NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|665391217|ref|NP_001285226|]
View 

Nna1 carboxypeptidase, isoform I [Drosophila melanogaster]

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

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

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; ...
 780-1031 2.13e-168

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: 511.84  E-value: 2.13e-168
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391217  780 KSKFCKLRLLCRTLAGNNVYYLTVTAPSSNEENMRRKKSIVVSARVHPSETPASWMMKGLMDFITGDTTVAKRLRHKFIF 859
Cdd:cd06907     1 RSQYCKRRVLCRTLAGNSVYVLTITSPSSNPEEAKAKKAVVLTARVHPGETNASWMMKGFLDFLTGSSPDAKLLRDNFVF 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391217  860 KLVPMLNPDGVIVGNTRNSLTGKDLNRQYRTVIRETYPSIWYTKAMIRRLIEECGVAMYCDMHAHSRKHNIFIYGCENKR 939
Cdd:cd06907    81 KIVPMLNPDGVIVGNYRCSLAGRDLNRNYKTPLKESFPTIWHTKMMIKRLLEEREVILYCDLHGHSRKQNVFMYGCENRK 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391217  940 NPEKKLTEQVFPLMLHKNSADRFSFESCKFKIQRSKEGTGRIVVWMLGITNSYTIEASFGGSSLGSRKGTHFNTQDYEHM 1019
Cdd:cd06907   161 NPEKPLKERVFPLMLSKNAPDKFSFESCKFKVQKSKEGTGRVVMWREGILNSYTLEATFCGSTLGRRKGTHFNTLDFEAM 240

                         250
                  ....*....|..
gi 665391217 1020 GRAFCETLLDYC 1031
Cdd:cd06907   241 GYHFCDTLLDYC 252
Pepdidase_M14_N super family cl39445
Cytosolic carboxypeptidase N-terminal domain; This entry corresponds to the N-terminal domain ...
 623-758 3.06e-17

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: 78.87  E-value: 3.06e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391217   623 FESRFESGNLAKAVQITPTYYELYLRPDlYTSRSKQWFYFRVRRTRRKMlYRFSIVNLvkSDSLYNDGMQPvmYSTlGAK 702
Cdd:pfam18027    1 ISSNFDSGNIEVVSASDPDAIRLRIRPD-NGSEHFQWFYFRVSGARGRP-LTFVIENA--GEASYPDGWTG--YRV-VAS 73

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 665391217   703 EKSEGWRRCGdniCYYRNDdesasssaneddednstytlTFTIEFEHDDDTVFFAH 758
Cdd:pfam18027   74 YDRENWFRVP---TEYDGG--------------------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; ...
 780-1031 2.13e-168

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: 511.84  E-value: 2.13e-168
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391217  780 KSKFCKLRLLCRTLAGNNVYYLTVTAPSSNEENMRRKKSIVVSARVHPSETPASWMMKGLMDFITGDTTVAKRLRHKFIF 859
Cdd:cd06907     1 RSQYCKRRVLCRTLAGNSVYVLTITSPSSNPEEAKAKKAVVLTARVHPGETNASWMMKGFLDFLTGSSPDAKLLRDNFVF 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391217  860 KLVPMLNPDGVIVGNTRNSLTGKDLNRQYRTVIRETYPSIWYTKAMIRRLIEECGVAMYCDMHAHSRKHNIFIYGCENKR 939
Cdd:cd06907    81 KIVPMLNPDGVIVGNYRCSLAGRDLNRNYKTPLKESFPTIWHTKMMIKRLLEEREVILYCDLHGHSRKQNVFMYGCENRK 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391217  940 NPEKKLTEQVFPLMLHKNSADRFSFESCKFKIQRSKEGTGRIVVWMLGITNSYTIEASFGGSSLGSRKGTHFNTQDYEHM 1019
Cdd:cd06907   161 NPEKPLKERVFPLMLSKNAPDKFSFESCKFKVQKSKEGTGRVVMWREGILNSYTLEATFCGSTLGRRKGTHFNTLDFEAM 240

                         250
                  ....*....|..
gi 665391217 1020 GRAFCETLLDYC 1031
Cdd:cd06907   241 GYHFCDTLLDYC 252
MpaA COG2866
Murein tripeptide amidase MpaA [Cell wall/membrane/envelope biogenesis];
762-922 7.78e-24

