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Conserved domains on  [gi|118421091|ref|NP_068603|]
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cytosolic carboxypeptidase-like protein 5 isoform 1 [Homo sapiens]

Protein Classification

cytosolic carboxypeptidase-like protein 5( domain architecture ID 15732921)

cytosolic carboxypeptidase-like protein 5 is an M14 family metallopeptidase that mediates the deglutamylation of tubulin and non-tubulin target proteins; it catalyzes the removal of polyglutamate side chains present on the gamma-carboxyl group of glutamate residues within the C-terminal tail of alpha- and beta-tubulin

CATH:  3.40.630.10
EC:  3.4.17.-
MEROPS:  M14
PubMed:  7674922|10493853

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
M14_AGBL5_like cd06236
Peptidase M14-like domain of ATP/GTP binding protein (AGBL)-5 and related proteins; Peptidase ...
183-574 5.91e-169

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: 490.62  E-value: 5.91e-169
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118421091 183 SSPLDTIYYHRELLCYSLDGLRVDLLTITSCHGLREDREPRLEQLFPDTSTPRPFRFAGKRIFFLSSRVHPGETPSSFVF 262
Cdd:cd06236    1 KSPESDIYYHRELLCYSLEGRRVDLLTITSCHGVTEEREERLPNLFPDTSKPRPHKFEGKKVVFISARVHPGETPSSFVF 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118421091 263 NGFLDFILRPDDPRAQTLRRLFVFKLIPMLNPDGVVRGHYRTDSRGVNLNRQYLKPDAVLHPAIYGAKAVLlyhhvhsrl 342
Cdd:cd06236   81 NGFLEFLLRPDDPRAIALRRLFVFKLIPMLNPDGVARGHYRTDTRGVNLNRVYLNPDPELHPSIYAAKALL--------- 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118421091 343 nsqsssehqpssclppdapvsdlekannlqneaqcghsadrhnaeawkqtepaeqklnsvwimpqqsagleesapdtipp 422
Cdd:cd06236      --------------------------------------------------------------------------------
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118421091 423 kesgvaYYVDLHGHASKRGCFMYGNSFSDESTQVENMLYPKLISLNSAHFDFQGCNFSEKNMYARDRRDGQSKEGSGRVA 502
Cdd:cd06236  152 ------FYIDLHAHASKRGCFIYGNALEDEEQQVENLLYPKLISLNSAHFDFDACNFSEKNMYSRDKRDGLSKEGSGRVA 225
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 118421091 503 IYKASGIIHSYTLECNYntgrsvnsipaachdngraspppppafpsrytveLFEQVGRAMAIAALDMAECNP 574
Cdd:cd06236  226 LYKATGIVHSYTLECNY----------------------------------HFEDVGRALAVALLDMLGCNP 263
Pepdidase_M14_N super family cl39445
Cytosolic carboxypeptidase N-terminal domain; This entry corresponds to the N-terminal domain ...
10-155 5.92e-06

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: 45.74  E-value: 5.92e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118421091   10 FSSRFDSGNLAHVEkveslssdgegvgggasaltsgiASSPDyEFNVWTRPDcAETEFengnRSWFYFSVRGGmPGKLIK 89
Cdd:pfam18027   1 ISSNFDSGNIEVVS-----------------------ASDPD-AIRLRIRPD-NGSEH----FQWFYFRVSGA-RGRPLT 50
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118421091   90 INIMNMNKQSklYSQGMAPFVRTLPT-RPRWERIrdrptfemtETQF---VLSFVHRFVegrGATTFFAF 155
Cdd:pfam18027  51 FVIENAGEAS--YPDGWTGYRVVASYdRENWFRV---------PTEYdggVLTITHTPE---ADTVYFAY 106
 
Name Accession Description Interval E-value
M14_AGBL5_like cd06236
Peptidase M14-like domain of ATP/GTP binding protein (AGBL)-5 and related proteins; Peptidase ...
183-574 5.91e-169

