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Conserved domains on  [gi|22218871|pdb|1JQG|A]
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Chain A, carboxypeptidase A

Protein Classification

M14 family carboxypeptidase B( domain architecture ID 10491436)

M14 family carboxypeptidase B found specifically in insects includes B-type carboxypeptidase of Helicoverpa zea (CPBHz, insect gut carboxypeptidase-3) and midgut procarboxypeptidase A (PCPAHa, insect gut carboxypeptidase-1) from Helicoverpa armigera larva; PCPAHa preferentially cleaves aliphatic and aromatic residues

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
M14_CP_insect cd06248
Peptidase M14 carboxypeptidase subfamily A/B-like; This family includes peptidase M14 ...
121-416 2.27e-158

Peptidase M14 carboxypeptidase subfamily A/B-like; This family includes peptidase M14 carboxypeptidases found specifically in insects, including B-type carboxypeptidase of H. zea (CPBHz, insect gut carboxypeptidase-3) that is insensitive to potato carboxypeptidase inhibitor (PCI) in corn earworm, and midgut procarboxypeptidase A (PCPAHa, insect gut carboxypeptidase-1) from Helicoverpa armigera larva, a devastating pest of crops. PCPAHa preferentially cleaves aliphatic and aromatic residues. The peptidase M14 Carboxypeptidase (CP) A/B subfamily is one of two main M14 CP subfamilies defined by sequence and structural homology, the other being the N/E subfamily. CPs hydrolyze single, C-terminal amino acids from polypeptide chains. They have a recognition site for the free C-terminal carboxyl group, which is a key determinant of specificity. Enzymes belonging to the A/B subfamily are normally synthesized as inactive precursors containing preceding signal peptide, followed by a globular N-terminal pro-region linked to the enzyme; these proenzymes are called procarboxypeptidases. The A/B enzymes can be further divided based on their substrate specificity; Carboxypeptidase A-like (CPA-like) enzymes favor hydrophobic residues while carboxypeptidase B-like (CPB-like) enzymes only cleave the basic residues lysine or arginine. There are nine members in the A/B family: CPA1, CPA2, CPA3, CPA4, CPA5, CPA6, CPB, CPO and CPU. CPA1, CPA2 and CPB are produced by the pancreas. The A forms have slightly different specificities, with CPA1 preferring aliphatic and small aromatic residues, and CPA2 preferring the bulkier aromatic side chains. CPA3 is found in secretory granules of mast cells and functions in inflammatory processes. CPA4 is detected in hormone-regulated tissues, and is thought to play a role in prostate cancer. CPA5 is present in discrete regions of pituitary and other tissues, and cleaves aliphatic C-terminal residues. CPA6 is highly expressed in embryonic brain and optic muscle, suggesting that it may play a specific role in cell migration and axonal guidance. CPU (also called CPB2) is produced and secreted by the liver as the inactive precursor, PCPU, commonly referred to as thrombin-activatable fibrinolysis inhibitor (TAFI). Little is known about CPO but it has been suggested to have specificity for acidic residues.


:

Pssm-ID: 349467 [Multi-domain]  Cd Length: 297  Bit Score: 448.83  E-value: 2.27e-158
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1JQG_A      121 IHSYEEVDAYLQELAKEFPNVVTVVEGGKSFEGRSIKYLRISTTNFQDASKPVVMMQSLLHCREWVTLPATLYAIHKLVI 200
Cdd:cd06248   1 YHSLDEIDEYLDGLAEESPDVVTVVEGGYTFEGRPIKYVRIRSTNSEDTSKPTIMIEGGINPREWISPPAALYAIHKLVE 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1JQG_A      201 DV-TESDLINNIDWIILPVANPDGYVHTFGGDRYWRKNRATGYMA-GNLCMGVDLNRNFGMNWG-TASSSSVCSDTFHGR 277
Cdd:cd06248  81 DVeTQSDLLNNFDWIILPVANPDGYVFTHTNDREWTKNRSTNSNPlGQICFGVNINRNFDYQWNpVLSSESPCSELYAGP 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1JQG_A      278 SAFSEPESSVIRDIIAEHRNRMALYLDIHSFGSMILYGYGN-GVLPSNALQLHLIGVQMAQAIDRvkwSSNKDYIVGNIF 356
Cdd:cd06248 161 SAFSEAESRAIRDILHEHGNRIHLYISFHSGGSFILYPWGYdGSTSSNARQLHLAGVAAAAAISS---NNGRPYVVGQSS 237
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|
1JQG_A      357 HVLYAASGGASDYAMQaAAPFSYTYELPAYRNsvwFDGFLVDPDFIEQAGFETWEGIKVG 416
Cdd:cd06248 238 VLLYRAAGTSSDYAMG-IAGIDYTYELPGYSS---GDPFYVPPAYIEQVVREAWEGIVVG 293
Propep_M14 pfam02244
Carboxypeptidase activation peptide; Carboxypeptidases are found in abundance in pancreatic ...
27-98 5.81e-11

Carboxypeptidase activation peptide; Carboxypeptidases are found in abundance in pancreatic secretions. The pro-segment moiety (activation peptide) accounts for up to a quarter of the total length of the peptidase, and is responsible for modulation of folding and activity of the pro-enzyme.


:

Pssm-ID: 460505  Cd Length: 73  Bit Score: 57.99  E-value: 5.81e-11
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
1JQG_A         27 YQVDVASMDQVKLVHDFENDLMLDVWSDAV-PGRPGKVLVPKFKREIFENFLKQSGVQYKLEVENVKEQLELE 98
Cdd:pfam02244   1 YRVTPETEEQLQLLKELEESYDLDFWKPPSkVGKPVDVMVPPSKLEAFEELLEKHGISYEVLIEDVQELIDEE 73
 
Name Accession Description Interval E-value
M14_CP_insect cd06248
Peptidase M14 carboxypeptidase subfamily A/B-like; This family includes peptidase M14 ...
121-416 2.27e-158

Peptidase M14 carboxypeptidase subfamily A/B-like; This family includes peptidase M14 carboxypeptidases found specifically in insects, including B-type carboxypeptidase of H. zea (CPBHz, insect gut carboxypeptidase-3) that is insensitive to potato carboxypeptidase inhibitor (PCI) in corn earworm, and midgut procarboxypeptidase A (PCPAHa, insect gut carboxypeptidase-1) from Helicoverpa armigera larva, a devastating pest of crops. PCPAHa preferentially cleaves aliphatic and aromatic residues. The peptidase M14 Carboxypeptidase (CP) A/B subfamily is one of two main M14 CP subfamilies defined by sequence and structural homology, the other being the N/E subfamily. CPs hydrolyze single, C-terminal amino acids from polypeptide chains. They have a recognition site for the free C-terminal carboxyl group, which is a key determinant of specificity. Enzymes belonging to the A/B subfamily are normally synthesized as inactive precursors containing preceding signal peptide, followed by a globular N-terminal pro-region linked to the enzyme; these proenzymes are called procarboxypeptidases. The A/B enzymes can be further divided based on their substrate specificity; Carboxypeptidase A-like (CPA-like) enzymes favor hydrophobic residues while carboxypeptidase B-like (CPB-like) enzymes only cleave the basic residues lysine or arginine. There are nine members in the A/B family: CPA1, CPA2, CPA3, CPA4, CPA5, CPA6, CPB, CPO and CPU. CPA1, CPA2 and CPB are produced by the pancreas. The A forms have slightly different specificities, with CPA1 preferring aliphatic and small aromatic residues, and CPA2 preferring the bulkier aromatic side chains. CPA3 is found in secretory granules of mast cells and functions in inflammatory processes. CPA4 is detected in hormone-regulated tissues, and is thought to play a role in prostate cancer. CPA5 is present in discrete regions of pituitary and other tissues, and cleaves aliphatic C-terminal residues. CPA6 is highly expressed in embryonic brain and optic muscle, suggesting that it may play a specific role in cell migration and axonal guidance. CPU (also called CPB2) is produced and secreted by the liver as the inactive precursor, PCPU, commonly referred to as thrombin-activatable fibrinolysis inhibitor (TAFI). Little is known about CPO but it has been suggested to have specificity for acidic residues.


Pssm-ID: 349467 [Multi-domain]  Cd Length: 297  Bit Score: 448.83  E-value: 2.27e-158
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1JQG_A      121 IHSYEEVDAYLQELAKEFPNVVTVVEGGKSFEGRSIKYLRISTTNFQDASKPVVMMQSLLHCREWVTLPATLYAIHKLVI 200
Cdd:cd06248   1 YHSLDEIDEYLDGLAEESPDVVTVVEGGYTFEGRPIKYVRIRSTNSEDTSKPTIMIEGGINPREWISPPAALYAIHKLVE 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1JQG_A      201 DV-TESDLINNIDWIILPVANPDGYVHTFGGDRYWRKNRATGYMA-GNLCMGVDLNRNFGMNWG-TASSSSVCSDTFHGR 277
Cdd:cd06248  81 DVeTQSDLLNNFDWIILPVANPDGYVFTHTNDREWTKNRSTNSNPlGQICFGVNINRNFDYQWNpVLSSESPCSELYAGP 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1JQG_A      278 SAFSEPESSVIRDIIAEHRNRMALYLDIHSFGSMILYGYGN-GVLPSNALQLHLIGVQMAQAIDRvkwSSNKDYIVGNIF 356
Cdd:cd06248 161 SAFSEAESRAIRDILHEHGNRIHLYISFHSGGSFILYPWGYdGSTSSNARQLHLAGVAAAAAISS---NNGRPYVVGQSS 237
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|
1JQG_A      357 HVLYAASGGASDYAMQaAAPFSYTYELPAYRNsvwFDGFLVDPDFIEQAGFETWEGIKVG 416
Cdd:cd06248 238 VLLYRAAGTSSDYAMG-IAGIDYTYELPGYSS---GDPFYVPPAYIEQVVREAWEGIVVG 293
Zn_pept smart00631
Zn_pept domain;
122-406 9.55e-104

Zn_pept domain;


