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Conserved domains on  [gi|1958699642|ref|XP_038951379|]
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cytosolic carboxypeptidase 1 isoform X1 [Rattus norvegicus]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
M14_Nna1 cd06906
Peptidase M14-like domain of ATP/GTP binding proteins and cytosolic carboxypeptidases; ...
862-1132 0e+00

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: 613.23  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958699642  862 QQIYFRKDVLCETLSGNSCPLVTITAMPESSYYEHICQFRTRPYIFLSARVHPGETNASWVMKGTLEYLMSNSPTAQSLR 941
Cdd:cd06906      1 SQIYYRQQTLCETLGGNSCPVLTITAMPESNNEEHICQFRNRPYIFLSARVHPGESNASWVMKGTLDFLLSSSPAAQSLR 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958699642  942 EAYIFKIVPMLNPDGVINGNHRCSLSGEDLNRQWQSPNPELHPTIYHAKGLLQYLAAVKRLPLVYCDYHGHSRKKNVFMY 1021
Cdd:cd06906     81 ESYIFKIVPMLNPDGVINGNHRCSLSGEDLNRRWLNPNPELHPTIYHTKGLLQYLRSIGRLPLVYCDYHGHSRKKNVFMY 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958699642 1022 GCSIKETVWHTHDNAASCDVVEDMGYRTLPKILSHIAPAFCMSSCSFVVEKSKESTARVVVWREIGVQRSYTMESTLCGC 1101
Cdd:cd06906    161 GCSPKESWSHGDTNNPSGDIVEDLGYRTLPKLLSHFAPAFSLSSCSFVVEKSKESTARVVVWREIGVLRSYTMESTYCGC 240
                          250       260       270
                   ....*....|....*....|....*....|.
gi 1958699642 1102 DQGRYKGLQIGTRELEEMGAKFCVGLLRLKR 1132
Cdd:cd06906    241 DQGKYKGLHIGTRELEEMGARFCEALLRLKR 271
Pepdidase_M14_N super family cl39445
Cytosolic carboxypeptidase N-terminal domain; This entry corresponds to the N-terminal domain ...
705-839 1.70e-15

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: 73.47  E-value: 1.70e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958699642  705 FNSKFESGNLRKVIQIRKSEYDLILNSDINSNHyHQWFYFEVSGMRpGVAYRFNIINCekSNSQFNYGMQPLMYSVQEal 784
Cdd:pfam18027    1 ISSNFDSGNIEVVSASDPDAIRLRIRPDNGSEH-FQWFYFRVSGAR-GRPLTFVIENA--GEASYPDGWTGYRVVASY-- 74
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1958699642  785 nARPWWIRMGTDicyYKNHfsrssvaaggqkgksyytiTFTVVFPHKDDVCYFAY 839
Cdd:pfam18027   75 -DRENWFRVPTE---YDGG-------------------VLTITHTPEADTVYFAY 106
 
Name Accession Description Interval E-value
M14_Nna1 cd06906
Peptidase M14-like domain of ATP/GTP binding proteins and cytosolic carboxypeptidases; ...
862-1132 0e+00

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: 613.23  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958699642  862 QQIYFRKDVLCETLSGNSCPLVTITAMPESSYYEHICQFRTRPYIFLSARVHPGETNASWVMKGTLEYLMSNSPTAQSLR 941
Cdd:cd06906      1 SQIYYRQQTLCETLGGNSCPVLTITAMPESNNEEHICQFRNRPYIFLSARVHPGESNASWVMKGTLDFLLSSSPAAQSLR 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958699642  942 EAYIFKIVPMLNPDGVINGNHRCSLSGEDLNRQWQSPNPELHPTIYHAKGLLQYLAAVKRLPLVYCDYHGHSRKKNVFMY 1021
Cdd:cd06906     81 ESYIFKIVPMLNPDGVINGNHRCSLSGEDLNRRWLNPNPELHPTIYHTKGLLQYLRSIGRLPLVYCDYHGHSRKKNVFMY 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958699642 1022 GCSIKETVWHTHDNAASCDVVEDMGYRTLPKILSHIAPAFCMSSCSFVVEKSKESTARVVVWREIGVQRSYTMESTLCGC 1101
Cdd:cd06906    161 GCSPKESWSHGDTNNPSGDIVEDLGYRTLPKLLSHFAPAFSLSSCSFVVEKSKESTARVVVWREIGVLRSYTMESTYCGC 240
                          250       260       270
                   ....*....|....*....|....*....|.
gi 1958699642 1102 DQGRYKGLQIGTRELEEMGAKFCVGLLRLKR 1132
Cdd:cd06906    241 DQGKYKGLHIGTRELEEMGARFCEALLRLKR 271
MpaA COG2866
Murein tripeptide amidase MpaA [Cell wall/membrane/envelope biogenesis];
843-1011 2.61e-20