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: 490.62  E-value: 5.91e-169
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118421091 183 SSPLDTIYYHRELLCYSLDGLRVDLLTITSCHGLREDREPRLEQLFPDTSTPRPFRFAGKRIFFLSSRVHPGETPSSFVF 262
Cdd:cd06236    1 KSPESDIYYHRELLCYSLEGRRVDLLTITSCHGVTEEREERLPNLFPDTSKPRPHKFEGKKVVFISARVHPGETPSSFVF 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118421091 263 NGFLDFILRPDDPRAQTLRRLFVFKLIPMLNPDGVVRGHYRTDSRGVNLNRQYLKPDAVLHPAIYGAKAVLlyhhvhsrl 342
Cdd:cd06236   81 NGFLEFLLRPDDPRAIALRRLFVFKLIPMLNPDGVARGHYRTDTRGVNLNRVYLNPDPELHPSIYAAKALL--------- 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118421091 343 nsqsssehqpssclppdapvsdlekannlqneaqcghsadrhnaeawkqtepaeqklnsvwimpqqsagleesapdtipp 422
Cdd:cd06236      --------------------------------------------------------------------------------
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118421091 423 kesgvaYYVDLHGHASKRGCFMYGNSFSDESTQVENMLYPKLISLNSAHFDFQGCNFSEKNMYARDRRDGQSKEGSGRVA 502
Cdd:cd06236  152 ------FYIDLHAHASKRGCFIYGNALEDEEQQVENLLYPKLISLNSAHFDFDACNFSEKNMYSRDKRDGLSKEGSGRVA 225
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 118421091 503 IYKASGIIHSYTLECNYntgrsvnsipaachdngraspppppafpsrytveLFEQVGRAMAIAALDMAECNP 574
Cdd:cd06236  226 LYKATGIVHSYTLECNY----------------------------------HFEDVGRALAVALLDMLGCNP 263
MpaA COG2866
Murein tripeptide amidase MpaA [Cell wall/membrane/envelope biogenesis];
159-320 1.25e-20

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


Pssm-ID: 442113 [Multi-domain]  Cd Length: 337  Bit Score: 94.37  E-value: 1.25e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118421091 159 FSYSDCQELLNQLDQRFPenhpthsspldtiYYHRELLCYSLDGLRVDLLTITSchglredreprleqlfpdtstprpfR 238
Cdd:COG2866   20 YTYEELLALLAKLAAASP-------------LVELESIGKSVEGRPIYLLKIGD-------------------------P 61
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118421091 239 FAGKRIFFLSSRVHPGETPSSFVFNGFLDFILRPDDPRAQTLRRLFVFKLIPMLNPDGVVRgHYRTDSRGVNLNRQYLKP 318
Cdd:COG2866   62 AEGKPKVLLNAQQHGNEWTGTEALLGLLEDLLDNYDPLIRALLDNVTLYIVPMLNPDGAER-NTRTNANGVDLNRDWPAP 140

                 ..
gi 118421091 319 DA 320
Cdd:COG2866  141 WL 142
Zn_pept smart00631
Zn_pept domain;
160-315 7.04e-10

Zn_pept domain;


Pssm-ID: 214748 [Multi-domain]  Cd Length: 277  Bit Score: 60.81  E-value: 7.04e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118421091   160 SYSDCQELLNQLDQRFPEnhpthsspldtiYYHRELLCYSLDGLRVDLLTITSCHGlredreprleqlfpdtstprpfrf 239
Cdd:smart00631   3 SYEEIEAWLKELAARYPD------------LVRLVSIGKSVEGRPIWVLKISNGGS------------------------ 46
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118421091   240 AGKRIFFLSSRVHPGETPSSFVFNGFLDFILRP--DDPRAQTLRRLFVFKLIPMLNPDGVVRGH-----------YRTDS 306
Cdd:smart00631  47 HDKPAIFIDAGIHAREWIGPATALYLINQLLENygRDPRVTNLLDKTDIYIVPVLNPDGYEYTHtgdrlwrknrsPNSNC 126

                   ....*....
gi 118421091   307 RGVNLNRQY 315
Cdd:smart00631 127 RGVDLNRNF 135
Peptidase_M14 pfam00246
Zinc carboxypeptidase;
232-315 1.27e-09

Zinc carboxypeptidase;