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


Pssm-ID: 442113 [Multi-domain]  Cd Length: 337  Bit Score: 104.77  E-value: 7.78e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391217  762 YTYSDLQDYLMEIQRhpvKSKFCKLRLLCRTLAGNNVYYLTVTAPSSNeenmrrKKSIVVSARVHPSETPASWMMKGLMD 841
Cdd:COG2866    20 YTYEELLALLAKLAA---ASPLVELESIGKSVEGRPIYLLKIGDPAEG------KPKVLLNAQQHGNEWTGTEALLGLLE 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391217  842 FI-TGDTTVAKRLRHKFIFKLVPMLNPDGVIVgNTRNSLTGKDLNRQYRTVIrETYPSiwyTKAMiRRLIEECGVAMYCD 920
Cdd:COG2866    91 DLlDNYDPLIRALLDNVTLYIVPMLNPDGAER-NTRTNANGVDLNRDWPAPW-LSEPE---TRAL-RDLLDEHDPDFVLD 164


                  ..
gi 665391217  921 MH 922
Cdd:COG2866   165 LH 166
Zn_pept smart00631
Zn_pept domain;
762-1002 3.33e-20

Zn_pept domain;


Pssm-ID: 214748 [Multi-domain]  Cd Length: 277  Bit Score: 92.78  E-value: 3.33e-20
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391217    762 YTYSDLQDYLMEI-QRHPvksKFCKLRLLCRTLAGNNVYYLTVTAPSSneenmRRKKSIVVSARVHPSETPASWMMKGLM 840
Cdd:smart00631    2 HSYEEIEAWLKELaARYP---DLVRLVSIGKSVEGRPIWVLKISNGGS-----HDKPAIFIDAGIHAREWIGPATALYLI 73

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391217    841 DFIT---GDTTVAKRLRHKFIFKLVPMLNPDGVIVGNTRNSL-----------TGKDLNRQY-------RTVIRETYP-- 897
Cdd:smart00631   74 NQLLenyGRDPRVTNLLDKTDIYIVPVLNPDGYEYTHTGDRLwrknrspnsncRGVDLNRNFpfhwgetGNPCSETYAgp 153

                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391217    898 ---SIWYTKAMIRRLIEECGVAMYCDMHAHSRKHNiFIYG-CENKRNPEKKLTEQVFPLM---LHKNSADRFSFE-SCKF 969
Cdd:smart00631  154 spfSEPETKAVRDFIRSNRRFKLYIDLHSYSQLIL-YPYGyTKNDLPPNVDDLDAVAKALakaLASVHGTRYTYGiSNGA 232

                           250       260       270
                    ....*....|....*....|....*....|....*.
gi 665391217    970 KIQRSkegtGRIVVWMLGITN---SYTIEASFGGSS 1002
Cdd:smart00631  233 IYPAS----GGSDDWAYGVLGipfSFTLELRDDGRY 264
Pepdidase_M14_N pfam18027
Cytosolic carboxypeptidase N-terminal domain; This entry corresponds to the N-terminal domain ...
 623-758 3.06e-17

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: 78.87  E-value: 3.06e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391217   623 FESRFESGNLAKAVQITPTYYELYLRPDlYTSRSKQWFYFRVRRTRRKMlYRFSIVNLvkSDSLYNDGMQPvmYSTlGAK 702
Cdd:pfam18027    1 ISSNFDSGNIEVVSASDPDAIRLRIRPD-NGSEHFQWFYFRVSGARGRP-LTFVIENA--GEASYPDGWTG--YRV-VAS 73

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 665391217   703 EKSEGWRRCGdniCYYRNDdesasssaneddednstytlTFTIEFEHDDDTVFFAH 758
Cdd:pfam18027   74 YDRENWFRVP---TEYDGG--------------------VLTITHTPEADTVYFAY 106
Peptidase_M14 pfam00246
Zinc carboxypeptidase;
791-934 4.37e-10

Zinc carboxypeptidase;