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


Pssm-ID: 442113 [Multi-domain]  Cd Length: 337  Bit Score: 93.99  E-value: 2.61e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958699642  843 YTYSTLQMHLQKLESAHNpqqiYFRKDVLCETLSGNSCPLVTITAMPESsyyehicqfrtRPYIFLSARVHPGETNASWV 922
Cdd:COG2866     20 YTYEELLALLAKLAAASP----LVELESIGKSVEGRPIYLLKIGDPAEG-----------KPKVLLNAQQHGNEWTGTEA 84
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958699642  923 MKGTLEYLMSN-SPTAQSLREAYIFKIVPMLNPDGVIN---GNHRcslsGEDLNRQWQSPN---PElhptiyhAKGLLQY 995
Cdd:COG2866     85 LLGLLEDLLDNyDPLIRALLDNVTLYIVPMLNPDGAERntrTNAN----GVDLNRDWPAPWlsePE-------TRALRDL 153
                          170
                   ....*....|....*.
gi 1958699642  996 LAAVKrlPLVYCDYHG 1011
Cdd:COG2866    154 LDEHD--PDFVLDLHG 167
Pepdidase_M14_N pfam18027
Cytosolic carboxypeptidase N-terminal domain; This entry corresponds to the N-terminal domain ...
705-839 1.70e-15

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: 73.47  E-value: 1.70e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958699642  705 FNSKFESGNLRKVIQIRKSEYDLILNSDINSNHyHQWFYFEVSGMRpGVAYRFNIINCekSNSQFNYGMQPLMYSVQEal 784
Cdd:pfam18027    1 ISSNFDSGNIEVVSASDPDAIRLRIRPDNGSEH-FQWFYFRVSGAR-GRPLTFVIENA--GEASYPDGWTGYRVVASY-- 74
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1958699642  785 nARPWWIRMGTDicyYKNHfsrssvaaggqkgksyytiTFTVVFPHKDDVCYFAY 839
Cdd:pfam18027   75 -DRENWFRVPTE---YDGG-------------------VLTITHTPEADTVYFAY 106
Zn_pept smart00631
Zn_pept domain;
843-1022 8.37e-15

Zn_pept domain;


Pssm-ID: 214748 [Multi-domain]  Cd Length: 277  Bit Score: 76.22  E-value: 8.37e-15
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958699642   843 YTYSTLQMHLQKLESAHnPQQIyfRKDVLCETLSGNSCPLVTITAMPEssyyehicqfRTRPYIFLSARVHPGETNASWV 922
Cdd:smart00631    2 HSYEEIEAWLKELAARY-PDLV--RLVSIGKSVEGRPIWVLKISNGGS----------HDKPAIFIDAGIHAREWIGPAT 68
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958699642   923 MKGTLEYLMSNS---PTAQSLREAYIFKIVPMLNPDG---VINGNH--RCSLS------GEDLNRQW-----QSPNPelH 983
Cdd:smart00631   69 ALYLINQLLENYgrdPRVTNLLDKTDIYIVPVLNPDGyeyTHTGDRlwRKNRSpnsncrGVDLNRNFpfhwgETGNP--C 146
                           170       180       190       200
                    ....*....|....*....|....*....|....*....|....*...
gi 1958699642   984 PTIYH---------AKGLLQYLAAVKRlPLVYCDYHGHSRkknVFMYG 1022
Cdd:smart00631  147 SETYAgpspfsepeTKAVRDFIRSNRR-FKLYIDLHSYSQ---LILYP 190
Peptidase_M14 pfam00246
Zinc carboxypeptidase;
852-1021 3.68e-07