Pssm-ID: 459730 [Multi-domain]  Cd Length: 287  Bit Score: 60.39  E-value: 1.27e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118421091  232 STPRPFRFAGKRIFFLSSRVHPGETPSSFVFNGFLDFILRP--DDPRAQTLRRLFVFKLIPMLNPDGVVRGHY------- 302
Cdd:pfam00246  36 SSGPGEHNPGKPAVFIDGGIHAREWIGPATALYLIHQLLTNygRDPEITELLDDTDIYILPVVNPDGYEYTHTtdrlwrk 115
                          90
                  ....*....|....*....
gi 118421091  303 -RTDSR-----GVNLNRQY 315
Cdd:pfam00246 116 nRSNANgssciGVDLNRNF 134
Pepdidase_M14_N pfam18027
Cytosolic carboxypeptidase N-terminal domain; This entry corresponds to the N-terminal domain ...
10-155 5.92e-06

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: 45.74  E-value: 5.92e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118421091   10 FSSRFDSGNLAHVEkveslssdgegvgggasaltsgiASSPDyEFNVWTRPDcAETEFengnRSWFYFSVRGGmPGKLIK 89
Cdd:pfam18027   1 ISSNFDSGNIEVVS-----------------------ASDPD-AIRLRIRPD-NGSEH----FQWFYFRVSGA-RGRPLT 50
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118421091   90 INIMNMNKQSklYSQGMAPFVRTLPT-RPRWERIrdrptfemtETQF---VLSFVHRFVegrGATTFFAF 155
Cdd:pfam18027  51 FVIENAGEAS--YPDGWTGYRVVASYdRENWFRV---------PTEYdggVLTITHTPE---ADTVYFAY 106
 
Name Accession Description Interval E-value
M14_AGBL5_like cd06236
Peptidase M14-like domain of ATP/GTP binding protein (AGBL)-5 and related proteins; Peptidase ...
183-574 5.91e-169

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: 490.62  E-value: 5.91e-169
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118421091 183 SSPLDTIYYHRELLCYSLDGLRVDLLTITSCHGLREDREPRLEQLFPDTSTPRPFRFAGKRIFFLSSRVHPGETPSSFVF 262
Cdd:cd06236    1 KSPESDIYYHRELLCYSLEGRRVDLLTITSCHGVTEEREERLPNLFPDTSKPRPHKFEGKKVVFISARVHPGETPSSFVF 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118421091 263 NGFLDFILRPDDPRAQTLRRLFVFKLIPMLNPDGVVRGHYRTDSRGVNLNRQYLKPDAVLHPAIYGAKAVLlyhhvhsrl 342
Cdd:cd06236   81 NGFLEFLLRPDDPRAIALRRLFVFKLIPMLNPDGVARGHYRTDTRGVNLNRVYLNPDPELHPSIYAAKALL--------- 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118421091 343 nsqsssehqpssclppdapvsdlekannlqneaqcghsadrhnaeawkqtepaeqklnsvwimpqqsagleesapdtipp 422
Cdd:cd06236      --------------------------------------------------------------------------------
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118421091 423 kesgvaYYVDLHGHASKRGCFMYGNSFSDESTQVENMLYPKLISLNSAHFDFQGCNFSEKNMYARDRRDGQSKEGSGRVA 502
Cdd:cd06236  152 ------FYIDLHAHASKRGCFIYGNALEDEEQQVENLLYPKLISLNSAHFDFDACNFSEKNMYSRDKRDGLSKEGSGRVA 225
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 118421091 503 IYKASGIIHSYTLECNYntgrsvnsipaachdngraspppppafpsrytveLFEQVGRAMAIAALDMAECNP 574
Cdd:cd06236  226 LYKATGIVHSYTLECNY----------------------------------HFEDVGRALAVALLDMLGCNP 263
M14_AGTPBP-like cd06235
Peptidase M14-like domain of human Nna1/AGTPBP-1, AGBL2 -5, and related proteins; Subgroup of ...
189-568 7.86e-121