Pssm-ID: 214748 [Multi-domain]  Cd Length: 277  Bit Score: 309.27  E-value: 9.55e-104
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1JQG_A         122 HSYEEVDAYLQELAKEFPNVVTVVEGGKSFEGRSIKYLRISTTNfqDASKPVVMMQSLLHCREWVTLPATLYAIHKLVI- 200
Cdd:smart00631   2 HSYEEIEAWLKELAARYPDLVRLVSIGKSVEGRPIWVLKISNGG--SHDKPAIFIDAGIHAREWIGPATALYLINQLLEn 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1JQG_A         201 ---DVTESDLINNIDWIILPVANPDGYVHTFGGDRYWRKNRATGYmagnLCMGVDLNRNFGMNWGTasSSSVCSDTFHGR 277
Cdd:smart00631  80 ygrDPRVTNLLDKTDIYIVPVLNPDGYEYTHTGDRLWRKNRSPNS----NCRGVDLNRNFPFHWGE--TGNPCSETYAGP 153
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1JQG_A         278 SAFSEPESSVIRDIIAEHRnRMALYLDIHSFGSMILYGYGNGV--LPSNALQLHLIGVQMAQAIDRVkwsSNKDYIVGNI 355
Cdd:smart00631 154 SPFSEPETKAVRDFIRSNR-RFKLYIDLHSYSQLILYPYGYTKndLPPNVDDLDAVAKALAKALASV---HGTRYTYGIS 229
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|..
1JQG_A         356 FHVLYAASGGASDYAMQAA-APFSYTYELPAYRNSvwfdGFLVDPDFIEQAG 406
Cdd:smart00631 230 NGAIYPASGGSDDWAYGVLgIPFSFTLELRDDGRY----GFLLPPSQIIPTG 277
Peptidase_M14 pfam00246
Zinc carboxypeptidase;
127-412 3.24e-79

Zinc carboxypeptidase;


Pssm-ID: 459730 [Multi-domain]  Cd Length: 287  Bit Score: 246.83  E-value: 3.24e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1JQG_A        127 VDAYLQELAKEFPNVVTVVEGGKSFEGRSIKYLRISTTNFQDAS-KPVVMMQSLLHCREWVTLPATLYAIHKLV----ID 201
Cdd:pfam00246   1 IEAWLDALAARYPDLVRLVSIGKSVEGRPLKVLKISSGPGEHNPgKPAVFIDGGIHAREWIGPATALYLIHQLLtnygRD 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1JQG_A        202 VTESDLINNIDWIILPVANPDGYVHTFGGDRYWRKNRATgyMAGNLCMGVDLNRNFGMNWG-TASSSSVCSDTFHGRSAF 280
Cdd:pfam00246  81 PEITELLDDTDIYILPVVNPDGYEYTHTTDRLWRKNRSN--ANGSSCIGVDLNRNFPDHWNeVGASSNPCSETYRGPAPF 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1JQG_A        281 SEPESSVIRDIIaEHRNRMALYLDIHSFGSMILYGYGNGV--LPSNALQLHLIGVQMAQAIdrVKWSSNKDYIVG-NIFH 357
Cdd:pfam00246 159 SEPETRAVADFI-RSKKPFVLYISLHSYSQVLLYPYGYTRdePPPDDEELKSLARAAAKAL--QKMVRGTSYTYGiTNGA 235
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*.
1JQG_A        358 VLYAASGGASDYAMQAA-APFSYTYELPAYRNsvwfDGFLVDPDFIEQAGFETWEG 412
Cdd:pfam00246 236 TIYPASGGSDDWAYGRLgIKYSYTIELRDTGR----YGFLLPASQIIPTAEETWEA 287
MpaA COG2866
Murein tripeptide amidase MpaA [Cell wall/membrane/envelope biogenesis];
117-318 3.77e-33

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


Pssm-ID: 442113 [Multi-domain]  Cd Length: 337  Bit Score: 127.50  E-value: 3.77e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1JQG_A      117 SFDKIHSYEEVDAYLQELAKEfPNVVTVVEGGKSFEGRSIKYLRISTTnfqDASKPVVMMQSLLHCREWVTLPATLYAIH 196
Cdd:COG2866  15 SYDRYYTYEELLALLAKLAAA-SPLVELESIGKSVEGRPIYLLKIGDP---AEGKPKVLLNAQQHGNEWTGTEALLGLLE 90
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1JQG_A      197 KLVIDVTES--DLINNIDWIILPVANPDGYvhtfggDRYWRKNRAtgymagnlcmGVDLNRNFGMNWgtassssvcsdtf 274
Cdd:COG2866  91 DLLDNYDPLirALLDNVTLYIVPMLNPDGA------ERNTRTNAN----------GVDLNRDWPAPW------------- 141
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....
1JQG_A      275 hgrsaFSEPESSVIRDIIAEHrnRMALYLDIHSFGSMILYGYGN 318
Cdd:COG2866 142 -----LSEPETRALRDLLDEH--DPDFVLDLHGQGELFYWFVGT 178
Propep_M14 pfam02244
Carboxypeptidase activation peptide; Carboxypeptidases are found in abundance in pancreatic ...
27-98 5.81e-11

Carboxypeptidase activation peptide; Carboxypeptidases are found in abundance in pancreatic secretions. The pro-segment moiety (activation peptide) accounts for up to a quarter of the total length of the peptidase, and is responsible for modulation of folding and activity of the pro-enzyme.


Pssm-ID: 460505  Cd Length: 73  Bit Score: 57.99  E-value: 5.81e-11
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
1JQG_A         27 YQVDVASMDQVKLVHDFENDLMLDVWSDAV-PGRPGKVLVPKFKREIFENFLKQSGVQYKLEVENVKEQLELE 98
Cdd:pfam02244   1 YRVTPETEEQLQLLKELEESYDLDFWKPPSkVGKPVDVMVPPSKLEAFEELLEKHGISYEVLIEDVQELIDEE 73
 
Name Accession Description Interval E-value
M14_CP_insect cd06248
Peptidase M14 carboxypeptidase subfamily A/B-like; This family includes peptidase M14 ...
121-416 2.27e-158

Peptidase M14 carboxypeptidase subfamily A/B-like; This family includes peptidase M14 carboxypeptidases found specifically in insects, including B-type carboxypeptidase of H. zea (CPBHz, insect gut carboxypeptidase-3) that is insensitive to potato carboxypeptidase inhibitor (PCI) in corn earworm, and midgut procarboxypeptidase A (PCPAHa, insect gut carboxypeptidase-1) from Helicoverpa armigera larva, a devastating pest of crops. PCPAHa preferentially cleaves aliphatic and aromatic residues. The peptidase M14 Carboxypeptidase (CP) A/B subfamily is one of two main M14 CP subfamilies defined by sequence and structural homology, the other being the N/E subfamily. CPs hydrolyze single, C-terminal amino acids from polypeptide chains. They have a recognition site for the free C-terminal carboxyl group, which is a key determinant of specificity. Enzymes belonging to the A/B subfamily are normally synthesized as inactive precursors containing preceding signal peptide, followed by a globular N-terminal pro-region linked to the enzyme; these proenzymes are called procarboxypeptidases. The A/B enzymes can be further divided based on their substrate specificity; Carboxypeptidase A-like (CPA-like) enzymes favor hydrophobic residues while carboxypeptidase B-like (CPB-like) enzymes only cleave the basic residues lysine or arginine. There are nine members in the A/B family: CPA1, CPA2, CPA3, CPA4, CPA5, CPA6, CPB, CPO and CPU. CPA1, CPA2 and CPB are produced by the pancreas. The A forms have slightly different specificities, with CPA1 preferring aliphatic and small aromatic residues, and CPA2 preferring the bulkier aromatic side chains. CPA3 is found in secretory granules of mast cells and functions in inflammatory processes. CPA4 is detected in hormone-regulated tissues, and is thought to play a role in prostate cancer. CPA5 is present in discrete regions of pituitary and other tissues, and cleaves aliphatic C-terminal residues. CPA6 is highly expressed in embryonic brain and optic muscle, suggesting that it may play a specific role in cell migration and axonal guidance. CPU (also called CPB2) is produced and secreted by the liver as the inactive precursor, PCPU, commonly referred to as thrombin-activatable fibrinolysis inhibitor (TAFI). Little is known about CPO but it has been suggested to have specificity for acidic residues.


Pssm-ID: 349467 [Multi-domain]  Cd Length: 297  Bit Score: 448.83  E-value: 2.27e-158
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1JQG_A      121 IHSYEEVDAYLQELAKEFPNVVTVVEGGKSFEGRSIKYLRISTTNFQDASKPVVMMQSLLHCREWVTLPATLYAIHKLVI 200
Cdd:cd06248   1 YHSLDEIDEYLDGLAEESPDVVTVVEGGYTFEGRPIKYVRIRSTNSEDTSKPTIMIEGGINPREWISPPAALYAIHKLVE 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1JQG_A      201 DV-TESDLINNIDWIILPVANPDGYVHTFGGDRYWRKNRATGYMA-GNLCMGVDLNRNFGMNWG-TASSSSVCSDTFHGR 277
Cdd:cd06248  81 DVeTQSDLLNNFDWIILPVANPDGYVFTHTNDREWTKNRSTNSNPlGQICFGVNINRNFDYQWNpVLSSESPCSELYAGP 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1JQG_A      278 SAFSEPESSVIRDIIAEHRNRMALYLDIHSFGSMILYGYGN-GVLPSNALQLHLIGVQMAQAIDRvkwSSNKDYIVGNIF 356
Cdd:cd06248 161 SAFSEAESRAIRDILHEHGNRIHLYISFHSGGSFILYPWGYdGSTSSNARQLHLAGVAAAAAISS---NNGRPYVVGQSS 237
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|
1JQG_A      357 HVLYAASGGASDYAMQaAAPFSYTYELPAYRNsvwFDGFLVDPDFIEQAGFETWEGIKVG 416
Cdd:cd06248 238 VLLYRAAGTSSDYAMG-IAGIDYTYELPGYSS---GDPFYVPPAYIEQVVREAWEGIVVG 293
Zn_pept smart00631
Zn_pept domain;
122-406 9.55e-104

Zn_pept domain;


Pssm-ID: 214748 [Multi-domain]  Cd Length: 277  Bit Score: 309.27  E-value: 9.55e-104
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1JQG_A         122 HSYEEVDAYLQELAKEFPNVVTVVEGGKSFEGRSIKYLRISTTNfqDASKPVVMMQSLLHCREWVTLPATLYAIHKLVI- 200
Cdd:smart00631   2 HSYEEIEAWLKELAARYPDLVRLVSIGKSVEGRPIWVLKISNGG--SHDKPAIFIDAGIHAREWIGPATALYLINQLLEn 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1JQG_A         201 ---DVTESDLINNIDWIILPVANPDGYVHTFGGDRYWRKNRATGYmagnLCMGVDLNRNFGMNWGTasSSSVCSDTFHGR 277
Cdd:smart00631  80 ygrDPRVTNLLDKTDIYIVPVLNPDGYEYTHTGDRLWRKNRSPNS----NCRGVDLNRNFPFHWGE--TGNPCSETYAGP 153
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1JQG_A         278 SAFSEPESSVIRDIIAEHRnRMALYLDIHSFGSMILYGYGNGV--LPSNALQLHLIGVQMAQAIDRVkwsSNKDYIVGNI 355
Cdd:smart00631 154 SPFSEPETKAVRDFIRSNR-RFKLYIDLHSYSQLILYPYGYTKndLPPNVDDLDAVAKALAKALASV---HGTRYTYGIS 229
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|..
1JQG_A         356 FHVLYAASGGASDYAMQAA-APFSYTYELPAYRNSvwfdGFLVDPDFIEQAG 406
Cdd:smart00631 230 NGAIYPASGGSDDWAYGVLgIPFSFTLELRDDGRY----GFLLPPSQIIPTG 277
M14_CP_A-B_like cd03860
Peptidase M14 carboxypeptidase subfamily A/B-like; The Peptidase M14 Carboxypeptidase (CP) A/B ...
122-415 2.10e-101