Zinc carboxypeptidase;


Pssm-ID: 459730 [Multi-domain]  Cd Length: 287  Bit Score: 53.07  E-value: 3.68e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958699642  852 LQKLESAHnPQQIyfRKDVLCETLSGNSCPLVTITAMPESSYyehicqfRTRPYIFLSARVHPGETNASWVMKGTLEYLM 931
Cdd:pfam00246    5 LDALAARY-PDLV--RLVSIGKSVEGRPLKVLKISSGPGEHN-------PGKPAVFIDGGIHAREWIGPATALYLIHQLL 74
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958699642  932 SN---SPTAQSLREAYIFKIVPMLNPDGVING------------NHRCSL-SGEDLNRQWQS------------------ 977
Cdd:pfam00246   75 TNygrDPEITELLDDTDIYILPVVNPDGYEYThttdrlwrknrsNANGSScIGVDLNRNFPDhwnevgassnpcsetyrg 154
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....
gi 1958699642  978 PNPELHPtiyHAKGLLQYLAAVKRLpLVYCDYHGHSRkknVFMY 1021
Cdd:pfam00246  155 PAPFSEP---ETRAVADFIRSKKPF-VLYISLHSYSQ---VLLY 191
 
Name Accession Description Interval E-value
M14_Nna1 cd06906
Peptidase M14-like domain of ATP/GTP binding proteins and cytosolic carboxypeptidases; ...
862-1132 0e+00

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: 613.23  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958699642  862 QQIYFRKDVLCETLSGNSCPLVTITAMPESSYYEHICQFRTRPYIFLSARVHPGETNASWVMKGTLEYLMSNSPTAQSLR 941
Cdd:cd06906      1 SQIYYRQQTLCETLGGNSCPVLTITAMPESNNEEHICQFRNRPYIFLSARVHPGESNASWVMKGTLDFLLSSSPAAQSLR 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958699642  942 EAYIFKIVPMLNPDGVINGNHRCSLSGEDLNRQWQSPNPELHPTIYHAKGLLQYLAAVKRLPLVYCDYHGHSRKKNVFMY 1021
Cdd:cd06906     81 ESYIFKIVPMLNPDGVINGNHRCSLSGEDLNRRWLNPNPELHPTIYHTKGLLQYLRSIGRLPLVYCDYHGHSRKKNVFMY 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958699642 1022 GCSIKETVWHTHDNAASCDVVEDMGYRTLPKILSHIAPAFCMSSCSFVVEKSKESTARVVVWREIGVQRSYTMESTLCGC 1101
Cdd:cd06906    161 GCSPKESWSHGDTNNPSGDIVEDLGYRTLPKLLSHFAPAFSLSSCSFVVEKSKESTARVVVWREIGVLRSYTMESTYCGC 240
                          250       260       270
                   ....*....|....*....|....*....|.
gi 1958699642 1102 DQGRYKGLQIGTRELEEMGAKFCVGLLRLKR 1132
Cdd:cd06906    241 DQGKYKGLHIGTRELEEMGARFCEALLRLKR 271
M14_AGTPBP-like cd06235
Peptidase M14-like domain of human Nna1/AGTPBP-1, AGBL2 -5, and related proteins; Subgroup of ...
864-1129 1.73e-139