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: 366.40  E-value: 7.86e-121
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118421091 189 IYYHRELLCYSLDGLRVDLLTITSCHGLREdreprleqlfpdtsTPRPFRFAGKRIFFLSSRVHPGETPSSFVFNGFLDF 268
Cdd:cd06235    1 IYFEREVLCHSLDGRKLDLLTITSPNNKKL--------------GPYPREFAGKKVVFLSGRVHPGETPASFVMKGFLDF 66
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118421091 269 ILRPDdPRAQTLRRLFVFKLIPMLNPDGVVRGHYRTDSRGVNLNRQYLKPDAVLHPAIYGAKAVLLYHHVHsrlnsqsss 348
Cdd:cd06235   67 LLSND-PRAQLLREHFVFKIVPMLNPDGVIRGNYRCSLNGFNLNRHYKNPDPELHPTIYGAKKVIDYLQKT--------- 136
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118421091 349 ehqpssclppdapvsdlekannlqneaqcghsadrhnaeawkqtepaeqklnsvwimpqqsagleesapdtippKESGVA 428
Cdd:cd06235  137 --------------------------------------------------------------------------YKRRVL 142
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118421091 429 YYVDLHGHASKRGCFMYGNSFSDESTQVENMLYPKLISLNSAHFDFQGCNfseknmyarDRRDGQSKEGSGRVAIYKASG 508
Cdd:cd06235  143 MYCDFHGHSSKSNGFMYGNSFPDTVQFHWNMVFPKILSLNAPDFFSSSCC---------SFGVMKSKEGTGRVVFGRRLI 213
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 118421091 509 IIHSYTLECNYNTGRSVNSIpAACHdngraspppppafpsrYTVELFEQVGRAMAIAALD 568
Cdd:cd06235  214 HSHSYTLESTFFSNNRGNID-GACG----------------YTEENLEDLGYSVASTLLD 256
M14_Nna1-like cd03856
Peptidase M14-like domain of ATP/GTP binding proteins, cytosolic carboxypeptidases and related ...
189-567 2.87e-95

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: 299.50  E-value: 2.87e-95
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118421091 189 IYYHRELLCYSLdgLRVDLLTITSCHGLREDREprleqlfpdTSTPRPFRFAGKRIFFLSSRVHPGETPSSFVFNGFLDF 268
Cdd:cd03856    1 HYARWLNLIATQ--PLVQLLEIGVTEQGREIQA---------LQSLRTERSDDKSWLFLIARQHPGETTGAWVFFGFLDQ 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118421091 269 ILRPDDPrAQTLRRLFVFKLIPMLNPDGVVRGHYRTDSRGVNLNRQYLKPDAVLHPAIYGAKAVLLYHHVHsrlnsqsss 348
Cdd:cd03856   70 LLSDDDP-AQQLRAEYNFYIIPMVNPDGVARGHWRTNSRGMDLNRDWHAPDALLSPETYAVAAALAERVQS--------- 139
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118421091 349 ehqpssclppdapvsdlekannlqneaqcghsadrhnaeawkqtepaeqklnsvwimpqqsagleesapdtippkESGVA 428
Cdd:cd03856  140 ---------------------------------------------------------------------------PEGVV 144
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118421091 429 YYVDLHGHAskRGCFMYGNSFSDESTqveNMLYPKLISLNSAHFDFQGcnfseknmyarDRRDGQSKE-----GSGRVAI 503
Cdd:cd03856  145 LALDLHGDN--RNVFLTGPDNKDEST---NHNPDKLNSLLTETDRRLP-----------DYNTEASPGdnpggTVGKQWI 208
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 118421091 504 YKASGIIHSYTLECNYNTGRSVNSipaachdngraspppppafpSRYTVELFEQVGRAMAIAAL 567
Cdd:cd03856  209 ADVYQITHSVTLEVGDNTDRSVAS--------------------SRYTPGEIELVAKTAATALL 252
M14_AGBL4_like cd06908
Peptidase M14-like domain of ATP/GTP binding protein AGBL-4 and related proteins; Peptidase ...
190-568 1.22e-49