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: 304.06  E-value: 2.10e-101
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1JQG_A      122 HSYEEVDAYLQELAKEFPNVVTVVEGGKSFEGRSIKYLRISTTNFQDaSKPVVMMQSLLHCREWVTLPATLYAIHKLVI- 200
Cdd:cd03860   2 HPLDDIVQWLDDLAAAFPDNVEIFTIGKSYEGRDITGIHIWGSGGKG-GKPAIVIHGGQHAREWISTSTVEYLAHQLLSg 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1JQG_A      201 ---DVTESDLINNIDWIILPVANPDGYVHTFGGDRYWRKNRATGYmaGNLCMGVDLNRNFGMNWGTA-SSSSVCSDTFHG 276
Cdd:cd03860  81 ygsDATITALLDKFDFYIIPVVNPDGYVYTWTTDRLWRKNRQPTG--GSSCVGIDLNRNWGYKWGGPgASTNPCSETYRG 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1JQG_A      277 RSAFSEPESSVIRDIIAEHR--NRMALYLDIHSFGSMIL--YGYGNGVLPSNALQLHLIGVQMAQAIDRVkwsSNKDYIV 352
Cdd:cd03860 159 PSAFSAPETKALADFINALAagQGIKGFIDLHSYSQLILypYGYSCDAVPPDLENLMELALGAAKAIRAV---HGTTYTV 235
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....
1JQG_A      353 GNIFHVLYAASGGASDYAM-QAAAPFSYTYELpayRNSVWFdGFLVDPDFIEQAGFETWEGIKV 415
Cdd:cd03860 236 GPACSTLYPASGSSLDWAYdVAKIKYSYTIEL---RDTGTY-GFLLPPEQILPTGEETWAGVKY 295
Peptidase_M14 pfam00246
Zinc carboxypeptidase;
127-412 3.24e-79

Zinc carboxypeptidase;


Pssm-ID: 459730 [Multi-domain]  Cd Length: 287  Bit Score: 246.83  E-value: 3.24e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1JQG_A        127 VDAYLQELAKEFPNVVTVVEGGKSFEGRSIKYLRISTTNFQDAS-KPVVMMQSLLHCREWVTLPATLYAIHKLV----ID 201
Cdd:pfam00246   1 IEAWLDALAARYPDLVRLVSIGKSVEGRPLKVLKISSGPGEHNPgKPAVFIDGGIHAREWIGPATALYLIHQLLtnygRD 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1JQG_A        202 VTESDLINNIDWIILPVANPDGYVHTFGGDRYWRKNRATgyMAGNLCMGVDLNRNFGMNWG-TASSSSVCSDTFHGRSAF 280
Cdd:pfam00246  81 PEITELLDDTDIYILPVVNPDGYEYTHTTDRLWRKNRSN--ANGSSCIGVDLNRNFPDHWNeVGASSNPCSETYRGPAPF 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1JQG_A        281 SEPESSVIRDIIaEHRNRMALYLDIHSFGSMILYGYGNGV--LPSNALQLHLIGVQMAQAIdrVKWSSNKDYIVG-NIFH 357
Cdd:pfam00246 159 SEPETRAVADFI-RSKKPFVLYISLHSYSQVLLYPYGYTRdePPPDDEELKSLARAAAKAL--QKMVRGTSYTYGiTNGA 235
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*.
1JQG_A        358 VLYAASGGASDYAMQAA-APFSYTYELPAYRNsvwfDGFLVDPDFIEQAGFETWEG 412
Cdd:pfam00246 236 TIYPASGGSDDWAYGRLgIKYSYTIELRDTGR----YGFLLPASQIIPTAEETWEA 287
M14_CPT cd03859
Peptidase M14 Carboxypeptidase T subfamily; Peptidase M14-like domain of carboxypeptidase (CP) ...
122-413 5.64e-67

Peptidase M14 Carboxypeptidase T subfamily; Peptidase M14-like domain of carboxypeptidase (CP) T (CPT), CPT belongs to the M14 family of metallocarboxypeptidases (MCPs). The M14 family are zinc-binding CPs which hydrolyze single, C-terminal amino acids from polypeptide chains, and have a recognition site for the free C-terminal carboxyl group, which is a key determinant of specificity. CPT has moderate similarity to CPA and CPB, and exhibits dual-substrate specificity by cleaving C-terminal hydrophobic amino acid residues like CPA and C-terminal positively charged residues like CPB. CPA and CPB are M14 family peptidases but do not belong to this CPT group. The substrate specificity difference between CPT and CPA and CPB is ascribed to a few amino acid substitutions at the substrate-binding pocket while the spatial organization of the binding site remains the same as in all Zn-CPs. CPT has increased thermal stability in presence of Ca2+ ions, and two disulfide bridges which give an additional stabilization factor.


Pssm-ID: 349432 [Multi-domain]  Cd Length: 292  Bit Score: 215.20  E-value: 5.64e-67
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1JQG_A      122 HSYEEVDAYLQELAKEFPNVVTVVEGGKSFEGRSIKYLRISTTNFQDASKPVVMMQSLLHCREWVTLPATLYAIHKLV-- 199
Cdd:cd03859   5 HTYAELVAELDQLAAEYPEITKLISIGKSVEGRPIWAVKISDNPDEDEDEPEVLFMGLHHAREWISLEVALYFADYLLen 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1JQG_A      200 --IDVTESDLINNIDWIILPVANPDGYVHTF--GGDRYWRKNRATGYMAGNLCMGVDLNRNFGMNWGTA---SSSSVCSD 272
Cdd:cd03859  85 ygTDPRITNLVDNREIWIIPVVNPDGYEYNRetGGGRLWRKNRRPNNGNNPGSDGVDLNRNYGYHWGGDnggSSPDPSSE 164
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1JQG_A      273 TFHGRSAFSEPESSVIRDIIAEHRNRMAlyLDIHSFGSMILYGYGNGVLPsNALQLHLIgVQMAQAIDRvkwsSNKDYIV 352
Cdd:cd03859 165 TYRGPAPFSEPETQAIRDLVESHDFKVA--ISYHSYGELVLYPWGYTSDA-PTPDEDVF-EELAEEMAS----YNGGGYT 236
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|.
1JQG_A      353 GNIFHVLYAASGGASDYAMQAAAPFSYTYELpayrnSVWFDGFLVDPDFIEQAGFETWEGI 413
Cdd:cd03859 237 PQQSSDLYPTNGDTDDWMYGEKGIIAFTPEL-----GPEFYPFYPPPSQIDPLAEENLPAA 292
M14_CPA cd03870
Peptidase M14 carboxypeptidase subfamily A/B-like; Carboxypeptidase A subgroup; Peptidase M14 ...
117-415 3.77e-61

Peptidase M14 carboxypeptidase subfamily A/B-like; Carboxypeptidase A subgroup; Peptidase M14 Carboxypeptidase (CP) A (CPA) belongs to the A/B subfamily of the M14 family of metallocarboxypeptidases (MCPs). The M14 family are zinc-binding CPs which hydrolyze single, C-terminal amino acids from polypeptide chains, and have a recognition site for the free C-terminal carboxyl group, which is a key determinant of specificity. CPA enzymes generally favor hydrophobic residues. A/B subfamily enzymes 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 procarboxypeptidase A (PCPA) is produced by the exocrine pancreas and stored as a stable zymogen in the pancreatic granules until secretion into the digestive tract occurs. This subfamily includes CPA1, CPA2 and CPA4 forms. Within these A forms, there are slightly different specificities, with CPA1 preferring aliphatic and small aromatic residues, and CPA2 preferring the bulkier aromatic side chains. CPA4, detected in hormone-regulated tissues, is thought to play a role in prostate cancer.


Pssm-ID: 349442 [Multi-domain]  Cd Length: 301  Bit Score: 200.74  E-value: 3.77e-61
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1JQG_A      117 SFDKIHSYEEVDAYLQELAKEFPNVVTVVEGGKSFEGRSIKYLRISTTNfqdASKPVVMMQSLLHCREWVTLPATLYAIH 196
Cdd:cd03870   2 NYAAYHTLEEIYFWMDNLVAEHPNLVSKLQIGSSFENRPMYVLKFSTGG---EERPAIWIDAGIHSREWVTQASAIWTAE 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1JQG_A      197 KLVIDVTE----SDLINNIDWIILPVANPDGYVHTFGGDRYWRKNRATgyMAGNLCMGVDLNRNFGMNW-GTASSSSVCS 271
Cdd:cd03870  79 KIVSDYGKdpsiTSILDTMDIFLEIVTNPDGYVFTHSSNRLWRKTRSV--NPGSLCIGVDPNRNWDAGFgGPGASSNPCS 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1JQG_A      272 DTFHGRSAFSEPESSVIRDIIAEHRNRMALyLDIHSFGSMILYGYGNGVLP-SNALQLHLIGVQMAQAIDRVkwsSNKDY 350
Cdd:cd03870 157 ETYHGPHANSEVEVKSIVDFIQSHGNFKAF-ISIHSYSQLLMYPYGYTVEKaPDQEELDEVAKKAVKALASL---HGTEY 232
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
1JQG_A      351 IVGNIFHVLYAASGGASDYAMQAAAPFSYTYELpayRNSVWFdGFLVDPDFIEQAGFETWEGIKV 415
Cdd:cd03870 233 KVGSISTTIYQASGSSIDWAYDNGIKYAFTFEL---RDTGRY-GFLLPANQIIPTAEETWLALKT 293
M14_CPO cd06247
Peptidase M14 carboxypeptidase subfamily A/B-like; Carboxypeptidase O subgroup; Peptidase M14 ...
118-413 4.61e-58

