N-acetyl L-aspartic acid (NAA) into aspartate and acetate. NAA is abundant in the brain, and hydrolysis of NAA by ASPA may help maintain white matter. ASPA is an NAA scavenger in other tissues. Mutations in the gene encoding ASPA cause Canavan disease (CD), a fatal progressive neurodegenerative disorder involving dysmyelination and spongiform degeneration of white matter in children. This enzyme binds zinc which is necessary for activity. Measurement of elevated NAA levels in urine is used in the diagnosis of CD.


Pssm-ID: 349469 [Multi-domain]  Cd Length: 195  Bit Score: 42.14  E-value: 2.97e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568943134 354 KAVILTARVHPGETNSSWIMKGFLDYIlgdssDARLLRDTFIfkVVPMLNPDGVIVGNYRCSLAGRDLNRNYTSLLKESF 433
Cdd:cd06251   13 PTLLLTAAIHGDELNGIEVIQRLLEDL-----DPSKLRGTLI--AIPVVNPLGFENNSRYLPDDGRDLNRSFPGSEKGSL 85
                         90       100
                 ....*....|....*....|....*.
gi 568943134 434 PSVwYTRNMINRLMEKREVILycDLH 459
Cdd:cd06251   86 ASR-LAHLLWNEIVKKADYVI--DLH 108
M14_CP_bacteria cd18173
bacterial peptidase M14 carboxypeptidase, uncharacterized; This family contains only bacterial ...
349-460 4.65e-04

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: 42.57  E-value: 4.65e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568943134 349 SDSKRKAVILTARVHPGETNSSWIMKGFLDYIL---GDSSDARLLRDTFIFKVVPMLNPDG-VIVGNYRCSLA------G 418
Cdd:cd18173   50 TEEAEPEFKYTSTMHGDETTGYELMLRLIDYLLtnyGTDPRITNLVDNTEIWINPLANPDGtYAGGNNTVSGAtrynanG 129
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 568943134 419 RDLNRNytsllkesFPSVWY------------TRNMINrLMEKREVILYCDLHG 460
Cdd:cd18173  130 VDLNRN--------FPDPVDgdhpdgngwqpeTQAMMN-FADEHNFVLSANFHG 174
M14_MpaA-like cd06904
Peptidase M14-like domain of Escherichia coli Murein Peptide Amidase A and related proteins; ...
346-427 6.54e-04

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: 41.49  E-value: 6.54e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568943134 346 LKTSDSKRKAVILTARVHPGETNSSWIMKGFLDYIlgdsSDARLLRDTFIFkVVPMLNPDGVIVGNyRCSLAGRDLNRNY 425
Cdd:cd06904   16 YKFGPGSRARILIIGGIHGDEPEGVSLVEHLLRWL----KNHPASGDFHIV-VVPCLNPDGLAAGT-RTNANGVDLNRNF 89

                 ..
gi 568943134 426 TS 427
Cdd:cd06904   90 PT 91
M14_CPD_I cd03868
Peptidase M14 carboxypeptidase subfamily N/E-like; Carboxypeptidase D, domain I subgroup; The ...
334-484 1.84e-03

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: 40.69  E-value: 1.84e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568943134 334 RNMvYVLTITTPLKTSDSKRKAVILTARVHPGETNSSWIMKGFLDYILG----DSSDARLLRDTFIFkVVPMLNPDG--- 406
Cdd:cd03868   34 REL-WVLEISDNVNRREPGKPMFKYVANMHGDETVGRQLLIYLAQYLLEnygkDERVTRLVNSTDIH-LMPSMNPDGfen 111
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568943134 407 ----------VIVGnyRCSLAGRDLNRNYTSLLKESFPSVWY-----TRNMINRLMEKREViLYCDLHGHSRKQNifmYG 471
Cdd:cd03868  112 skegdcsgdpGYGG--RENANNVDLNRNFPDQFEDSDDRLLEgrqpeTLAMMKWIVENPFV-LSANLHGGSVVAS---YP 185
                        170
                 ....*....|...
gi 568943134 472 CDGSSRSKTKGLY 484
Cdd:cd03868  186 FDDSPSHIECGVY 198
M14_CPT cd03859
Peptidase M14 Carboxypeptidase T subfamily; Peptidase M14-like domain of carboxypeptidase (CP) ...
376-425 4.79e-03

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: 39.55  E-value: 4.79e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568943134 376 FLDYIL---GDSSDARLLRDTFIFKVVPMLNPDGVIV----GNYR-------------CSLAGRDLNRNY 425
Cdd:cd03859   77 FADYLLenyGTDPRITNLVDNREIWIIPVVNPDGYEYnretGGGRlwrknrrpnngnnPGSDGVDLNRNY 146
COG3608 COG3608
Predicted deacylase [General function prediction only];
354-459 5.03e-03