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: 423.02  E-value: 1.73e-139
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958699642  864 IYFRKDVLCETLSGNSCPLVTITAMPESSYYEHICQFRTRPYIFLSARVHPGETNASWVMKGTLEYLMSNSPTAQSLREA 943
Cdd:cd06235      1 IYFEREVLCHSLDGRKLDLLTITSPNNKKLGPYPREFAGKKVVFLSGRVHPGETPASFVMKGFLDFLLSNDPRAQLLREH 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958699642  944 YIFKIVPMLNPDGVINGNHRCSLSGEDLNRQWQSPNPELHPTIYHAKGLLQYLAAV-KRLPLVYCDYHGHSRKKNVFMYG 1022
Cdd:cd06235     81 FVFKIVPMLNPDGVIRGNYRCSLNGFNLNRHYKNPDPELHPTIYGAKKVIDYLQKTyKRRVLMYCDFHGHSSKSNGFMYG 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958699642 1023 CSIKETVWHthdnaascdvvedMGYRTLPKILSHIAPAFCMSS-CSFVVEKSKESTARVVVWREIGVQRSYTMESTLCGC 1101
Cdd:cd06235    161 NSFPDTVQF-------------HWNMVFPKILSLNAPDFFSSScCSFGVMKSKEGTGRVVFGRRLIHSHSYTLESTFFSN 227
                          250       260
                   ....*....|....*....|....*....
gi 1958699642 1102 DQGRY-KGLQIGTRELEEMGAKFCVGLLR 1129
Cdd:cd06235    228 NRGNIdGACGYTEENLEDLGYSVASTLLD 256
M14_AGBL2-3_like cd06907
Peptidase M14-like domain of ATP/GTP binding protein AGBL-2 and AGBL-3, and related proteins; ...
865-1128 1.10e-109

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: 343.90  E-value: 1.10e-109
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958699642  865 YFRKDVLCETLSGNSCPLVTITAMpeSSYYEHIcqfRTRPYIFLSARVHPGETNASWVMKGTLEYLMSNSPTAQSLREAY 944
Cdd:cd06907      4 YCKRRVLCRTLAGNSVYVLTITSP--SSNPEEA---KAKKAVVLTARVHPGETNASWMMKGFLDFLTGSSPDAKLLRDNF 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958699642  945 IFKIVPMLNPDGVINGNHRCSLSGEDLNRQWQSPNPELHPTIYHAKGLLQYLAAvKRLPLVYCDYHGHSRKKNVFMYGCs 1024
Cdd:cd06907     79 VFKIVPMLNPDGVIVGNYRCSLAGRDLNRNYKTPLKESFPTIWHTKMMIKRLLE-EREVILYCDLHGHSRKQNVFMYGC- 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958699642 1025 iketvwhTHDNAASCDVVEdmgyRTLPKILSHIAPA-FCMSSCSFVVEKSKESTARVVVWREiGVQRSYTMESTLCGCDQ 1103
Cdd:cd06907    157 -------ENRKNPEKPLKE----RVFPLMLSKNAPDkFSFESCKFKVQKSKEGTGRVVMWRE-GILNSYTLEATFCGSTL 224
                          250       260
                   ....*....|....*....|....*
gi 1958699642 1104 GRYKGLQIGTRELEEMGAKFCVGLL 1128
Cdd:cd06907    225 GRRKGTHFNTLDFEAMGYHFCDTLL 249
M14_AGBL4_like cd06908
Peptidase M14-like domain of ATP/GTP binding protein AGBL-4 and related proteins; Peptidase ...
865-1095 9.78e-62