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


Pssm-ID: 349466 [Multi-domain]  Cd Length: 298  Bit Score: 192.37  E-value: 4.61e-58
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1JQG_A      118 FDKIHSYEEVDAYLQELAKEFPNVVTVVEGGKSFEGRSIKYLRISTTNfqDASKPVVMMQSLLHCREWVTlPATLYAIHK 197
Cdd:cd06247   1 YTKYHPMDEIYQWMDQMQEKNSEVVSQHYLGQTYEKRPMYYLKIGWPS--DKPKKIIWMDCGIHAREWIA-PAFCQWFVK 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1JQG_A      198 LVIDVTESD-----LINNIDWIILPVANPDGYVHTFGGDRYWRKNRATgYMAGNlCMGVDLNRNFGMNWGTASSSSVCSD 272
Cdd:cd06247  78 EILQNYKTDsrlnkLLKNLDFYVLPVLNIDGYIYSWTTDRLWRKSRSP-HNNGT-CYGTDLNRNFNSQWCSIGASRNCCS 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1JQG_A      273 -TFHGRSAFSEPESSVIRDIIAEHRNRMALYLDIHSFGSMILYGYGNGVLPS-NALQLHLIGVQMAQAIdrvKWSSNKDY 350
Cdd:cd06247 156 iIFCGTGPESEPETKAVADLIEKKKSDILCYLTIHSYGQLILLPYGYTKEPSpNHEEMMEVGEKAAAAL---KEKHGTSY 232
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|...
1JQG_A      351 IVGNIFHVLYAASGGASDYAMQAAAPFSYTYELpayRNSVWFdGFLVDPDFIEQAGFETWEGI 413
Cdd:cd06247 233 RVGSSADILYSNSGSSRDWARDIGIPFSYTFEL---RDTGTY-GFVLPEDQIQPTCEETMEAV 291
M14_CPB cd03871
Peptidase M14 carboxypeptidase subfamily A/B-like; Carboxypeptidase B subgroup; Peptidase M14 ...
117-414 1.33e-53

Peptidase M14 carboxypeptidase subfamily A/B-like; Carboxypeptidase B subgroup; Peptidase M14 Carboxypeptidase B (CPB) belongs to the carboxypeptidase A/B subfamily of the M14 family of metallocarboxypeptidases (MCPs). The M14 family are zinc-binding CPs which hydrolyze single, C-terminal amino acids from polypeptide chains, and have a recognition site for the free C-terminal carboxyl group, which is a key determinant of specificity. Carboxypeptidase B (CPB) enzymes only cleave the basic residues lysine or arginine. A/B subfamily enzymes 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 procarboxypeptidase B (PCPB) is produced by the exocrine pancreas and stored as stable zymogen in the pancreatic granules until secretion into the digestive tract occurs. PCPB has been reported to be a good serum marker for the diagnosis of acute pancreatitis and graft rejection in pancreas transplant recipients. this subfamily also includes thrombin activatable fibrinolysis inhibitor (TAFIa), a carboxypeptidase that stabilizes fibrin clots by removing C-terminal arginines and lysines from partially degraded fibrin. Inhibition of TAFIa stimulates the degradation of fibrin clots and may help in prevention of thrombosis.


Pssm-ID: 349443 [Multi-domain]  Cd Length: 300  Bit Score: 180.73  E-value: 1.33e-53
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1JQG_A      117 SFDKIHSYEEVDAYLQELAKEFPNVVTVVEGGKSFEGRSIKYLRISTTNfqdASKPVVMMQSLLHCREWVTlPA-----T 191
Cdd:cd03871   2 SYEKYNNWETIEAWTEQVASKNPDLVSRSQIGTTFEGRPIYLLKVGKPG---SNKKAIFMDCGFHAREWIS-PAfcqwfV 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1JQG_A      192 LYAIHKLVIDVTESDLINNIDWIILPVANPDGYVHTFGGDRYWRKNRATGymAGNLCMGVDLNRNFGMNWGT-ASSSSVC 270
Cdd:cd03871  78 REAVRTYGKEKIMTKLLDRLDFYILPVLNIDGYVYTWTKNRMWRKTRSPN--AGSSCIGTDPNRNFNAGWCTvGASSNPC 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1JQG_A      271 SDTFHGRSAFSEPESSVIRDIIAEHRNRMALYLDIHSFGSMILYGYG-NGVLPSNALQLHLIGVqmaQAIDRVKWSSNKD 349
Cdd:cd03871 156 SETYCGSAPESEKETKALANFIRNNLSSIKAYLTIHSYSQMLLYPYSyTYKLAPNHEELNSIAK---GAVKELSSLYGTK 232
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
1JQG_A      350 YIVGNIFHVLYAASGGASDYAMQAAAPFSYTYELpayRNSVWFdGFLVDPDFIEQAGFETWEGIK 414
Cdd:cd03871 233 YTYGPGATTIYPAAGGSDDWAYDQGIKYSFTFEL---RDKGRY-GFLLPESQIKPTCEETMLAVK 293
M14_CPB2 cd06246
Peptidase M14 carboxypeptidase subfamily A/B-like; Carboxypeptidase B2 subgroup; Peptidase M14 ...
118-415 7.07e-48

Peptidase M14 carboxypeptidase subfamily A/B-like; Carboxypeptidase B2 subgroup; Peptidase M14 Carboxypeptidase (CP) B2 (CPB2, also known as plasma carboxypeptidase B, carboxypeptidase U, and CPU), belongs to the carboxpeptidase A/B subfamily of the M14 family of metallocarboxypeptidases (MCPs). The M14 family are zinc-binding CPs which hydrolyze single, C-terminal amino acids from polypeptide chains, and have a recognition site for the free C-terminal carboxyl group, which is a key determinant of specificity. CPB2 enzyme displays B-like activity; it only cleaves the basic residues lysine or arginine. It is produced and secreted by the liver as the inactive precursor, procarboxypeptidase U or PCPB2, commonly referred to as thrombin-activatable fibrinolysis inhibitor (TAFI). It circulates in plasma as a zymogen bound to plasminogen, and the active enzyme, TAFIa, inhibits fibrinolysis. It is highly regulated, increased TAFI concentrations are thought to increase the risk of thrombosis and coronary artery disease by reducing fibrinolytic activity while low TAFI levels have been correlated with chronic liver disease.


Pssm-ID: 349465 [Multi-domain]  Cd Length: 300  Bit Score: 165.75  E-value: 7.07e-48
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1JQG_A      118 FDKIHSYEEVDAYLQELAKEFPNVVTVVEGGKSFEGRSIKYLRISTTNfqDASKPVVMMQSLLHCREWVTLPATLYAIHK 197
Cdd:cd06246   2 YEQYHSLNEIYSWIEFITERHPDMLTKIHIGSSFEKYPLYVLKVSGKE--QTAKNAIWIDCGIHAREWISPAFCLWFIGH 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1JQG_A      198 LV----IDVTESDLINNIDWIILPVANPDGYVHTFGGDRYWRKNRAtgYMAGNLCMGVDLNRNFGMNW-GTASSSSVCSD 272
Cdd:cd06246  80 ASyfygIIGQHTNLLNLVDFYVMPVVNVDGYDYSWKKNRMWRKNRS--KHANNRCIGTDLNRNFDAGWcGKGASSDSCSE 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1JQG_A      273 TFHGRSAFSEPESSVIRDIIAEHRNRMALYLDIHSFGSMIL--YGYGNGVLPsNALQLHLIGVQMAQAIDRvkwSSNKDY 350
Cdd:cd06246 158 TYCGPYPESEPEVKAVASFLRRHKDTIKAYISMHSYSQMVLfpYSYTRNKSK-DHDELSLLAKEAVTAIRK---TSRNRY 233
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
1JQG_A      351 IVGNIFHVLYAASGGASDYAMQAAAPFSYTYELP---AYrnsvwfdGFLVDPDFIEQAGFETWEGIKV 415
Cdd:cd06246 234 TYGPGAETIYLAPGGSDDWAYDLGIKYSFTFELRdrgTY-------GFLLPPSYIKPTCNEALLAVKK 294
M14_CPA6 cd03872
Peptidase M14 carboxypeptidase subfamily A/B-like; Carboxypeptidase A6 subgroup; ...
122-414 2.27e-37

Peptidase M14 carboxypeptidase subfamily A/B-like; Carboxypeptidase A6 subgroup; Carboxypeptidase (CP) A6 (CPA6, also known as CPAH; EC 3.4.17.1), belongs to the carboxypeptidase A/B subfamily of the M14 family of metallocarboxypeptidases (MCPs). The M14 family are zinc-binding CPs which hydrolyze single, C-terminal amino acids from polypeptide chains, and have a recognition site for the free C-terminal carboxyl group, which is a key determinant of specificity. CPA6 prefers large hydrophobic C-terminal amino acids as well as histidine, while peptides with a penultimate glycine or proline are very poorly cleaved. Several neuropeptides are processed by CPA6, including Met- and Leu-enkephalin, angiotensin I, and neurotensin. CPA6 converts enkephalin and neurotensin into forms known to be inactive toward their receptors, but converts inactive angiotensin I into the biologically active angiotensin II. Thus, CPA6 plays a possible role in the regulation of neuropeptides in the extracellular environment within the olfactory bulb where it is highly expressed. It is also broadly expressed in embryonic tissue, being found in neuronal tissues, bone, skin as well as the lateral rectus eye muscle. A disruption in the CPA6 gene is linked to Duane syndrome, a defect in the abducens nerve/lateral rectus muscle connection.