Pssm-ID: 459730 [Multi-domain]  Cd Length: 287  Bit Score: 62.70  E-value: 4.37e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391217   791 RTLAGNNVYYLTVTAPSSneENMRRKKSIVVSARVHPSETPAS----WMMKGLMDFITGDTTVaKRLRHKFIFKLVPMLN 866
Cdd:pfam00246   23 KSVEGRPLKVLKISSGPG--EHNPGKPAVFIDGGIHAREWIGPatalYLIHQLLTNYGRDPEI-TELLDDTDIYILPVVN 99

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391217   867 PDGVIVGNTRNSL-------------TGKDLNRQY----------RTVIRETY-----PSIWYTKAMIRRLIEECGVAMY 918
Cdd:pfam00246  100 PDGYEYTHTTDRLwrknrsnangsscIGVDLNRNFpdhwnevgasSNPCSETYrgpapFSEPETRAVADFIRSKKPFVLY 179

                          170
                   ....*....|....*.
gi 665391217   919 CDMHAHSRKHNiFIYG 934
Cdd:pfam00246  180 ISLHSYSQVLL-YPYG 194
 
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; ...
 780-1031 2.13e-168

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: 511.84  E-value: 2.13e-168
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391217  780 KSKFCKLRLLCRTLAGNNVYYLTVTAPSSNEENMRRKKSIVVSARVHPSETPASWMMKGLMDFITGDTTVAKRLRHKFIF 859
Cdd:cd06907     1 RSQYCKRRVLCRTLAGNSVYVLTITSPSSNPEEAKAKKAVVLTARVHPGETNASWMMKGFLDFLTGSSPDAKLLRDNFVF 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391217  860 KLVPMLNPDGVIVGNTRNSLTGKDLNRQYRTVIRETYPSIWYTKAMIRRLIEECGVAMYCDMHAHSRKHNIFIYGCENKR 939
Cdd:cd06907    81 KIVPMLNPDGVIVGNYRCSLAGRDLNRNYKTPLKESFPTIWHTKMMIKRLLEEREVILYCDLHGHSRKQNVFMYGCENRK 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391217  940 NPEKKLTEQVFPLMLHKNSADRFSFESCKFKIQRSKEGTGRIVVWMLGITNSYTIEASFGGSSLGSRKGTHFNTQDYEHM 1019
Cdd:cd06907   161 NPEKPLKERVFPLMLSKNAPDKFSFESCKFKVQKSKEGTGRVVMWREGILNSYTLEATFCGSTLGRRKGTHFNTLDFEAM 240

                         250
                  ....*....|..
gi 665391217 1020 GRAFCETLLDYC 1031
Cdd:cd06907   241 GYHFCDTLLDYC 252
M14_AGTPBP-like cd06235
Peptidase M14-like domain of human Nna1/AGTPBP-1, AGBL2 -5, and related proteins; Subgroup of ...
 783-1029 1.29e-88

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: 289.36  E-value: 1.29e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391217  783 FCKLRLLCRTLAGNNVYYLTVTAPSSNEENMR-----RKKSIVVSARVHPSETPASWMMKGLMDFITGDTTVAKRLRHKF 857
Cdd:cd06235     2 YFEREVLCHSLDGRKLDLLTITSPNNKKLGPYprefaGKKVVFLSGRVHPGETPASFVMKGFLDFLLSNDPRAQLLREHF 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391217  858 IFKLVPMLNPDGVIVGNTRNSLTGKDLNRQYRTVIRETYPSIWYTKAMIRRLIE--ECGVAMYCDMHAHSRKHNIFIYGC 935
Cdd:cd06235    82 VFKIVPMLNPDGVIRGNYRCSLNGFNLNRHYKNPDPELHPTIYGAKKVIDYLQKtyKRRVLMYCDFHGHSSKSNGFMYGN 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391217  936 ENKrNPEKKLTEQVFPLMLHKNSADRFSFESCKFKIQRSKEGTGRIVVW-MLGITNSYTIEASFGGSSLG-SRKGTHFNT 1013
Cdd:cd06235   162 SFP-DTVQFHWNMVFPKILSLNAPDFFSSSCCSFGVMKSKEGTGRVVFGrRLIHSHSYTLESTFFSNNRGnIDGACGYTE 240