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


Pssm-ID: 349479  Cd Length: 254  Bit Score: 211.39  E-value: 9.78e-62
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958699642  865 YFRKDVLCETLSGNSCPLVTITAmPESSYYEHICQFRTrpyIFLSARVHPGETNASWVMKGTLEYLMSNSPTAQSLREAY 944
Cdd:cd06908      2 FFTRELLGKSVQQRRLDLLTITD-PVNKHLTVEKKKKV---VFITARVHPGETPSSFVCQGLIDFLVSNHPVAKVLRDHL 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958699642  945 IFKIVPMLNPDGVINGNHRCSLSGEDLNRQWQSPNPELHPTIYHAKGLLQYLAAVKRLPLV-YCDYHGHSRKKNVFMYGc 1023
Cdd:cd06908     78 VFKIVPMLNPDGVFLGNYRCSLMGFDLNRHWHEPSPWAHPTLYAVKNLLRELDNDPTVQLDfYIDIHAHSTLMNGFMYG- 156
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958699642 1024 siketvwhthdnaascDVVEDMgYRT-----LPKILSHIAPAFCMSSCSFVVEKSKESTARVVVwREIGVQRS--YTME 1095
Cdd:cd06908    157 ----------------NIYDDV-YRFerqavFPKLLCQNAEDFSLSNTVFNRDPVKAGTGRRFL-GGLLDDTAncYTLE 217
M14_AGBL5_like cd06236
Peptidase M14-like domain of ATP/GTP binding protein (AGBL)-5 and related proteins; Peptidase ...
861-1095 3.15e-56

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: 195.94  E-value: 3.15e-56
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958699642  861 PQQIYFRKDVLCETLSGNSCPLVTITAM---------------PESSyyEHIC-QFRTRPYIFLSARVHPGETNASWVMK 924
Cdd:cd06236      4 ESDIYYHRELLCYSLEGRRVDLLTITSChgvteereerlpnlfPDTS--KPRPhKFEGKKVVFISARVHPGETPSSFVFN 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958699642  925 GTLEYLMS-NSPTAQSLREAYIFKIVPMLNPDGVINGNHRCSLSGEDLNRQWQSPNPELHPTIYHAKGLLQYLaavkrlp 1003
Cdd:cd06236     82 GFLEFLLRpDDPRAIALRRLFVFKLIPMLNPDGVARGHYRTDTRGVNLNRVYLNPDPELHPSIYAAKALLFYI------- 154
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958699642 1004 lvycDYHGHSRKKNVFMYGCSIKETVWHthdnaascdvVEDMGYrtlPKILSHIAPAFCMSSCSFvVEK----------- 1072
Cdd:cd06236    155 ----DLHAHASKRGCFIYGNALEDEEQQ----------VENLLY---PKLISLNSAHFDFDACNF-SEKnmysrdkrdgl 216
                          250       260
                   ....*....|....*....|...
gi 1958699642 1073 SKESTARVVVWREIGVQRSYTME 1095
Cdd:cd06236    217 SKEGSGRVALYKATGIVHSYTLE 239
M14_Nna1-like cd03856
Peptidase M14-like domain of ATP/GTP binding proteins, cytosolic carboxypeptidases and related ...
899-1038 2.61e-36

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: 138.10  E-value: 2.61e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958699642  899 QFRTRPYIFLSARVHPGETNASWVMKGTLEYLMSNSPTAQSLREAYIFKIVPMLNPDGVINGNHRCSLSGEDLNRQWQSP 978
Cdd:cd03856     39 RSDDKSWLFLIARQHPGETTGAWVFFGFLDQLLSDDDPAQQLRAEYNFYIIPMVNPDGVARGHWRTNSRGMDLNRDWHAP 118
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958699642  979 NPELHPTIYHAKGLLQYLAAVKRLPLVYCDYHGHSRkkNVFMYGCS-IKETVWHTHDNAAS 1038
Cdd:cd03856    119 DALLSPETYAVAAALAERVQSPEGVVLALDLHGDNR--NVFLTGPDnKDESTNHNPDKLNS 177
M14_PaCCP-like cd06234
Peptidase M14-like domain of ATP/GTP binding proteins and cytosolic carboxypeptidases similar ...
847-1023 1.98e-27