Pssm-ID: 349444 [Multi-domain]  Cd Length: 300  Bit Score: 137.80  E-value: 2.27e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1JQG_A      122 HSYEEVDAYLQELAKEFPNVVTVVEGGKSFEGRSIKYLRISTTNfqDASKPVVMMQSLLHCREWVTlPATLYAIHKLVID 201
Cdd:cd03872   3 HSLEEIESWMFYMNKTHSDLVHMFSIGKSYEGRSLYVLKLGKRS--RSYKKAVWIDCGIHAREWIG-PAFCQWFVKEAIN 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1JQG_A      202 VTESD-----LINNIDWIILPVANPDGYVHTFGGDRYWRKNRATGYMAGnlCMGVDLNRNFGMNW-GTASSSSVCSDTFH 275
Cdd:cd03872  80 SYQTDpamkkMLNQLYFYVMPVFNVDGYHYSWTNDRFWRKTRSKNSRFQ--CRGVDANRNWKVKWcDEGASLHPCDDTYC 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1JQG_A      276 GRSAFSEPESSVIRDIIAEHRNRMALYLDIHSFGSMIL--YGYGNGVLPSnalqLHLIGVQMAQAIDRVKWSSNKDYIVG 353
Cdd:cd03872 158 GPFPESEPEVKAVAQFLRKHRKHVRAYLSFHAYAQMLLypYSYKYATIPN----FGCVESAAHNAVNALQSAYGVRYRYG 233
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|.
1JQG_A      354 NIFHVLYAASGGASDYAMQAAAPFSYTYELpayRNSVWFdGFLVDPDFIEQAGFETWEGIK 414
Cdd:cd03872 234 PASSTLYVSSGSSMDWAYKNGIPYAFAFEL---RDTGYF-GFLLPEGLIKPTCTETMLAVK 290
MpaA COG2866
Murein tripeptide amidase MpaA [Cell wall/membrane/envelope biogenesis];
117-318 3.77e-33

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


Pssm-ID: 442113 [Multi-domain]  Cd Length: 337  Bit Score: 127.50  E-value: 3.77e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1JQG_A      117 SFDKIHSYEEVDAYLQELAKEfPNVVTVVEGGKSFEGRSIKYLRISTTnfqDASKPVVMMQSLLHCREWVTLPATLYAIH 196
Cdd:COG2866  15 SYDRYYTYEELLALLAKLAAA-SPLVELESIGKSVEGRPIYLLKIGDP---AEGKPKVLLNAQQHGNEWTGTEALLGLLE 90
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1JQG_A      197 KLVIDVTES--DLINNIDWIILPVANPDGYvhtfggDRYWRKNRAtgymagnlcmGVDLNRNFGMNWgtassssvcsdtf 274
Cdd:COG2866  91 DLLDNYDPLirALLDNVTLYIVPMLNPDGA------ERNTRTNAN----------GVDLNRDWPAPW------------- 141
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....
1JQG_A      275 hgrsaFSEPESSVIRDIIAEHrnRMALYLDIHSFGSMILYGYGN 318
Cdd:COG2866 142 -----LSEPETRALRDLLDEH--DPDFVLDLHGQGELFYWFVGT 178
Peptidase_M14_like cd00596
M14 family of metallocarboxypeptidases and related proteins; The M14 family of ...
174-396 5.95e-33

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: 123.72  E-value: 5.95e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1JQG_A      174 VMMQSLLHCREWVTLPATLYAIHKLVIDVTESD---LINNIDWIILPVANPDGYVHTFggDRYWRKNRAtgymagnlcmG 250
Cdd:cd00596   1 ILITGGIHGNEVIGVELALALIEYLLENYGNDPlkrLLDNVELWIVPLVNPDGFARVI--DSGGRKNAN----------G 68
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1JQG_A      251 VDLNRNFGMNWGTASSSSVCSDTFHGRSAFSEPESSVIRDIIAEHrnRMALYLDIHSFGSMILYGYG--NGVLPSNALQl 328
Cdd:cd00596  69 VDLNRNFPYNWGKDGTSGPSSPTYRGPAPFSEPETQALRDLAKSH--RFDLAVSYHSSSEAILYPYGytNEPPPDFSEF- 145
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
1JQG_A      329 hligVQMAQAIDRvkWSSNKDYIVGNIfHVLYAASGGASDYAMQAAAPFSYTYELPAYRNSVWFDGFL 396
Cdd:cd00596 146 ----QELAAGLAR--ALGAGEYGYGYS-YTWYSTTGTADDWLYGELGILAFTVELGTADYPLPGTLLD 206
M14_CPT_like cd06226
Peptidase M14-like domain of an uncharacterized group of Peptidase M14 Carboxypeptidase T (CPT) ...
156-383 1.31e-31

Peptidase M14-like domain of an uncharacterized group of Peptidase M14 Carboxypeptidase T (CPT)-like proteins; Peptidase M14-like domain of an uncharacterized group of Peptidase M14 Carboxypeptidase T (CPT)-like proteins. This group belongs to the M14 family of metallocarboxypeptidases (MCPs). The M14 family are zinc-binding CPs which hydrolyze single, C-terminal amino acids from polypeptide chains, and have a recognition site for the free C-terminal carboxyl group, which is a key determinant of specificity. CPT exhibits dual-substrate specificity by cleaving C-terminal hydrophobic amino acid residues and C-terminal positively charged residues. However, CPT does not belong to this CPT-like group.


Pssm-ID: 349445 [Multi-domain]  Cd Length: 267  Bit Score: 121.41  E-value: 1.31e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1JQG_A      156 IKYLRISTTNFQDAS-KPVVMMQSLLHCREWVTLPATLYAIHKLV------IDVTesdlinnidWI-------ILPVANP 221
Cdd:cd06226   2 IRALKLTNKQATPPGeKPKFFMMAAIHAREYTTAELVARFAEDLVagygtdADAT---------WLldytelhLVPQVNP 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1JQG_A      222 DGYVHTFGGdRYWRKNRATGY-MAGNLCMGVDLNRNFGMNWGTA-SSSSVCSDTFHGRSAFSEPESSVIRDIIA------ 293
Cdd:cd06226  73 DGRKIAETG-LLWRKNTNTTPcPASSPTYGVDLNRNSSFKWGGAgAGGSACSETYRGPSAASEPETQAIENYVKqlfpdq 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1JQG_A      294 --EHRNRMA------LYLDIHSFGSMILYGYGNGVLPS-NALQLHLIGVQMA--------QAIdrvkwssnkdyivgnif 356
Cdd:cd06226 152 rgPGLTDPApddtsgIYIDIHSYGNLVLYPWGWTGTPApNAAGLRTLGRKFAyfngytpqQAV----------------- 214
                       250       260
                ....*....|....*....|....*..
1JQG_A      357 hVLYAASGGASDYAMQAAAPFSYTYEL 383
Cdd:cd06226 215 -ALYPTDGTTDDFAYGTLGVAAYTFEL 240
M14-like cd06228
Peptidase M14-like domain; uncharacterized subfamily; A functionally uncharacterized subgroup ...
172-370 1.69e-31

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: 349447  Cd Length: 294  Bit Score: 121.72  E-value: 1.69e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1JQG_A      172 PVVMMQSLLHCREW------VTLPATLYAIHKLVIDVTE----------SDLINNIDWIILPVANPDGYVHTFGGDRYWR 235
Cdd:cd06228   1 PGVYFIGGVHAREWgspdilIYFAADLLEAYTNNTGLTYggktftaaqvKSILENVDLVVFPLVNPDGRWYSQTSESMWR 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1JQG_A      236 KNRATGYMAG-NLCMGVDLNRNFGMNWG---------TASSSSVCSDTFHGRSAFSEPESSVIRDIIAEHRNrMALYLDI 305
Cdd:cd06228  81 KNRNPASAGDgGSCIGVDINRNFDFLWDfpryfdpgrVPASTSPCSETYHGPSAFSEPETRNVVWLFDAYPN-IRWFVDV 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1JQG_A      306 HSFGSMILYGYG------------------NGV-----------LPSNALQLHLIGV--QMAQAIDRVKwssNKDYIVGN 354
Cdd:cd06228 160 HSASELILYSWGddenqstdpamnflnpayDGKrgiagdtryreFIPSDDRTIAVNLanRMALAIAAVR---GRVYTVQQ 236
                       250
                ....*....|....*.
1JQG_A      355 IFHvLYAASGGASDYA 370
Cdd:cd06228 237 AFG-LYPTSGASDDYA 251
M14-CPA-like cd06227
Peptidase M14 carboxypeptidase A-like domain; uncharacterized subfamily; A functionally ...
181-383 9.81e-23

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: 95.80  E-value: 9.81e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1JQG_A      181 HCREWVTLPATLYAIHKLVIDVTESDLINNIDWI----------ILPVANPDGYVHTFGGDRYWRKNratgymaGNlcmG 250
Cdd:cd06227  11 HARELISVESALRLLRQLCGGLQEPAASALRELAreildnvelkIIPNANPDGRRLVESGDYCWRGN-------EN---G 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1JQG_A      251 VDLNRNFGMNWGTASSSSVcSDTFHGRSAFSEPESSVIRDIIAEHRNRmaLYLDIHSFGSMIL--YGYGNGVLPSNALQL 328
Cdd:cd06227  81 VDLNRNWGVDWGKGEKGAP-SEEYPGPKPFSEPETRALRDLALSFKPH--AFVSVHSGMLAIYtpYAYSASVPRPNRAAD 157
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*..
1JQG_A      329 hligvqMAQAIDRVKWSSNKDYIVGNIFHVL-YAASGGASDYAM-QAAAPFSYTYEL 383
Cdd:cd06227 158 ------MDDLLDVVAKASCGDCTVGSAGKLVgYLADGTAMDYMYgKLKVPYSFTFEI 208
M14_CP_bacteria cd18173
bacterial peptidase M14 carboxypeptidase, uncharacterized; This family contains only bacterial ...
118-307 1.26e-19

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: 88.40  E-value: 1.26e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1JQG_A      118 FDKIHSYEEVDAYLQELAKEFPNVVTVVEGGKSFEGRSIKYLRISTTNFQDASKPVVMMQSLLHCREWVTLPATLYAIHK 197
Cdd:cd18173   1 WDSYPTYEEYEAMMQSFAANYPNICRLVSIGTSVQGRKLLALKISDNVNTEEAEPEFKYTSTMHGDETTGYELMLRLIDY 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1JQG_A      198 LV----IDVTESDLINNIDWIILPVANPDGYVHtfGGDRywRKNRATGYMAgNlcmGVDLNRNFGMNWgtassssvcsDT 273
Cdd:cd18173  81 LLtnygTDPRITNLVDNTEIWINPLANPDGTYA--GGNN--TVSGATRYNA-N---GVDLNRNFPDPV----------DG 142
                       170       180       190
                ....*....|....*....|....*....|....
1JQG_A      274 FHGRSAFSEPESSVIRDIIAEHRNRMAlyLDIHS 307
Cdd:cd18173 143 DHPDGNGWQPETQAMMNFADEHNFVLS--ANFHG 174
M14_Endopeptidase_I cd06229
Peptidase M14 carboxypeptidase family-like domain of Endopeptidase I; Peptidase M14-like ...
174-386 2.58e-17

Peptidase M14 carboxypeptidase family-like domain of Endopeptidase I; Peptidase M14-like domain of Gamma-D-glutamyl-L-diamino acid endopeptidase 1 (also known as Gamma-D-glutamyl-meso-diaminopimelate peptidase I, and Endopeptidase I (ENP1); EC 3.4.19.11). ENP1 is a member of the M14 family of metallocarboxypeptidases (MCPs), and is classified as belonging to subfamily C. However it has an exceptional type of activity of hydrolyzing the gamma-D-Glu-(L)meso-diaminopimelic acid (gamma-D-Glu-Dap) bond of L-Ala-gamma-D-Glu-(L)meso-diaminopimelic acid and L-Ala-gamma-D-Glu-(L)meso-diaminopimelic acid(L)-D-Ala peptides. ENP1 has a different substrate specificity and cellular role than MpaA (MpaA does not belong to this group). ENP1 hydrolyzes the gamma-D-Glu-Dap bond of MurNAc-tripeptide and MurNAc-tetrapeptide, as well as the amide bond of free tripeptide and tetrapeptide. ENP1 is active on spore cortex peptidoglycan, and is produced at stage IV of sporulation in forespore and spore integuments.