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: 175.95  E-value: 1.22e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118421091 190 YYHRELLCYSLDGLRVDLLTITSchglrEDREPRLEQLFpdtstprpfrfagKRIFFLSSRVHPGETPSSFVFNGFLDFI 269
Cdd:cd06908    2 FFTRELLGKSVQQRRLDLLTITD-----PVNKHLTVEKK-------------KKVVFITARVHPGETPSSFVCQGLIDFL 63
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118421091 270 LRpDDPRAQTLRRLFVFKLIPMLNPDGVVRGHYRTDSRGVNLNRQYLKPDAVLHPAIYGAKAVLLyhhvhsRLNSQSSSE 349
Cdd:cd06908   64 VS-NHPVAKVLRDHLVFKIVPMLNPDGVFLGNYRCSLMGFDLNRHWHEPSPWAHPTLYAVKNLLR------ELDNDPTVQ 136
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118421091 350 hqpssclppdapvsdlekannlqneaqcghsadrhnaeawkqtepaeqklnsvwimpqqsagleesapdtippkesgVAY 429
Cdd:cd06908  137 -----------------------------------------------------------------------------LDF 139
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118421091 430 YVDLHGHASKRGCFMYGNSFSDESTQVENMLYPKLISLNSAHFDFQGCNFSeknmyaRDrrdgQSKEGSGRVAIykaSGI 509
Cdd:cd06908  140 YIDIHAHSTLMNGFMYGNIYDDVYRFERQAVFPKLLCQNAEDFSLSNTVFN------RD----PVKAGTGRRFL---GGL 206
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 118421091 510 I----HSYTLECN---YNTGRSVNSIPaachdngraspppppafpsrYTVELFEQVGRAMAIAALD 568
Cdd:cd06908  207 LddtaNCYTLEVSfysYRLSDSSSATP--------------------YTEEGYMKLGRNMARALLD 252
M14_AGBL2-3_like cd06907
Peptidase M14-like domain of ATP/GTP binding protein AGBL-2 and AGBL-3, and related proteins; ...
190-523 1.36e-48

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: 172.87  E-value: 1.36e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118421091 190 YYHRELLCYSLDGLRVDLLTITSCHGLREDREprleqlfpdtstprpfrfaGKRIFFLSSRVHPGETPSSFVFNGFLDFI 269
Cdd:cd06907    4 YCKRRVLCRTLAGNSVYVLTITSPSSNPEEAK-------------------AKKAVVLTARVHPGETNASWMMKGFLDFL 64
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118421091 270 LrPDDPRAQTLRRLFVFKLIPMLNPDGVVRGHYRTDSRGVNLNRQYLKPDAVLHPAIYGAKAVLlyhhvhsrlnsqssse 349
Cdd:cd06907   65 T-GSSPDAKLLRDNFVFKIVPMLNPDGVIVGNYRCSLAGRDLNRNYKTPLKESFPTIWHTKMMI---------------- 127
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118421091 350 hqpssclppdapvsdlekannlqneaqcghsadrhnaeawkqtepaeQKLNsvwimpqqsagleesapdtippKESGVAY 429
Cdd:cd06907  128 -----------------------------------------------KRLL----------------------EEREVIL 138
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118421091 430 YVDLHGHASKRGCFMYG-NSFSDESTQVENMLYPKLISLNSA-HFDFQGCNFSEKnmyardrrdgQSKEGSGRVAIYKaS 507
Cdd:cd06907  139 YCDLHGHSRKQNVFMYGcENRKNPEKPLKERVFPLMLSKNAPdKFSFESCKFKVQ----------KSKEGTGRVVMWR-E 207
                        330
                 ....*....|....*....
gi 118421091 508 GIIHSYTLE---CNYNTGR 523
Cdd:cd06907  208 GILNSYTLEatfCGSTLGR 226
M14_Nna1 cd06906
Peptidase M14-like domain of ATP/GTP binding proteins and cytosolic carboxypeptidases; ...
188-519 1.48e-46