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: 112.66  E-value: 1.98e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958699642  847 TLQMHLQKLESAhnPQQIYFRKDVLCETLSGNSCPLVTITAMPESsyyehicqfrtRPYIFLSARVHPGETNASWVMKGT 926
Cdd:cd06234      2 SYERHLDLVARA--QASPGVRLEVLGQTLDGRDIDLLTIGDPGTG-----------KKKVWIIARQHPGETMAEWFMEGL 68
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958699642  927 LEYLMSNS-PTAQSLREAYIFKIVPMLNPDGVINGNHRCSLSGEDLNRQWQSPNPELHPTIYHAKgllqylAAVKRLPL- 1004
Cdd:cd06234     69 LDRLLDEDdPVSRALLEKAVFYVVPNMNPDGSVRGNLRTNAAGVNLNREWANPSLERSPEVFAVR------QAMDATGVd 142
                          170
                   ....*....|....*....
gi 1958699642 1005 VYCDYHGHSRKKNVFMYGC 1023
Cdd:cd06234    143 FFLDVHGDEALPYNFIAGA 161
MpaA COG2866
Murein tripeptide amidase MpaA [Cell wall/membrane/envelope biogenesis];
843-1011 2.61e-20

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


Pssm-ID: 442113 [Multi-domain]  Cd Length: 337  Bit Score: 93.99  E-value: 2.61e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958699642  843 YTYSTLQMHLQKLESAHNpqqiYFRKDVLCETLSGNSCPLVTITAMPESsyyehicqfrtRPYIFLSARVHPGETNASWV 922
Cdd:COG2866     20 YTYEELLALLAKLAAASP----LVELESIGKSVEGRPIYLLKIGDPAEG-----------KPKVLLNAQQHGNEWTGTEA 84
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958699642  923 MKGTLEYLMSN-SPTAQSLREAYIFKIVPMLNPDGVIN---GNHRcslsGEDLNRQWQSPN---PElhptiyhAKGLLQY 995
Cdd:COG2866     85 LLGLLEDLLDNyDPLIRALLDNVTLYIVPMLNPDGAERntrTNAN----GVDLNRDWPAPWlsePE-------TRALRDL 153
                          170
                   ....*....|....*.
gi 1958699642  996 LAAVKrlPLVYCDYHG 1011
Cdd:COG2866    154 LDEHD--PDFVLDLHG 167
M14_Nna1-like cd18429
Peptidase M14-like domain of ATP/GTP binding proteins and cytosolic carboxypeptidases; ...
904-1010 2.36e-17

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: 83.28  E-value: 2.36e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958699642  904 PY-IFLSARVHPGETNASWVMKGTLEYLMSNSPTAQSLREAYIFKIVPMLNPDGVINGNHRCSLSGEDLNRQWQSP-NPE 981
Cdd:cd18429     40 PHrVFLRARAHPWEAGGNWVVEGLVERLLQNDEEAKRFLKRYCVYILPMANKDGVARGRTRFNANGKDLNREWDKPaDPV 119
                           90       100
                   ....*....|....*....|....*....
gi 1958699642  982 LHPTIYHAKGLLQYLAAVKRLPLVYCDYH 1010
Cdd:cd18429    120 LAPENFALEKWLEEMIKAGKKPDLAIELH 148
M14_Nna1-like cd06237
Peptidase M14-like domain of ATP/GTP binding proteins and cytosolic carboxypeptidases; ...
903-1019 6.51e-16

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: 78.76  E-value: 6.51e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958699642  903 RPYIFLSARVHPGETNASWVMKGTLEYLMSNSPTAQSLREAYIFKIVPMLNPDGVINGNHRCSLSGEDLNRQWQSPN-PE 981
Cdd:cd06237     41 KELVVLLGRQHPPEVTGALAMQAFVETLLADTELAKAFRARFRVLVVPLLNPDGVDLGHWRHNAGGVDLNRDWGPFTqPE 120
                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 1958699642  982 lhpTIYHAKGLLQYLAAVKRlPLVYC-DYhgHSRKKNVF 1019
Cdd:cd06237    121 ---TRAVRDFLLELVEEPGG-KVVFGlDF--HSTWEDVF 153
Pepdidase_M14_N pfam18027
Cytosolic carboxypeptidase N-terminal domain; This entry corresponds to the N-terminal domain ...
705-839 1.70e-15