Pssm-ID: 349448 [Multi-domain]  Cd Length: 238  Bit Score: 80.85  E-value: 2.58e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1JQG_A      174 VMMQSLLHCREWVTLPATL---------YAIHKLVIDVTESDLINNIDWIILPVANPDGYVHTFGG----DRYWRKNRAT 240
Cdd:cd06229   1 VLYNASFHAREYITTLLLMkfiedyakaYVNKSYIRGKDVGELLNKVTLHIVPMVNPDGVEISQNGsnaiNPYYLRLVAW 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1JQG_A      241 GYMAGNLCM------GVDLNRNFGMNWGTASSSSVCSDT---FHGRSAFSEPESSVIRDIIaeHRNRMALYLDIHSFGSM 311
Cdd:cd06229  81 NKKGTDFTGwkanirGVDLNRNFPAGWEKEKRLGPKAPGprdYPGKEPLSEPETKAMAALT--RQNDFDLVLAYHSQGEE 158
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
1JQG_A      312 ILYGYGNGVLPSNAlqlhligvQMAQAIDRVkwSSNKDYIVGNIfhvlyAASGGASDYamqaaapFSYTYELPAY 386
Cdd:cd06229 159 IYWGYNGLEPEESK--------AMAEKFASV--SGYEPVEAEAI-----DSYGGFKDW-------FIYEFKKPSF 211
M14-like cd06905
Peptidase M14-like domain; uncharacterized subfamily; A functionally uncharacterized subgroup ...
116-319 3.78e-17

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: 82.28  E-value: 3.78e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1JQG_A      116 LSFDKIHSYEEVDAYLQELAKEFPNVVTVVEGGKSFEGRSIKYLRIstTNFQ---DASKPVVMMQSLLHCREWVTLPATL 192
Cdd:cd06905   1 LAFDRYYTYAELTARLKALAEAYPNLVRLESIGKSYEGRDIWLLTI--TNGEtgpADEKPALWVDGNIHGNEVTGSEVAL 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1JQG_A      193 YAIHKLVIDVTESDLINNI-DWI---ILPVANPDGYvhtfggDRYW----RKNRAT-------GYMA----------GNL 247
Cdd:cd06905  79 YLAEYLLTNYGKDPEITRLlDTRtfyILPRLNPDGA------EAYKlkteRSGRSSprdddrdGDGDedgpedlngdGLI 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1JQG_A      248 CM----------------------------------------------------GVDLNRNFGMNWGTASSSSVCsdtfh 275
Cdd:cd06905 153 TQmrvkdptgtwkvdpddprlmvdrekgekgfyrlypegidndgdgrynedgpgGVDLNRNFPYNWQPFYVQPGA----- 227
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....
1JQG_A      276 GRSAFSEPESSVIRDIIAEHRNrMALYLDIHSFGSMILYGYGNG 319
Cdd:cd06905 228 GPYPLSEPETRAVADFLLAHPN-IAAVLTFHTSGGMILRPPGTG 270
M14_CPD_I cd03868
Peptidase M14 carboxypeptidase subfamily N/E-like; Carboxypeptidase D, domain I subgroup; The ...
122-257 7.79e-15

Peptidase M14 carboxypeptidase subfamily N/E-like; Carboxypeptidase D, domain I subgroup; The first carboxypeptidase (CP)-like domain of Carboxypeptidase D (CPD; EC 3.4.17.22), domain I. CPD differs from all other metallocarboxypeptidases in that it contains multiple CP-like domains. CPD belongs to the N/E-like subfamily of the M14 family of metallocarboxypeptidases (MCPs).The M14 family are zinc-binding CPs which hydrolyze single, C-terminal amino acids from polypeptide chains, and have a recognition site for the free C-terminal carboxyl group, which is a key determinant of specificity. CPD is a single-chain protein containing a signal peptide, three tandem repeats of CP-like domains separated by short bridge regions, followed by a transmembrane domain, and a C-terminal cytosolic tail. The first two CP-like domains of CPD contain all of the essential active site and substrate-binding residues, the third CP-like domain lacks critical residues necessary for enzymatic activity and is inactive towards standard CP substrates. Domain I is optimally active at pH 6.3-7.5 and prefers substrates with C-terminal Arg, whereas domain II is active at pH 5.0-6.5 and prefers substrates with C-terminal Lys. This Domain I family contains two contiguous surface cysteines that may become palmitoylated and target the enzyme to membranes, thus regulating intracellular trafficking. CPD functions in the processing of proteins that transit the secretory pathway, and is present in all vertebrates as well as Drosophila. It is broadly distributed in all tissue types. Within cells, CPD is present in the trans Golgi network and immature secretory vesicles, but is excluded from mature vesicles. It is thought to play a role in the processing of proteins that are initially processed by furin or related endopeptidases present in the trans Golgi network, such as growth factors and receptors. CPD is implicated in the pathogenesis of lupus erythematosus (LE), it is regulated by TGF-beta in various cell types of murine and human origin and is significantly down-regulated in CD14 positive cells isolated from patients with LE. As down-regulation of CPD leads to down-modulation of TGF-beta, CPD may have a role in a positive feedback loop. In D. melanogaster, the CPD variant 1B short (DmCPD1Bs) is necessary and sufficient for viability of the fruit fly.


Pssm-ID: 349440  Cd Length: 294  Bit Score: 74.59  E-value: 7.79e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1JQG_A      122 HSYEEVDAYLQELAKEFPNVVTVVEGGKSFEGRSIKYLRIST-TNFQDASKPVVMMQSLLHCREWVTLPATLYAIHKLV- 199
Cdd:cd03868   2 HNYDELTDLLHKLAETYPNIAKLHSIGKSVQGRELWVLEISDnVNRREPGKPMFKYVANMHGDETVGRQLLIYLAQYLLe 81
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|.
1JQG_A      200 ---IDVTESDLINNIDWIILPVANPDGYVHTFGGDrYWRKNRATGYMAGNlcmGVDLNRNF 257
Cdd:cd03868  82 nygKDERVTRLVNSTDIHLMPSMNPDGFENSKEGD-CSGDPGYGGRENAN---NVDLNRNF 138
M14_CP_N-E_like cd03858
Peptidase M14 carboxypeptidase subfamily N/E-like; Carboxypeptidase (CP) N/E-like subfamily of ...
122-257 9.41e-14

Peptidase M14 carboxypeptidase subfamily N/E-like; Carboxypeptidase (CP) N/E-like subfamily of the M14 family of metallocarboxypeptidases (MCPs). The M14 family are zinc-binding CPs which hydrolyze single, C-terminal amino acids from polypeptide chains, and have a recognition site for the free C-terminal carboxyl group, which is a key determinant of specificity. 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: 349431 [Multi-domain]  Cd Length: 292  Bit Score: 71.53  E-value: 9.41e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1JQG_A      122 HSYEEVDAYLQELAKEFPNVVTVVEGGKSFEGRSIKYLRIST-TNFQDASKP------------VVMMQSLLHCREWVTL 188
Cdd:cd03858   2 HNYEELEEFLKQVAKRYPNITRLYSIGKSVEGRELWVLEISDnPGVHEPGEPefkyvanmhgneVVGRELLLLLAEYLCE 81
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
1JQG_A      189 PatlYAIHKLVIdvtesDLINNIDWIILPVANPDGYVHTFGGDRYWRKNRATGYmagnlcmGVDLNRNF 257
Cdd:cd03858  82 N---YGKDPRVT-----QLVNSTRIHIMPSMNPDGYEKAQEGDCGGLIGRNNAN-------GVDLNRNF 135
M14_MpaA-like cd06904
Peptidase M14-like domain of Escherichia coli Murein Peptide Amidase A and related proteins; ...
148-321 1.00e-12

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: 66.92  E-value: 1.00e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1JQG_A      148 GKSFEGRSIKYLRisttnFQDASKPVVMMQSLLHCREwvtlPATLYAIHKLVIDVTESDLINNIDWIILPVANPDGYvht 227
Cdd:cd06904   5 GTSVKGRPILAYK-----FGPGSRARILIIGGIHGDE----PEGVSLVEHLLRWLKNHPASGDFHIVVVPCLNPDGL--- 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1JQG_A      228 FGGDRYwrkNRAtgymagnlcmGVDLNRNF-GMNWGTASSSSVCSDTFHGRSAFSEPESSVIRDIIaeHRNRMALYLDIH 306
Cdd:cd06904  73 AAGTRT---NAN----------GVDLNRNFpTKNWEPDARKPKDPRYYPGPKPASEPETRALVELI--ERFKPDRIISLH 137
                       170
                ....*....|....*
1JQG_A      307 SFGSMILYGYGNGVL 321
Cdd:cd06904 138 APYLVNYDGPAKSLL 152
Propep_M14 pfam02244
Carboxypeptidase activation peptide; Carboxypeptidases are found in abundance in pancreatic ...
27-98 5.81e-11

Carboxypeptidase activation peptide; Carboxypeptidases are found in abundance in pancreatic secretions. The pro-segment moiety (activation peptide) accounts for up to a quarter of the total length of the peptidase, and is responsible for modulation of folding and activity of the pro-enzyme.