                         250
                  ....*....|....*.
gi 665391217 1014 QDYEHMGRAFCETLLD 1029
Cdd:cd06235   241 ENLEDLGYSVASTLLD 256
M14_Nna1 cd06906
Peptidase M14-like domain of ATP/GTP binding proteins and cytosolic carboxypeptidases; ...
 789-1028 1.00e-77

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: 258.85  E-value: 1.00e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391217  789 LCRTLAGNNVYYLTVTA-PSSNEEN----MRRKKSIVVSARVHPSETPASWMMKGLMDFITGDTTVAKRLRHKFIFKLVP 863
Cdd:cd06906    10 LCETLGGNSCPVLTITAmPESNNEEhicqFRNRPYIFLSARVHPGESNASWVMKGTLDFLLSSSPAAQSLRESYIFKIVP 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391217  864 MLNPDGVIVGNTRNSLTGKDLNRQYRTVIRETYPSIWYTKAMIR--RLIEECGVaMYCDMHAHSRKHNIFIYGCENK--- 938
Cdd:cd06906    90 MLNPDGVINGNHRCSLSGEDLNRRWLNPNPELHPTIYHTKGLLQylRSIGRLPL-VYCDYHGHSRKKNVFMYGCSPKesw 168

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391217  939 -----RNPEKKLTEQV----FPLMLHkNSADRFSFESCKFKIQRSKEGTGRIVVW-MLGITNSYTIEASFGGSSLGSRKG 1008
Cdd:cd06906   169 shgdtNNPSGDIVEDLgyrtLPKLLS-HFAPAFSLSSCSFVVEKSKESTARVVVWrEIGVLRSYTMESTYCGCDQGKYKG 247

                         250       260
                  ....*....|....*....|
gi 665391217 1009 THFNTQDYEHMGRAFCETLL 1028
Cdd:cd06906   248 LHIGTRELEEMGARFCEALL 267
M14_AGBL4_like cd06908
Peptidase M14-like domain of ATP/GTP binding protein AGBL-4 and related proteins; Peptidase ...
 788-1030 3.57e-63

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: 216.40  E-value: 3.57e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391217  788 LLCRTLAGNNVYYLTVTAPSSNEENMR-RKKSIVVSARVHPSETPASWMMKGLMDFITGDTTVAKRLRHKFIFKLVPMLN 866
Cdd:cd06908     7 LLGKSVQQRRLDLLTITDPVNKHLTVEkKKKVVFITARVHPGETPSSFVCQGLIDFLVSNHPVAKVLRDHLVFKIVPMLN 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391217  867 PDGVIVGNTRNSLTGKDLNRQYRTVIRETYPSIWYTKAMIRRLIEE--CGVAMYCDMHAHSRKHNIFIYGceNKRNPEKK 944
Cdd:cd06908    87 PDGVFLGNYRCSLMGFDLNRHWHEPSPWAHPTLYAVKNLLRELDNDptVQLDFYIDIHAHSTLMNGFMYG--NIYDDVYR 164

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391217  945 LTEQ-VFPLMLHKNSADrFSFESCKFKIQRSKEGTGRIVvwmLG-----ITNSYTIEASFGGSSLGSRKG-THFNTQDYE 1017
Cdd:cd06908   165 FERQaVFPKLLCQNAED-FSLSNTVFNRDPVKAGTGRRF---LGgllddTANCYTLEVSFYSYRLSDSSSaTPYTEEGYM 240

                         250
                  ....*....|...
gi 665391217 1018 HMGRAFCETLLDY 1030
Cdd:cd06908   241 KLGRNMARALLDY 253
M14_AGBL5_like cd06236
Peptidase M14-like domain of ATP/GTP binding protein (AGBL)-5 and related proteins; Peptidase ...
 788-1035 1.66e-52