Predicted deacylase [General function prediction only];


Pssm-ID: 442826 [Multi-domain]  Cd Length: 296  Bit Score: 39.45  E-value: 5.03e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568943134 354 KAVILTARVHPGETNSSWIMKGFLDYIlgdssDARLLRDTFIfkVVPMLNPDGVIVGNYRCSLAGRDLNRNYTSLLKESf 433
Cdd:COG3608   27 PTLLITAGIHGDELNGIEALRRLLREL-----DPGELRGTVI--LVPVANPPGFLQGSRYLPIDGRDLNRSFPGDADGS- 98
                         90       100       110
                 ....*....|....*....|....*....|
gi 568943134 434 psvwYTRNMINRLMekREVILYC----DLH 459
Cdd:COG3608   99 ----LAERIAHALF--EEILPDAdyviDLH 122
M14_CPO cd06247
Peptidase M14 carboxypeptidase subfamily A/B-like; Carboxypeptidase O subgroup; Peptidase M14 ...
334-471 5.92e-03

Peptidase M14 carboxypeptidase subfamily A/B-like; Carboxypeptidase O subgroup; Peptidase M14 carboxypeptidase (CP) O (CPO, also known as metallocarboxypeptidase C; EC 3.4.17.) belongs to the carboxypeptidase A/B subfamily of the M14 family of metallocarboxypeptidases (MCPs). The M14 family are zinc-binding CPs which hydrolyze single, C-terminal amino acids from polypeptide chains, and have a recognition site for the free C-terminal carboxyl group, which is a key determinant of specificity. CPO has not been well characterized as yet, and little is known about it. Based on modeling studies, CPO has been suggested to have specificity for acidic residues rather than aliphatic/aromatic residues as in A-like enzymes or basic residues as in B-like enzymes. It remains to be demonstrated that CPO is functional as an MCP.


Pssm-ID: 349466 [Multi-domain]  Cd Length: 298  Bit Score: 39.06  E-value: 5.92e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568943134 334 RNMvYVLTITTPlktSDSKRKAVILTARVHPGEtnssWIMKGFLDY----ILG----DSSDARLLRDtFIFKVVPMLNPD 405
Cdd:cd06247   37 RPM-YYLKIGWP---SDKPKKIIWMDCGIHARE----WIAPAFCQWfvkeILQnyktDSRLNKLLKN-LDFYVLPVLNID 107
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568943134 406 GVIVG---------------NYRCSlaGRDLNRNYTSllkeSFPSVWYTRN------------------MINRLMEKREV 452
Cdd:cd06247  108 GYIYSwttdrlwrksrsphnNGTCY--GTDLNRNFNS----QWCSIGASRNccsiifcgtgpesepetkAVADLIEKKKS 181
                        170       180
                 ....*....|....*....|
gi 568943134 453 ILYCDLHGHSRKQNIFM-YG 471
Cdd:cd06247  182 DILCYLTIHSYGQLILLpYG 201
M14-like cd06905
Peptidase M14-like domain; uncharacterized subfamily; A functionally uncharacterized subgroup ...
301-406 7.47e-03

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


Pssm-ID: 349476 [Multi-domain]  Cd Length: 359  Bit Score: 39.14  E-value: 7.47e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568943134 301 YTYSNLQEYLSGINSDpvRSKFCKIRVLCHTL-ARNMvYVLTITTPLKTSDSKRKAVILTARVHPGETNSSWIMKGFLDY 379
Cdd:cd06905    7 YTYAELTARLKALAEA--YPNLVRLESIGKSYeGRDI-WLLTITNGETGPADEKPALWVDGNIHGNEVTGSEVALYLAEY 83
                         90       100       110
                 ....*....|....*....|....*....|.
gi 568943134 380 IL----GDSSDARLLrDTFIFKVVPMLNPDG 406
Cdd:cd06905   84 LLtnygKDPEITRLL-DTRTFYILPRLNPDG 113
M14-like cd06242
Peptidase M14-like domain; uncharacterized subgroup; Peptidase M14-like domain of a ...
353-428 8.17e-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 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: 38.44  E-value: 8.17e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568943134 353 RKAVILTARVHPGETNSSWIMKGFLDYILGDSSDARLLRD-TFIfkVVPMLNPDGVIVgNYRCSLAGRDLNRNYTSL 428
Cdd:cd06242    1 KPTVLLVGQQHGNEPAGREAALALARDLAFGDDARELLEKvNVL--VVPRANPDGRAA-NTRGNANGVDLNRDHLLL 74
 
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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