Pssm-ID: 460505  Cd Length: 73  Bit Score: 57.99  E-value: 5.81e-11
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
1JQG_A         27 YQVDVASMDQVKLVHDFENDLMLDVWSDAV-PGRPGKVLVPKFKREIFENFLKQSGVQYKLEVENVKEQLELE 98
Cdd:pfam02244   1 YRVTPETEEQLQLLKELEESYDLDFWKPPSkVGKPVDVMVPPSKLEAFEELLEKHGISYEVLIEDVQELIDEE 73
M14_Nna1-like cd06237
Peptidase M14-like domain of ATP/GTP binding proteins and cytosolic carboxypeptidases; ...
127-307 2.86e-10

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: 60.27  E-value: 2.86e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1JQG_A      127 VDAYLQELAKEFPnvVTVVEGGKSFEGRSIKYLRISTTNfqdaSKPVVMMQSLLHCREwVT--LpATLYAIHKLVIDvte 204
Cdd:cd06237   3 YDAWIDSLAKKPF--VKRSTIGKSVEGRPIEALTIGNPD----SKELVVLLGRQHPPE-VTgaL-AMQAFVETLLAD--- 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1JQG_A      205 SDLIN------NIdwIILPVANPDGYVHtfGgdrYWRKNratgymAGnlcmGVDLNRnfgmNWGtassssvcsdtfhgrs 278
Cdd:cd06237  72 TELAKafrarfRV--LVVPLLNPDGVDL--G---HWRHN------AG----GVDLNR----DWG---------------- 114
                       170       180       190
                ....*....|....*....|....*....|...
1JQG_A      279 AFSEPESSVIRD----IIAEHRNRMALYLDIHS 307
Cdd:cd06237 115 PFTQPETRAVRDflleLVEEPGGKVVFGLDFHS 147
M14_CPD_III cd06245
Peptidase M14 carboxypeptidase subfamily N/E-like; Carboxypeptidase D, domain III subgroup; ...
122-294 4.80e-09

Peptidase M14 carboxypeptidase subfamily N/E-like; Carboxypeptidase D, domain III subgroup; The third carboxypeptidase (CP)-like domain of Carboxypeptidase D (CPD; EC 3.4.17.22), domain III. CPD differs from all other metallocarboxypeptidases in that it contains multiple CP-like domains. CPD belongs to the N/E-like subfamily of the M14 family of metallocarboxypeptidases (MCPs).The M14 family are zinc-binding CPs which hydrolyze single, C-terminal amino acids from polypeptide chains, and have a recognition site for the free C-terminal carboxyl group, which is a key determinant of specificity. CPD is a single-chain protein containing a signal peptide, three tandem repeats of CP-like domains separated by short bridge regions, followed by a transmembrane domain, and a C-terminal cytosolic tail. The first two CP-like domains of CPD contain all of the essential active site and substrate-binding residues, the third CP-like domain lacks critical residues necessary for enzymatic activity and is inactive towards standard CP substrates. Domain I is optimally active at pH 6.3-7.5 and prefers substrates with C-terminal Arg, whereas domain II is active at pH 5.0-6.5 and prefers substrates with C-terminal Lys. CPD functions in the processing of proteins that transit the secretory pathway, and is present in all vertebrates as well as Drosophila. It is broadly distributed in all tissue types. Within cells, CPD is present in the trans-Golgi network and immature secretory vesicles, but is excluded from mature vesicles. It is thought to play a role in the processing of proteins that are initially processed by furin or related endopeptidases present in the trans-Golgi network, such as growth factors and receptors. CPD is implicated in the pathogenesis of lupus erythematosus (LE), it is regulated by TGF-beta in various cell types of murine and human origin and is significantly down-regulated in CD14 positive cells isolated from patients with LE. As down -regulation of CPD leads to down-modulation of TGF-beta, CPD may have a role in a positive feedback loop.


Pssm-ID: 349464 [Multi-domain]  Cd Length: 283  Bit Score: 57.07  E-value: 4.80e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1JQG_A      122 HSYEEVDAYLQELAKEFPNVVTVVEGGKSFEGRSIKYLRIS-TTNFQDASKPVVMMQSLLHCREWVTLPATLYAIHKLVI 200
Cdd:cd06245   2 HSYKQLSKFLRGLNSNYPTITNLTSLGQSVEKRDIWVLEIGnKPNESEPSEPKILFVGGIHGNAPVGTELLLLLAHFLCH 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1JQG_A      201 ----DVTESDLINNIDWIILPVANPDGYVHTfggdrywRKNRATGYMAGNLCMGVDLNRNFGMNWGtassssvcsdtfhG 276
Cdd:cd06245  82 nykkDSAITKLLNRTRIHIVPSLNPDGAEKA-------EEKKCTSKIGEKNANGVDLDTDFESNAN-------------N 141
                       170
                ....*....|....*...
1JQG_A      277 RSAFSEPESSVIRDIIAE 294
Cdd:cd06245 142 RSGAAQPETKAIMDWLKE 159
M14_CPD_II cd03863
Peptidase M14 carboxypeptidase subfamily N/E-like; Carboxypeptidase D, domain II subgroup; The ...
122-278 2.28e-08

Peptidase M14 carboxypeptidase subfamily N/E-like; Carboxypeptidase D, domain II subgroup; The second carboxypeptidase (CP)-like domain of Carboxypeptidase D (CPD; EC 3.4.17.22), domain II. CPD differs from all other metallocarboxypeptidases in that it contains multiple CP-like domains. CPD belongs to the N/E-like subfamily of the M14 family of metallocarboxypeptidases (MCPs).The M14 family are zinc-binding CPs which hydrolyze single, C-terminal amino acids from polypeptide chains, and have a recognition site for the free C-terminal carboxyl group, which is a key determinant of specificity. CPD is a single-chain protein containing a signal peptide, three tandem repeats of CP-like domains separated by short bridge regions, followed by a transmembrane domain, and a C-terminal cytosolic tail. The first two CP-like domains of CPD contain all of the essential active site and substrate-binding residues, while the third CP-like domain lacks critical residues necessary for enzymatic activity and is inactive towards standard CP substrates. Domain I is optimally active at pH 6.3-7.5 and prefers substrates with C-terminal Arg, whereas domain II is active at pH 5.0-6.5 and prefers substrates with C-terminal Lys. CPD functions in the processing of proteins that transit the secretory pathway, and is present in all vertebrates as well as Drosophila. It is broadly distributed in all tissue types. Within cells, CPD is present in the trans-Golgi network and immature secretory vesicles, but is excluded from mature vesicles. It is thought to play a role in the processing of proteins that are initially processed by furin or related endopeptidases present in the trans-Golgi network, such as growth factors and receptors. CPD is implicated in the pathogenesis of lupus erythematosus (LE), it is regulated by TGF-beta in various cell types of murine and human origin and is significantly down-regulated in CD14 positive cells isolated from patients with LE. As down -regulation of CPD leads to down-modulation of TGF-beta, CPD may have a role in a positive feedback loop.


Pssm-ID: 349435 [Multi-domain]  Cd Length: 296  Bit Score: 55.34  E-value: 2.28e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1JQG_A      122 HSYEEVDAYLQELAKEFPNVVTVVEGGKSFEGRSIKYLRISTT-NFQDASKPVVMMQSLLHCREWVTLPATLYAIHKLV- 199
Cdd:cd03863   9 HHFSDMEIFLRRYANEYPSITRLYSVGKSVELRELYVMEISDNpGVHEPGEPEFKYIGNMHGNEVVGRELLLNLIEYLCk 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1JQG_A      200 ---IDVTESDLINNIDWIILPVANPDGYVHTFGGDRywrknraTGYMAGNLCMGVDLNRNFG-----------------M 259
Cdd:cd03863  89 nfgTDPEVTDLVQNTRIHIMPSMNPDGYEKSQEGDR-------GGTVGRNNSNNYDLNRNFPdqffqitdppqpetlavM 161
                       170
                ....*....|....*....
1JQG_A      260 NWgTASSSSVCSDTFHGRS 278
Cdd:cd03863 162 SW-LKTYPFVLSANLHGGS 179
M14_CP_plant cd18172
Zinc carboxypeptidase, including SOL1, a carboxypeptidase D in plant; This family includes ...
122-257 1.05e-06

Zinc carboxypeptidase, including SOL1, a carboxypeptidase D in plant; This family includes only plant members of the carboxypeptidase (CP) N/E-like subfamily of the M14 family of metallocarboxypeptidases (MCPs). It includes Arabidopsis thaliana SOL1 carboxypeptidase D which is known to possess enzymatic activity to remove the C-terminal arginine residue of CLE19 proprotein in vitro, and SOL1-dependent cleavage of the C-terminal arginine residue is necessary for CLE19 activity in vivo. 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: 349482 [Multi-domain]  Cd Length: 276  Bit Score: 50.10  E-value: 1.05e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1JQG_A      122 HSYEEVDAYLQELAKEFPNVVTVVEGGKSFEGRSIKYLRISTTNFQDASKPVVMMQSLLH-----CREWVTLPATLYAIH 196
Cdd:cd18172   2 HSNAELEDALKAFTRRCGAISRLIVIGSSVNGFPLWALEISDGPGEDETEPAFKFVGNMHgdepvGRELLLRLADWLCAN 81
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|.
1JQG_A      197 KLVIDVTESDLINNIDWIILPVANPDGYvhtfggDRYWRKNRAtgymagnlcmGVDLNRNF 257
Cdd:cd18172  82 YKAKDPLAAKIVENAHLHLVPTMNPDGF------ARRRRNNAN----------NVDLNRDF 126
M14_CPM cd03866
Peptidase M14 carboxypeptidase subfamily N/E-like; Carboxypeptidase M subgroup; Peptidase M14 ...
122-276 2.73e-06

Peptidase M14 carboxypeptidase subfamily N/E-like; Carboxypeptidase M subgroup; Peptidase M14 Carboxypeptidase (CP) M (CPM) belongs to the N/E subfamily of the M14 family of metallocarboxypeptidases (MCPs).The M14 family are zinc-binding CPs which hydrolyze single, C-terminal amino acids from polypeptide chains, and have a recognition site for the free C-terminal carboxyl group, which is a key determinant of specificity. CPM is an extracellular glycoprotein, bound to cell membranes via a glycosyl-phosphatidylinositol on the C-terminus of the protein. It specifically removes C-terminal basic residues such as lysine and arginine from peptides and proteins. The highest levels of CPM have been found in human lung and placenta, but significant amounts are present in kidney, blood vessels, intestine, brain, and peripheral nerves. CPM has also been found in soluble form in various body fluids, including amniotic fluid, seminal plasma and urine. Due to its wide distribution in a variety of tissues, it is believed that it plays an important role in the control of peptide hormones and growth factor activity on the cell surface and in the membrane-localized degradation of extracellular proteins, for example it hydrolyses the C-terminal arginine of epidermal growth factor (EGF) resulting in des-Arg-EGF which binds to the EGF receptor (EGFR) with an equal or greater affinity than native EGF. CPM is a required processing enzyme that generates specific agonists for the B1 receptor.