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: 185.93  E-value: 1.66e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391217  788 LLCRTLAGNNVYYLTVTAP---SSNEENMRR----------------KKSIVVSARVHPSETPASWMMKGLMDFITG-DT 847
Cdd:cd06236    13 LLCYSLEGRRVDLLTITSChgvTEEREERLPnlfpdtskprphkfegKKVVFISARVHPGETPSSFVFNGFLEFLLRpDD 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391217  848 TVAKRLRHKFIFKLVPMLNPDGVIVGNTRNSLTGKDLNRQYRTVIRETYPSIWYTKAMIrrlieecgvaMYCDMHAHSRK 927
Cdd:cd06236    93 PRAIALRRLFVFKLIPMLNPDGVARGHYRTDTRGVNLNRVYLNPDPELHPSIYAAKALL----------FYIDLHAHASK 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391217  928 HNIFIYGcenkrNPEKKLTEQV----FPLMLHKNSAdRFSFESCKF----------KIQRSKEGTGRIVVW-MLGITNSY 992
Cdd:cd06236   163 RGCFIYG-----NALEDEEQQVenllYPKLISLNSA-HFDFDACNFseknmysrdkRDGLSKEGSGRVALYkATGIVHSY 236

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 665391217  993 TIEASFggsslgsrkgthfntqDYEHMGRAFCETLLDYCDENP 1035
Cdd:cd06236   237 TLECNY----------------HFEDVGRALAVALLDMLGCNP 263
M14_Nna1-like cd03856
Peptidase M14-like domain of ATP/GTP binding proteins, cytosolic carboxypeptidases and related ...
 816-998 1.49e-33

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: 130.78  E-value: 1.49e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391217  816 KKSIVVSARVHPSETPASWMMKGLMDFITGDTTVAKRLRHKFIFKLVPMLNPDGVIVGNTRNSLTGKDLNRQYRTVIRET 895
Cdd:cd03856    43 KSWLFLIARQHPGETTGAWVFFGFLDQLLSDDDPAQQLRAEYNFYIIPMVNPDGVARGHWRTNSRGMDLNRDWHAPDALL 122

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391217  896 YPSIWYTKA-MIRRLIEECGVAMYCDMHAHSRkhNIFIYGCENKRNPekklTEQVFPLMLHKNSaDRFSFEScKFKIQRS 974
Cdd:cd03856   123 SPETYAVAAaLAERVQSPEGVVLALDLHGDNR--NVFLTGPDNKDES----TNHNPDKLNSLLT-ETDRRLP-DYNTEAS 194

                         170       180       190
                  ....*....|....*....|....*....|
gi 665391217  975 KEGTGRIVV---WM---LGITNSYTIEASF 998
Cdd:cd03856   195 PGDNPGGTVgkqWIadvYQITHSVTLEVGD 224
M14_PaCCP-like cd06234
Peptidase M14-like domain of ATP/GTP binding proteins and cytosolic carboxypeptidases similar ...
 762-950 7.59e-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: 123.06  E-value: 7.59e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391217  762 YTYSDLQDYLMEIQRHPvkskFCKLRLLCRTLAGNNVYYLTVTAPSSNeenmrrKKSIVVSARVHPSETPASWMMKGLMD 841
Cdd:cd06234     1 YSYERHLDLVARAQASP----GVRLEVLGQTLDGRDIDLLTIGDPGTG------KKKVWIIARQHPGETMAEWFMEGLLD 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391217  842 FITG-DTTVAKRLRHKFIFKLVPMLNPDGVIVGNTRNSLTGKDLNRQYRTVIRETYPSIWYtkamIRRLIEECGVAMYCD 920
Cdd:cd06234    71 RLLDeDDPVSRALLEKAVFYVVPNMNPDGSVRGNLRTNAAGVNLNREWANPSLERSPEVFA----VRQAMDATGVDFFLD 146

                         170       180       190
                  ....*....|....*....|....*....|..
gi 665391217  921 MHAHSRKHNIFIYGCEN--KRNPEKKLTEQVF 950
Cdd:cd06234   147 VHGDEALPYNFIAGAEGipSWTPRLAALEAAF 178
MpaA COG2866
Murein tripeptide amidase MpaA [Cell wall/membrane/envelope biogenesis];
762-922 7.78e-24

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


Pssm-ID: 442113 [Multi-domain]  Cd Length: 337  Bit Score: 104.77  E-value: 7.78e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391217  762 YTYSDLQDYLMEIQRhpvKSKFCKLRLLCRTLAGNNVYYLTVTAPSSNeenmrrKKSIVVSARVHPSETPASWMMKGLMD 841
Cdd:COG2866    20 YTYEELLALLAKLAA---ASPLVELESIGKSVEGRPIYLLKIGDPAEG------KPKVLLNAQQHGNEWTGTEALLGLLE 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391217  842 FI-TGDTTVAKRLRHKFIFKLVPMLNPDGVIVgNTRNSLTGKDLNRQYRTVIrETYPSiwyTKAMiRRLIEECGVAMYCD 920
Cdd:COG2866    91 DLlDNYDPLIRALLDNVTLYIVPMLNPDGAER-NTRTNANGVDLNRDWPAPW-LSEPE---TRAL-RDLLDEHDPDFVLD 164