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: 73.47  E-value: 1.70e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958699642  705 FNSKFESGNLRKVIQIRKSEYDLILNSDINSNHyHQWFYFEVSGMRpGVAYRFNIINCekSNSQFNYGMQPLMYSVQEal 784
Cdd:pfam18027    1 ISSNFDSGNIEVVSASDPDAIRLRIRPDNGSEH-FQWFYFRVSGAR-GRPLTFVIENA--GEASYPDGWTGYRVVASY-- 74
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1958699642  785 nARPWWIRMGTDicyYKNHfsrssvaaggqkgksyytiTFTVVFPHKDDVCYFAY 839
Cdd:pfam18027   75 -DRENWFRVPTE---YDGG-------------------VLTITHTPEADTVYFAY 106
Zn_pept smart00631
Zn_pept domain;
843-1022 8.37e-15

Zn_pept domain;


Pssm-ID: 214748 [Multi-domain]  Cd Length: 277  Bit Score: 76.22  E-value: 8.37e-15
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958699642   843 YTYSTLQMHLQKLESAHnPQQIyfRKDVLCETLSGNSCPLVTITAMPEssyyehicqfRTRPYIFLSARVHPGETNASWV 922
Cdd:smart00631    2 HSYEEIEAWLKELAARY-PDLV--RLVSIGKSVEGRPIWVLKISNGGS----------HDKPAIFIDAGIHAREWIGPAT 68
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958699642   923 MKGTLEYLMSNS---PTAQSLREAYIFKIVPMLNPDG---VINGNH--RCSLS------GEDLNRQW-----QSPNPelH 983
Cdd:smart00631   69 ALYLINQLLENYgrdPRVTNLLDKTDIYIVPVLNPDGyeyTHTGDRlwRKNRSpnsncrGVDLNRNFpfhwgETGNP--C 146
                           170       180       190       200
                    ....*....|....*....|....*....|....*....|....*...
gi 1958699642   984 PTIYH---------AKGLLQYLAAVKRlPLVYCDYHGHSRkknVFMYG 1022
Cdd:smart00631  147 SETYAgpspfsepeTKAVRDFIRSNRR-FKLYIDLHSYSQ---LILYP 190
Peptidase_M14_like cd00596
M14 family of metallocarboxypeptidases and related proteins; The M14 family of ...
906-981 8.89e-08

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: 54.00  E-value: 8.89e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958699642  906 IFLSARVHPGETNASWVMKGTLEYLMSN---SPTAQSLREAYIFkIVPMLNPDGVINGNHRCS---LSGEDLNRQWQSPN 979
Cdd:cd00596      1 ILITGGIHGNEVIGVELALALIEYLLENygnDPLKRLLDNVELW-IVPLVNPDGFARVIDSGGrknANGVDLNRNFPYNW 79

                   ..
gi 1958699642  980 PE 981
Cdd:cd00596     80 GK 81
Peptidase_M14 pfam00246
Zinc carboxypeptidase;
852-1021 3.68e-07

Zinc carboxypeptidase;


Pssm-ID: 459730 [Multi-domain]  Cd Length: 287  Bit Score: 53.07  E-value: 3.68e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958699642  852 LQKLESAHnPQQIyfRKDVLCETLSGNSCPLVTITAMPESSYyehicqfRTRPYIFLSARVHPGETNASWVMKGTLEYLM 931
Cdd:pfam00246    5 LDALAARY-PDLV--RLVSIGKSVEGRPLKVLKISSGPGEHN-------PGKPAVFIDGGIHAREWIGPATALYLIHQLL 74
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958699642  932 SN---SPTAQSLREAYIFKIVPMLNPDGVING------------NHRCSL-SGEDLNRQWQS------------------ 977
Cdd:pfam00246   75 TNygrDPEITELLDDTDIYILPVVNPDGYEYThttdrlwrknrsNANGSScIGVDLNRNFPDhwnevgassnpcsetyrg 154
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....
gi 1958699642  978 PNPELHPtiyHAKGLLQYLAAVKRLpLVYCDYHGHSRkknVFMY 1021
Cdd:pfam00246  155 PAPFSEP---ETRAVADFIRSKKPF-VLYISLHSYSQ---VLLY 191
M14-like cd06905
Peptidase M14-like domain; uncharacterized subfamily; A functionally uncharacterized subgroup ...
840-956 6.83e-05