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: 167.56  E-value: 1.48e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118421091 188 TIYYHRELLCYSLDGLRVDLLTITSchglredrEPRLEQLFPDTSTP-RPFrfagkriFFLSSRVHPGETPSSFVFNGFL 266
Cdd:cd06906    2 QIYYRQQTLCETLGGNSCPVLTITA--------MPESNNEEHICQFRnRPY-------IFLSARVHPGESNASWVMKGTL 66
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118421091 267 DFILRpDDPRAQTLRRLFVFKLIPMLNPDGVVRGHYRTDSRGVNLNRQYLKPDAVLHPAIYGAKAVLLYhhvhsrlnsqs 346
Cdd:cd06906   67 DFLLS-SSPAAQSLRESYIFKIVPMLNPDGVINGNHRCSLSGEDLNRRWLNPNPELHPTIYHTKGLLQY----------- 134
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118421091 347 ssehqpssclppdapvsdlekannlqneaqcghsadrhnaeawkqtepaeqkLNSVWIMPqqsagleesapdtippkesg 426
Cdd:cd06906  135 ----------------------------------------------------LRSIGRLP-------------------- 142
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118421091 427 vAYYVDLHGHASKRGCFMYGNSFSDESTQ----------VENMLY---PKLISLNSAHFDFQGCNFS-EKnmyardrrdg 492
Cdd:cd06906  143 -LVYCDYHGHSRKKNVFMYGCSPKESWSHgdtnnpsgdiVEDLGYrtlPKLLSHFAPAFSLSSCSFVvEK---------- 211
                        330       340
                 ....*....|....*....|....*..
gi 118421091 493 qSKEGSGRVAIYKASGIIHSYTLECNY 519
Cdd:cd06906  212 -SKESTARVVVWREIGVLRSYTMESTY 237
M14_PaCCP-like cd06234
Peptidase M14-like domain of ATP/GTP binding proteins and cytosolic carboxypeptidases similar ...
193-320 9.19e-23

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: 98.41  E-value: 9.19e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118421091 193 RELLCYSLDGLRVDLLTITSchglredreprleqlfPDTstprpfrfaGKRIFFLSSRVHPGETPSSFVFNGFLDFILRP 272
Cdd:cd06234   21 LEVLGQTLDGRDIDLLTIGD----------------PGT---------GKKKVWIIARQHPGETMAEWFMEGLLDRLLDE 75
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 118421091 273 DDPRAQTLRRLFVFKLIPMLNPDGVVRGHYRTDSRGVNLNRQYLKPDA 320
Cdd:cd06234   76 DDPVSRALLEKAVFYVVPNMNPDGSVRGNLRTNAAGVNLNREWANPSL 123
MpaA COG2866
Murein tripeptide amidase MpaA [Cell wall/membrane/envelope biogenesis];
159-320 1.25e-20

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


Pssm-ID: 442113 [Multi-domain]  Cd Length: 337  Bit Score: 94.37  E-value: 1.25e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118421091 159 FSYSDCQELLNQLDQRFPenhpthsspldtiYYHRELLCYSLDGLRVDLLTITSchglredreprleqlfpdtstprpfR 238
Cdd:COG2866   20 YTYEELLALLAKLAAASP-------------LVELESIGKSVEGRPIYLLKIGD-------------------------P 61
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118421091 239 FAGKRIFFLSSRVHPGETPSSFVFNGFLDFILRPDDPRAQTLRRLFVFKLIPMLNPDGVVRgHYRTDSRGVNLNRQYLKP 318
Cdd:COG2866   62 AEGKPKVLLNAQQHGNEWTGTEALLGLLEDLLDNYDPLIRALLDNVTLYIVPMLNPDGAER-NTRTNANGVDLNRDWPAP 140

                 ..
gi 118421091 319 DA 320
Cdd:COG2866  141 WL 142
M14_Nna1-like cd06237
Peptidase M14-like domain of ATP/GTP binding proteins and cytosolic carboxypeptidases; ...
241-313 2.77e-13

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: 70.29  E-value: 2.77e-13
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 118421091 241 GKRIFFLSSRVHPGETPSSFVFNGFLDFILRpDDPRAQTLRRLFVFKLIPMLNPDGVVRGHYRTDSRGVNLNR 313
Cdd:cd06237   40 SKELVVLLGRQHPPEVTGALAMQAFVETLLA-DTELAKAFRARFRVLVVPLLNPDGVDLGHWRHNAGGVDLNR 111
M14_Nna1-like cd18429
Peptidase M14-like domain of ATP/GTP binding proteins and cytosolic carboxypeptidases; ...
240-324 2.67e-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: 64.79  E-value: 2.67e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118421091 240 AGKRIFfLSSRVHPGETPSSFVFNGFLDFILRPDDPRAQTLRRlFVFKLIPMLNPDGVVRGHYRTDSRGVNLNRQYLKP- 318
Cdd:cd18429   39 APHRVF-LRARAHPWEAGGNWVVEGLVERLLQNDEEAKRFLKR-YCVYILPMANKDGVARGRTRFNANGKDLNREWDKPa 116