                  ..
gi 665391217  921 MH 922
Cdd:COG2866   165 LH 166
Zn_pept smart00631
Zn_pept domain;
762-1002 3.33e-20

Zn_pept domain;


Pssm-ID: 214748 [Multi-domain]  Cd Length: 277  Bit Score: 92.78  E-value: 3.33e-20
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391217    762 YTYSDLQDYLMEI-QRHPvksKFCKLRLLCRTLAGNNVYYLTVTAPSSneenmRRKKSIVVSARVHPSETPASWMMKGLM 840
Cdd:smart00631    2 HSYEEIEAWLKELaARYP---DLVRLVSIGKSVEGRPIWVLKISNGGS-----HDKPAIFIDAGIHAREWIGPATALYLI 73

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391217    841 DFIT---GDTTVAKRLRHKFIFKLVPMLNPDGVIVGNTRNSL-----------TGKDLNRQY-------RTVIRETYP-- 897
Cdd:smart00631   74 NQLLenyGRDPRVTNLLDKTDIYIVPVLNPDGYEYTHTGDRLwrknrspnsncRGVDLNRNFpfhwgetGNPCSETYAgp 153

                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391217    898 ---SIWYTKAMIRRLIEECGVAMYCDMHAHSRKHNiFIYG-CENKRNPEKKLTEQVFPLM---LHKNSADRFSFE-SCKF 969
Cdd:smart00631  154 spfSEPETKAVRDFIRSNRRFKLYIDLHSYSQLIL-YPYGyTKNDLPPNVDDLDAVAKALakaLASVHGTRYTYGiSNGA 232

                           250       260       270
                    ....*....|....*....|....*....|....*.
gi 665391217    970 KIQRSkegtGRIVVWMLGITN---SYTIEASFGGSS 1002
Cdd:smart00631  233 IYPAS----GGSDDWAYGVLGipfSFTLELRDDGRY 264
M14_Nna1-like cd06237
Peptidase M14-like domain of ATP/GTP binding proteins and cytosolic carboxypeptidases; ...
 765-931 8.71e-20

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: 90.70  E-value: 8.71e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391217  765 SDLQDYLMEIQRHPvkskFCKLRLLCRTLAGNNVYYLTVTAPSSneenmrrKKSIVVSARVHPSETPASWMMKGLMDFIT 844
Cdd:cd06237     1 ADYDAWIDSLAKKP----FVKRSTIGKSVEGRPIEALTIGNPDS-------KELVVLLGRQHPPEVTGALAMQAFVETLL 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391217  845 GDTTVAKRLRHKFIFKLVPMLNPDGVIVGNTRNSLTGKDLNRQyrtviretypsiWY------TKAM---IRRLIEECGV 915
Cdd:cd06237    70 ADTELAKAFRARFRVLVVPLLNPDGVDLGHWRHNAGGVDLNRD------------WGpftqpeTRAVrdfLLELVEEPGG 137

                         170
                  ....*....|....*.
gi 665391217  916 AMYCDMHAHSRKHNIF 931
Cdd:cd06237   138 KVVFGLDFHSTWEDVF 153
Pepdidase_M14_N pfam18027
Cytosolic carboxypeptidase N-terminal domain; This entry corresponds to the N-terminal domain ...
 623-758 3.06e-17

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: 78.87  E-value: 3.06e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391217   623 FESRFESGNLAKAVQITPTYYELYLRPDlYTSRSKQWFYFRVRRTRRKMlYRFSIVNLvkSDSLYNDGMQPvmYSTlGAK 702
Cdd:pfam18027    1 ISSNFDSGNIEVVSASDPDAIRLRIRPD-NGSEHFQWFYFRVSGARGRP-LTFVIENA--GEASYPDGWTG--YRV-VAS 73