Pssm-ID: 349438  Cd Length: 289  Bit Score: 48.64  E-value: 2.73e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1JQG_A      122 HSYEEVDAYLQELAKEFPNVVTVVEGGKSFEGRSIKYL---------RISTTNFqdasKPVVMMqsllHCREWVTLPATL 192
Cdd:cd03866   2 HNQEQMETYLKDVNKNYPSITHLHSIGKSVEGRDLWVLvlgrfptkhRIGIPEF----KYVANM----HGDEVVGRELLL 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1JQG_A      193 YAIHKLV----IDVTESDLINNIDWIILPVANPDGYVHTFGGDRYWRKNRATGYmagnlcmGVDLNRNFG---------- 258
Cdd:cd03866  74 HLIEFLVtsygSDPVITRLINSTRIHIMPSMNPDGFEATKKPDCYYTKGRYNKN-------GYDLNRNFPdafeennvqr 146
                       170       180
                ....*....|....*....|....*
1JQG_A      259 -------MNWgTASSSSVCSDTFHG 276
Cdd:cd03866 147 qpetravMDW-IKNETFVLSANLHG 170
M14_CPZ cd03867
Peptidase M14 carboxypeptidase subfamily N/E-like; Carboxypeptidase Z subgroup; Peptidase ...
122-257 5.95e-06

Peptidase M14 carboxypeptidase subfamily N/E-like; Carboxypeptidase Z subgroup; Peptidase M14-like domain of carboxypeptidase (CP) Z (CPZ), CPZ belongs to the N/E subfamily of the M14 family of metallocarboxypeptidases (MCPs). The M14 family are zinc-binding CPs which hydrolyze single, C-terminal amino acids from polypeptide chains, and have a recognition site for the free C-terminal carboxyl group, which is a key determinant of specificity. CPZ is a secreted Zn-dependent enzyme whose biological function is largely unknown. Unlike other members of the N/E subfamily, CPZ has a bipartite structure, which consists of an N-terminal cysteine-rich domain (CRD) whose sequence is similar to Wnt-binding proteins, and a C-terminal CP catalytic domain that removes C-terminal Arg residues from substrates. CPZ is enriched in the extracellular matrix and is widely distributed during early embryogenesis. That the CRD of CPZ can bind to Wnt4 suggests that CPZ plays a role in Wnt signaling.


Pssm-ID: 349439  Cd Length: 315  Bit Score: 47.96  E-value: 5.95e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1JQG_A      122 HSYEEVDAYLQELAKEFPNVVTVVEGGKSFEGRSIKYLRISTTNFQ-DASKPVVMMQSLLHCREWVTLPATLYAIHKLVI 200
Cdd:cd03867   2 HSYSQMVRVLKKTAARCAHIARTYSIGRSFEGKDLLVIEFSSNPGQhELLEPEVKYIGNMHGNEVVGREMLIYLAQYLCS 81
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
1JQG_A      201 DVTESD-----LINNIDWIILPVANPDGYVHTFG-GDRY--WRKNRATgymAGNLcmgvDLNRNF 257
Cdd:cd03867  82 EYLLGNpriqtLINTTRIHLLPSMNPDGYEVAAEeGAGYngWTSGRQN---AQNL----DLNRNF 139
M14-like cd06242
Peptidase M14-like domain; uncharacterized subgroup; Peptidase M14-like domain of a ...
171-310 7.02e-06

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


Pssm-ID: 349461 [Multi-domain]  Cd Length: 220  Bit Score: 46.91  E-value: 7.02e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1JQG_A      171 KPVVMMQSLLHCREwvtlPA----TLYAIHKLVIDVTESDLINNIDWIILPVANPDGYvhtfggDRYWRKNRAtgymagn 246
Cdd:cd06242   1 KPTVLLVGQQHGNE----PAgreaALALARDLAFGDDARELLEKVNVLVVPRANPDGR------AANTRGNAN------- 63
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....
1JQG_A      247 lcmGVDLNRNFgmnwgtassssvcsdtfhgrSAFSEPESSVIRDIIAEHRNRMAlyLDIHSFGS 310
Cdd:cd06242  64 ---GVDLNRDH--------------------LLLSTPETRALARVLRDYRPEVV--IDAHEFGG 102
M14_CPE cd03865
Peptidase M14 carboxypeptidase subfamily N/E-like; Carboxypeptidase E subgroup; Peptidase M14 ...
122-257 9.85e-05

Peptidase M14 carboxypeptidase subfamily N/E-like; Carboxypeptidase E subgroup; Peptidase M14 Carboxypeptidase (CP) E (CPE, also known as carboxypeptidase H, and enkephalin convertase; EC 3.4.17.10) belongs to the N/E subfamily of the M14 family of metallocarboxypeptidases (MCPs).The M14 family are zinc-binding CPs which hydrolyze single, C-terminal amino acids from polypeptide chains, and have a recognition site for the free C-terminal carboxyl group, which is a key determinant of specificity. CPE is an important enzyme responsible for the proteolytic processing of prohormone intermediates (such as pro-insulin, pro-opiomelanocortin, or pro-gonadotropin-releasing hormone) by specifically removing C-terminal basic residues. In addition, it has been proposed that the regulated secretory pathway (RSP) of the nervous and endocrine systems utilizes membrane-bound CPE as a sorting receptor. A naturally occurring point mutation in CPE reduces the stability of the enzyme and causes its degradation, leading to an accumulation of numerous neuroendocrine peptides that result in obesity and hyperglycemia. Reduced CPE enzyme and receptor activity could underlie abnormal placental phenotypes from the observation that CPE is down-regulated in enlarged placentas of interspecific hybrid (interspecies hybrid placental dysplasia, IHPD) and cloned mice.


Pssm-ID: 349437 [Multi-domain]  Cd Length: 319  Bit Score: 44.20  E-value: 9.85e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1JQG_A      122 HSYEEVDAYLQELAKEFPNVVTVVEGGKSFEGRSIKYLRISTT-NFQDASKPVVMMQSLLHCREWVTLPATLYAIHKLVI 200
Cdd:cd03865   2 HRYPELREALVSVWLQCPAISRIYTVGRSFEGRELLVIEVSDNpGEHEPGEPEFKYVGNMHGNEAVGRELLIFLAQYLCN 81
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
1JQG_A      201 DVTES-----DLINNIDWIILPVANPDGY---VHTFGGDRYWRKNRATGymagnlcMGVDLNRNF 257
Cdd:cd03865  82 EYQKGnetiiNLIHSTRIHIMPSLNPDGFekaASQPGELKDWFVGRSNA-------QGIDLNRNF 139
COG3608 COG3608
Predicted deacylase [General function prediction only];
172-309 4.40e-04

Predicted deacylase [General function prediction only];


Pssm-ID: 442826 [Multi-domain]  Cd Length: 296  Bit Score: 42.14  E-value: 4.40e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1JQG_A      172 PVVMMQSLLHCREwvtLPATlYAIHKLVIDVTESDLINNIdwIILPVANPDGYVHtfgGDRYWRKNratgymagnlcmGV 251
Cdd:COG3608  27 PTLLITAGIHGDE---LNGI-EALRRLLRELDPGELRGTV--ILVPVANPPGFLQ---GSRYLPID------------GR 85
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*....
1JQG_A      252 DLNRNFgmnWGTASSSsvcsdtfhgrsafsepESSVIRDIIAEHRNRMA-LYLDIHSFG 309
Cdd:COG3608  86 DLNRSF---PGDADGS----------------LAERIAHALFEEILPDAdYVIDLHSGG 125
M14-like cd03857
Peptidase M14-like domain; uncharacterized subfamily; Peptidase M14-like domain of a ...
173-353 1.44e-03

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


Pssm-ID: 349430 [Multi-domain]  Cd Length: 203  Bit Score: 39.75  E-value: 1.44e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1JQG_A      173 VVMMQSLLHCREWVTLPATLYAIHKLVIDVTE-SDLINNIDWIILPVANPDGYV--HTFGGDRY--WRKNRATGYmagnl 247
Cdd:cd03857   1 TVLLAAQIHGNETTGTEALMELIRDLASESDEaAKLLDNIVILLVPQLNPDGAElfVNFYLDSMngLPGTRYNAN----- 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1JQG_A      248 cmGVDLNRNFGMnwgtassssvcsdtfhgrsaFSEPESSVIRDIIaEHRnRMALYLDIHS-FGSMILYG--YGNGVLPSN 324
Cdd:cd03857  76 --GIDLNRDHVK--------------------LTQPETQAVAENF-IHW-WPDIFIDLHEqVGASIPYPtpPDAPNYNLV 131
                       170       180       190
                ....*....|....*....|....*....|
1JQG_A      325 ALQLHLIGVQMAQA-IDRVKWSSNKDYIVG 353
Cdd:cd03857 132 DLRSDAENGQEHIRlIAGEGSGELGKYFSP 161
M14_Nna1-like cd03856
Peptidase M14-like domain of ATP/GTP binding proteins, cytosolic carboxypeptidases and related ...
142-307 1.79e-03

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: 39.88  E-value: 1.79e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1JQG_A      142 VTVVEGGKSFEGRSIKYLRISTTnFQDASKPVVMMQSLLHCREwvtlPATLYAIHKLVIDVTESD-----LINNIDWIIL 216
Cdd:cd03856  15 VQLLEIGVTEQGREIQALQSLRT-ERSDDKSWLFLIARQHPGE----TTGAWVFFGFLDQLLSDDdpaqqLRAEYNFYII 89
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1JQG_A      217 PVANPDGYVHTfggdrYWRKNratgymagnlCMGVDLNRnfgmNWGTAssssvcsdtfhgrSAFSEPESSVIRDIIAE-- 294
Cdd:cd03856  90 PMVNPDGVARG-----HWRTN----------SRGMDLNR----DWHAP-------------DALLSPETYAVAAALAErv 137
                       170
                ....*....|....
1JQG_A      295 -HRNRMALYLDIHS 307
Cdd:cd03856 138 qSPEGVVLALDLHG 151
M14_REP34-like cd06231
Peptidase M14-like domain similar to rapid encystment phenotype 34 (REP34); This family ...
206-385 2.46e-03

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: 39.21  E-value: 2.46e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1JQG_A      206 DLINNIDWIILPVANPDGYVHtfgGDRYwrkNRAtgymagnlcmGVDLNRNFGMNwgtassssvcsdtfhgrsaFSEPES 285
Cdd:cd06231  72 KYLRRVNLLVLPCVNPWGFER---NTRE---NAD----------GIDLNRSFLKD-------------------SPSPEV 116
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1JQG_A      286 SVIRDIIAeHRNRMALYLDIH----SFGSmilYGY---GNGVLPSNALQLHLIGVQMAQAIDRVKWSSNKDYIVGNifHV 358
Cdd:cd06231 117 RALMEFLA-SLGRFDLHLDLHedwdSDGF---YLYelgPALKAGRDGLQAVDAVIPPDPISLTIDGSPAPDGVILR--PD 190
                       170       180
                ....*....|....*....|....*....
1JQG_A      359 LYAASGGAS--DYAMQAAAPFSYTYELPA 385
Cdd:cd06231 191 DPAERPGWPfaIYLVANGAVRTYTTETPS 219
 
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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