                 ....*.
gi 118421091 319 DAVLHP 324
Cdd:cd18429  117 DPVLAP 122
Zn_pept smart00631
Zn_pept domain;
160-315 7.04e-10

Zn_pept domain;


Pssm-ID: 214748 [Multi-domain]  Cd Length: 277  Bit Score: 60.81  E-value: 7.04e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118421091   160 SYSDCQELLNQLDQRFPEnhpthsspldtiYYHRELLCYSLDGLRVDLLTITSCHGlredreprleqlfpdtstprpfrf 239
Cdd:smart00631   3 SYEEIEAWLKELAARYPD------------LVRLVSIGKSVEGRPIWVLKISNGGS------------------------ 46
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118421091   240 AGKRIFFLSSRVHPGETPSSFVFNGFLDFILRP--DDPRAQTLRRLFVFKLIPMLNPDGVVRGH-----------YRTDS 306
Cdd:smart00631  47 HDKPAIFIDAGIHAREWIGPATALYLINQLLENygRDPRVTNLLDKTDIYIVPVLNPDGYEYTHtgdrlwrknrsPNSNC 126

                   ....*....
gi 118421091   307 RGVNLNRQY 315
Cdd:smart00631 127 RGVDLNRNF 135
Peptidase_M14 pfam00246
Zinc carboxypeptidase;
232-315 1.27e-09

Zinc carboxypeptidase;


Pssm-ID: 459730 [Multi-domain]  Cd Length: 287  Bit Score: 60.39  E-value: 1.27e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118421091  232 STPRPFRFAGKRIFFLSSRVHPGETPSSFVFNGFLDFILRP--DDPRAQTLRRLFVFKLIPMLNPDGVVRGHY------- 302
Cdd:pfam00246  36 SSGPGEHNPGKPAVFIDGGIHAREWIGPATALYLIHQLLTNygRDPEITELLDDTDIYILPVVNPDGYEYTHTtdrlwrk 115
                          90
                  ....*....|....*....
gi 118421091  303 -RTDSR-----GVNLNRQY 315
Cdd:pfam00246 116 nRSNANgssciGVDLNRNF 134
Pepdidase_M14_N pfam18027
Cytosolic carboxypeptidase N-terminal domain; This entry corresponds to the N-terminal domain ...
10-155 5.92e-06

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: 45.74  E-value: 5.92e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118421091   10 FSSRFDSGNLAHVEkveslssdgegvgggasaltsgiASSPDyEFNVWTRPDcAETEFengnRSWFYFSVRGGmPGKLIK 89
Cdd:pfam18027   1 ISSNFDSGNIEVVS-----------------------ASDPD-AIRLRIRPD-NGSEH----FQWFYFRVSGA-RGRPLT 50
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118421091   90 INIMNMNKQSklYSQGMAPFVRTLPT-RPRWERIrdrptfemtETQF---VLSFVHRFVegrGATTFFAF 155
Cdd:pfam18027  51 FVIENAGEAS--YPDGWTGYRVVASYdRENWFRV---------PTEYdggVLTITHTPE---ADTVYFAY 106
Peptidase_M14_like cd00596
M14 family of metallocarboxypeptidases and related proteins; The M14 family of ...
245-315 8.24e-06