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 665391217   703 EKSEGWRRCGdniCYYRNDdesasssaneddednstytlTFTIEFEHDDDTVFFAH 758
Cdd:pfam18027   74 YDRENWFRVP---TEYDGG--------------------VLTITHTPEADTVYFAY 106
M14_Nna1-like cd18429
Peptidase M14-like domain of ATP/GTP binding proteins and cytosolic carboxypeptidases; ...
 766-888 4.04e-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: 65.56  E-value: 4.04e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391217  766 DLQDYLMEIQrhpvKSKFCKLRLLCRTLAGNNVYYLTVTAPSSneenmrrKKSIVVSARVHPSETPASWMMKGLMDFITG 845
Cdd:cd18429     1 DLDRLLAKIR----KNPLVEITTIGKTVEGRPLEIIRIGNESA-------PHRVFLRARAHPWEAGGNWVVEGLVERLLQ 69

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 665391217  846 DTTVAKRLRHKFIFKLVPMLNPDGVIVGNTRNSLTGKDLNRQY 888
Cdd:cd18429    70 NDEEAKRFLKRYCVYILPMANKDGVARGRTRFNANGKDLNREW 112
Peptidase_M14 pfam00246
Zinc carboxypeptidase;
791-934 4.37e-10

Zinc carboxypeptidase;


Pssm-ID: 459730 [Multi-domain]  Cd Length: 287  Bit Score: 62.70  E-value: 4.37e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391217   791 RTLAGNNVYYLTVTAPSSneENMRRKKSIVVSARVHPSETPAS----WMMKGLMDFITGDTTVaKRLRHKFIFKLVPMLN 866
Cdd:pfam00246   23 KSVEGRPLKVLKISSGPG--EHNPGKPAVFIDGGIHAREWIGPatalYLIHQLLTNYGRDPEI-TELLDDTDIYILPVVN 99

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391217   867 PDGVIVGNTRNSL-------------TGKDLNRQY----------RTVIRETY-----PSIWYTKAMIRRLIEECGVAMY 918
Cdd:pfam00246  100 PDGYEYTHTTDRLwrknrsnangsscIGVDLNRNFpdhwnevgasSNPCSETYrgpapFSEPETRAVADFIRSKKPFVLY 179

                          170
                   ....*....|....*.
gi 665391217   919 CDMHAHSRKHNiFIYG 934
Cdd:pfam00246  180 ISLHSYSQVLL-YPYG 194
M14-like cd03857
Peptidase M14-like domain; uncharacterized subfamily; Peptidase M14-like domain of a ...
 819-901 1.94e-05

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: 47.45  E-value: 1.94e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391217  819 IVVSARVHPSETPASwmmKGLMDFI----TGDTTVAKRLRhKFIFKLVPMLNPDG------------VIVGNTRNSLTGK 882
Cdd:cd03857     2 VLLAAQIHGNETTGT---EALMELIrdlaSESDEAAKLLD-NIVILLVPQLNPDGaelfvnfyldsmNGLPGTRYNANGI 77

                          90       100       110
                  ....*....|....*....|....*....|
gi 665391217  883 DLNR-----------QYRTVIRETYPSIWY 901
Cdd:cd03857    78 DLNRdhvkltqpetqAVAENFIHWWPDIFI 107
M14_REP34-like cd06231
Peptidase M14-like domain similar to rapid encystment phenotype 34 (REP34); This family ...
 814-890 3.98e-05

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


Pssm-ID: 349450 [Multi-domain]  Cd Length: 239  Bit Score: 47.30  E-value: 3.98e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 665391217  814 RRKKSIVVSARVHPSETPASWmmkGLMDFITgdtTVAKRLRHKFIFKLVPMLNPDGvIVGNTRNSLTGKDLNRQYRT 890
Cdd:cd06231    40 GDKPRVLISAGIHGDEPAGVE---ALLRFLE---SLAEKYLRRVNLLVLPCVNPWG-FERNTRENADGIDLNRSFLK 109
M14_CP_A-B_like cd03860
Peptidase M14 carboxypeptidase subfamily A/B-like; The Peptidase M14 Carboxypeptidase (CP) A/B ...
 763-925 5.14e-04