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


Pssm-ID: 349476 [Multi-domain]  Cd Length: 359  Bit Score: 46.46  E-value: 6.83e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958699642  840 HYpYTYSTLQMHLQKLESAHnPQqiYFRKDVLCETLSGNSCPLVTITAMPESSYYEhicqfrtRPYIFLSARVHPGETNA 919
Cdd:cd06905      5 RY-YTYAELTARLKALAEAY-PN--LVRLESIGKSYEGRDIWLLTITNGETGPADE-------KPALWVDGNIHGNEVTG 73
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|
gi 1958699642  920 SWVMKGTLEYLMSN---SPTAQSLREAYIFKIVPMLNPDG 956
Cdd:cd06905     74 SEVALYLAEYLLTNygkDPEITRLLDTRTFYILPRLNPDG 113
M14_REP34-like cd06231
Peptidase M14-like domain similar to rapid encystment phenotype 34 (REP34); This family ...
903-1001 8.57e-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: 45.38  E-value: 8.57e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958699642  903 RPYIFLSARVHPGETNASWvmkGTLEYLMSNsptAQSLREAYIFKIVPMLNPDGVINgNHRCSLSGEDLNRQWQ--SPNP 980
Cdd:cd06231     42 KPRVLISAGIHGDEPAGVE---ALLRFLESL---AEKYLRRVNLLVLPCVNPWGFER-NTRENADGIDLNRSFLkdSPSP 114
                           90       100
                   ....*....|....*....|.
gi 1958699642  981 ElhptiyhAKGLLQYLAAVKR 1001
Cdd:cd06231    115 E-------VRALMEFLASLGR 128
M14-CPA-like cd06227
Peptidase M14 carboxypeptidase A-like domain; uncharacterized subfamily; A functionally ...
937-978 3.50e-04

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: 43.41  E-value: 3.50e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 1958699642  937 AQSLREAYIFKIVPMLNPDG---VINGNH--RCSLSGEDLNRQWQSP 978
Cdd:cd06227     44 AREILDNVELKIIPNANPDGrrlVESGDYcwRGNENGVDLNRNWGVD 90
M14_CP_A-B_like cd03860
Peptidase M14 carboxypeptidase subfamily A/B-like; The Peptidase M14 Carboxypeptidase (CP) A/B ...
901-1010 4.71e-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: 43.67  E-value: 4.71e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958699642  901 RTRPYIFLSARVHPGEtnasWVMKGTLEYLMS-------NSPTAQSLREAYIFKIVPMLNPDGVI--------------- 958
Cdd:cd03860     48 GGKPAIVIHGGQHARE----WISTSTVEYLAHqllsgygSDATITALLDKFDFYIIPVVNPDGYVytwttdrlwrknrqp 123
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958699642  959 NGNHRCslSGEDLNR----QWQSPNPELHPT--IYH---------AKGLLQYLAAVKRLP--LVYCDYH 1010
Cdd:cd03860    124 TGGSSC--VGIDLNRnwgyKWGGPGASTNPCseTYRgpsafsapeTKALADFINALAAGQgiKGFIDLH 190
M14-like cd06239
Peptidase M14-like domain; uncharacterized subgroup; Peptidase M14-like domain of a ...
906-973 2.00e-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: 40.86  E-value: 2.00e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958699642  906 IFLSARVHPGETNASWVMKGTLEYLMSNSPTAQSLREAYIFKIVPMLNPDGvINGNHRCSLSGEDLNR 973
Cdd:cd06239      2 VLLWSQMHGNEPTGTEALLDLISYLRRERQEFEKILERLTLVAIPMLNPDG-AELFTRHNAEGIDLNR 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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