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: 47.84  E-value: 8.24e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 118421091 245 FFLSSRVHPGETPSSFVFNGFLDFIL--RPDDPRAQTL--RRLFVfklIPMLNPDGVVRGHY---RTDSRGVNLNRQY 315
Cdd:cd00596    1 ILITGGIHGNEVIGVELALALIEYLLenYGNDPLKRLLdnVELWI---VPLVNPDGFARVIDsggRKNANGVDLNRNF 75
M14-CPA-like cd06227
Peptidase M14 carboxypeptidase A-like domain; uncharacterized subfamily; A functionally ...
276-315 1.39e-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: 1.39e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 118421091 276 RAQTLRRLFVFKLIPMLNPDG---VVRGHY--RTDSRGVNLNRQY 315
Cdd:cd06227   43 LAREILDNVELKIIPNANPDGrrlVESGDYcwRGNENGVDLNRNW 87
M14_CP_bacteria cd18173
bacterial peptidase M14 carboxypeptidase, uncharacterized; This family contains only bacterial ...
245-324 1.13e-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: 44.88  E-value: 1.13e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118421091 245 FFLSSRVHPGETPSSFVFNGFLDFILR--PDDPRAQTLRRLFVFKLIPMLNPDG-------VVRGHYRTDSRGVNLNRQY 315
Cdd:cd18173   57 FKYTSTMHGDETTGYELMLRLIDYLLTnyGTDPRITNLVDNTEIWINPLANPDGtyaggnnTVSGATRYNANGVDLNRNF 136

                 ....*....
gi 118421091 316 LKPDAVLHP 324
Cdd:cd18173  137 PDPVDGDHP 145
M14_MpaA-like cd06904
Peptidase M14-like domain of Escherichia coli Murein Peptide Amidase A and related proteins; ...
241-313 1.15e-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: 44.19  E-value: 1.15e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 118421091 241 GKRIFFLSSrVHPGETPSSFVFNGFLDFILRPDDPRAQTLRrlfvfkLIPMLNPDGVVRGHyRTDSRGVNLNR 313
Cdd:cd06904   23 RARILIIGG-IHGDEPEGVSLVEHLLRWLKNHPASGDFHIV------VVPCLNPDGLAAGT-RTNANGVDLNR 87
M14_REP34-like cd06231
Peptidase M14-like domain similar to rapid encystment phenotype 34 (REP34); This family ...
232-326 7.07e-04

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: 42.29  E-value: 7.07e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118421091 232 STPRPFRFAGKRIFfLSSRVHpGETPSSfVFnGFLDFIlrpDDPRAQTLRRlFVFKLIPMLNPDGVVRGHyRTDSRGVNL 311
Cdd:cd06231   33 LKSPNPRGDKPRVL-ISAGIH-GDEPAG-VE-ALLRFL---ESLAEKYLRR-VNLLVLPCVNPWGFERNT-RENADGIDL 103
                         90
                 ....*....|....*
gi 118421091 312 NRQYLKPDAVLHPAI 326
Cdd:cd06231  104 NRSFLKDSPSPEVRA 118
M14-like cd03857
Peptidase M14-like domain; uncharacterized subfamily; Peptidase M14-like domain of a ...
244-376 1.99e-03

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


Pssm-ID: 349430 [Multi-domain]  Cd Length: 203  Bit Score: 40.52  E-value: 1.99e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118421091 244 IFFLSSRVHPGETPSSfvfNGFLDFILR---PDDPRAQTLRRlFVFKLIPMLNPDGVVR------------GHYRTDSRG 308
Cdd:cd03857    1 TVLLAAQIHGNETTGT---EALMELIRDlasESDEAAKLLDN-IVILLVPQLNPDGAELfvnfyldsmnglPGTRYNANG 76
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 118421091 309 VNLNRQYLKPDavlHPAIYGAKAVLL--YHHVHSRLNSQSSS--EHQPSSCLPPDAPVSDLEKANNLQNEAQ 376
Cdd:cd03857   77 IDLNRDHVKLT---QPETQAVAENFIhwWPDIFIDLHEQVGAsiPYPTPPDAPNYNLVDLRSDAENGQEHIR 145
M14-like cd06239
Peptidase M14-like domain; uncharacterized subgroup; Peptidase M14-like domain of a ...
249-313 2.01e-03

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


Pssm-ID: 349458 [Multi-domain]  Cd Length: 194  Bit Score: 40.48  E-value: 2.01e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 118421091 249 SRVHpGETPSSFvfNGFLDFI--LRPDDPRAQTLRRLFVFKLIPMLNPDGVVRgHYRTDSRGVNLNR 313
Cdd:cd06239    6 SQMH-GNEPTGT--EALLDLIsyLRRERQEFEKILERLTLVAIPMLNPDGAEL-FTRHNAEGIDLNR 68
 
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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