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: 44.05  E-value: 5.14e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391217  763 TYSDLQDYLMEIQ-RHPvksKFCKLRLLCRTLAGNNVYYLTVTAPSSNEEnmrrKKSIVVSARVHPSE--TPAS--WMMK 837
Cdd:cd03860     3 PLDDIVQWLDDLAaAFP---DNVEIFTIGKSYEGRDITGIHIWGSGGKGG----KPAIVIHGGQHAREwiSTSTveYLAH 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391217  838 GLMDFITGDTTVAKRLRhKFIFKLVPMLNPDGVIVGNTRNSL-------------TGKDLNRQY----------RTVIRE 894
Cdd:cd03860    76 QLLSGYGSDATITALLD-KFDFYIIPVVNPDGYVYTWTTDRLwrknrqptggsscVGIDLNRNWgykwggpgasTNPCSE 154

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 665391217  895 TYP-----SIWYTKAM---IRRLIEECGVAMYCDMHAHS 925
Cdd:cd03860   155 TYRgpsafSAPETKALadfINALAAGQGIKGFIDLHSYS 193
M14_CP_bacteria cd18173
bacterial peptidase M14 carboxypeptidase, uncharacterized; This family contains only bacterial ...
 759-888 5.66e-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: 44.11  E-value: 5.66e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391217  759 SYPyTYSDLQDYLMEI-QRHPvksKFCKLRLLCRTLAGNNVYYLTVTAPSSNEENmrrKKSIVVSARVHPSETPASWMMK 837
Cdd:cd18173     3 SYP-TYEEYEAMMQSFaANYP---NICRLVSIGTSVQGRKLLALKISDNVNTEEA---EPEFKYTSTMHGDETTGYELML 75

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 665391217  838 GLMDFIT---GDTTVAKRLRHKFIFKLVPMLNPDG-------VIVGNTRNSLTGKDLNRQY 888
Cdd:cd18173    76 RLIDYLLtnyGTDPRITNLVDNTEIWINPLANPDGtyaggnnTVSGATRYNANGVDLNRNF 136
Peptidase_M14_like cd00596
M14 family of metallocarboxypeptidases and related proteins; The M14 family of ...
 819-1012 1.40e-03

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: 42.06  E-value: 1.40e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391217  819 IVVSARVHPSETPASWMMKGLMDFITGD--TTVAKRLRHKFIFKLVPMLNPDG---VIVGNTRNSLTGKDLNRQYRT--- 890
Cdd:cd00596     1 ILITGGIHGNEVIGVELALALIEYLLENygNDPLKRLLDNVELWIVPLVNPDGfarVIDSGGRKNANGVDLNRNFPYnwg 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391217  891 VIRETYPSIWYTK----------AMIRRLIEECGVAMYCDMhaHSRKHNIFI-YGCENKRNPEKKLTEQVFPLMLHKNSA 959
Cdd:cd00596    81 KDGTSGPSSPTYRgpapfsepetQALRDLAKSHRFDLAVSY--HSSSEAILYpYGYTNEPPPDFSEFQELAAGLARALGA 158

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 665391217  960 DRFSFESCKFKIQRSkeGTGRIvvWMLGITN--SYTIEasfGGSSLGSRKGTHFN 1012
Cdd:cd00596   159 GEYGYGYSYTWYSTT--GTADD--WLYGELGilAFTVE---LGTADYPLPGTLLD 206
M14-like cd06244
Peptidase M14-like domain; uncharacterized subgroup; Peptidase M14-like domain of a ...
 819-922 2.22e-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: 349463 [Multi-domain]  Cd Length: 223  Bit Score: 41.67  E-value: 2.22e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665391217  819 IVVSARVHPSETPAS-WMMKGLMDFITGDTTVAKRLRHKF----------------IFKLVPMLNPDGViVGNTRNSLTG 881
Cdd:cd06244     2 PIVYNNIHGNEVEGVdALLEFLEMLATEPNVTYNTLVKYYkvenvdlevkdllddvFFIVVPTENPDGR-VANTRTNANG 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 665391217  882 KDLNRQYrtvireTYPSIWYTKAMIRRLIEECGVAMYcDMH 922
Cdd:cd06244    81 FDLNRDN------AYQTQPETRAMQELISKWNPVTFL-DMH 114
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH