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Conserved domains on  [gi|663499727|gb|AIE90645|]
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peptidase M14 carboxypeptidase A (cpt) [uncultured marine group II/III euryarchaeote AD1000_04_H03]

Protein Classification

M14 family metallopeptidase( domain architecture ID 27772)

M14 family metallopeptidase is a zinc-binding carboxypeptidase (CP) which hydrolyzes single, C-terminal amino acids from polypeptide chains, and has a recognition site for the free C-terminal carboxyl group, which is a key determinant of specificity.

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Peptidase_M14_like super family cl11393
M14 family of metallocarboxypeptidases and related proteins; The M14 family of ...
 62-496 2.49e-57

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.


The actual alignment was detected with superfamily member cd03859:

Pssm-ID: 472171 [Multi-domain]  Cd Length: 292  Bit Score: 196.32  E-value: 2.49e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663499727  62 YHDYFSMKQRMQTLAAYYPDFLQYHEglLGgvnargdeMTSEDYEGWFYKhsspwmkITGNVQGGDyndfndddgnyaDR 141
Cdd:cd03859    4 YHTYAELVAELDQLAAEYPEITKLIS--IG--------KSVEGRPIWAVK-------ISDNPDEDE------------DE 54

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663499727 142 PDVMLVGNHHAREWMSYEVPMFFLETIAYYYGkagidndgdglvdedgwdgidndgdcsllnatnqdsngdgtpcgpgdl 221
Cdd:cd03859   55 PEVLFMGLHHAREWISLEVALYFADYLLENYG------------------------------------------------ 86

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663499727 222 gvdedfSEQFITDLINTREIYLIPMLNTDGNRYDREEYcgetawencYRSGWRKNLRDNTvtgvtpipdvdeEVDEGCDG 301
Cdd:cd03859   87 ------TDPRITNLVDNREIWIIPVVNPDGYEYNRETG---------GGRLWRKNRRPNN------------GNNPGSDG 139

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663499727 302 VDLNRNYQFEWGaplgatgplfpgmCYADGANN----DVYNGPvnyedndddglvnedhvdgkdddadgqvdedwmGGNS 377
Cdd:cd03859  140 VDLNRNYGYHWG-------------GDNGGSSPdpssETYRGP---------------------------------APFS 173

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663499727 378 EPETKFIQDMTEMNDddgdgasdFKVTLTWHSFSELVLWPWGHCTNCYTPDDEYLVYHGNVMGQMTD--YAPMQSSELYP 455
Cdd:cd03859  174 EPETQAIRDLVESHD--------FKVAISYHSYGELVLYPWGYTSDAPTPDEDVFEELAEEMASYNGggYTPQQSSDLYP 245

                        410       420       430       440
                 ....*....|....*....|....*....|....*....|....
gi 663499727 456 TTGDFCDWHYGVHESYCYTIEIGNAFH---ELPEDIAHIAVRNL 496
Cdd:cd03859  246 TNGDTDDWMYGEKGIIAFTPELGPEFYpfyPPPSQIDPLAEENL 289
Peptidases_S8_S53 super family cl10459
Peptidase domain in the S8 and S53 families; Members of the peptidases S8 (subtilisin and ...
 176-216 3.69e-03

Peptidase domain in the S8 and S53 families; Members of the peptidases S8 (subtilisin and kexin) and S53 (sedolisin) family include endopeptidases and exopeptidases. The S8 family has an Asp/His/Ser catalytic triad similar to that found in trypsin-like proteases, but do not share their three-dimensional structure and are not homologous to trypsin. Serine acts as a nucleophile, aspartate as an electrophile, and histidine as a base. The S53 family contains a catalytic triad Glu/Asp/Ser with an additional acidic residue Asp in the oxyanion hole, similar to that of subtilisin. The serine residue here is the nucleophilic equivalent of the serine residue in the S8 family, while glutamic acid has the same role here as the histidine base. However, the aspartic acid residue that acts as an electrophile is quite different. In S53, it follows glutamic acid, while in S8 it precedes histidine. The stability of these enzymes may be enhanced by calcium; some members have been shown to bind up to 4 ions via binding sites with different affinity. There is a great diversity in the characteristics of their members: some contain disulfide bonds, some are intracellular while others are extracellular, some function at extreme temperatures, and others at high or low pH values.


The actual alignment was detected with superfamily member cd07473:

Pssm-ID: 415849 [Multi-domain]  Cd Length: 259  Bit Score: 39.87  E-value: 3.69e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 663499727 176 GIDNDGDGLVDED-GWDGIDNDGDcsllnatNQDSNGDGTPC 216
Cdd:cd07473   35 GIDDDGNGYVDDIyGWNFVNNDND-------PMDDNGHGTHV 69
 
Name Accession Description Interval E-value
M14_CPT cd03859
Peptidase M14 Carboxypeptidase T subfamily; Peptidase M14-like domain of carboxypeptidase (CP) ...
 62-496 2.49e-57

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: 196.32  E-value: 2.49e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663499727  62 YHDYFSMKQRMQTLAAYYPDFLQYHEglLGgvnargdeMTSEDYEGWFYKhsspwmkITGNVQGGDyndfndddgnyaDR 141
Cdd:cd03859    4 YHTYAELVAELDQLAAEYPEITKLIS--IG--------KSVEGRPIWAVK-------ISDNPDEDE------------DE 54

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663499727 142 PDVMLVGNHHAREWMSYEVPMFFLETIAYYYGkagidndgdglvdedgwdgidndgdcsllnatnqdsngdgtpcgpgdl 221
Cdd:cd03859   55 PEVLFMGLHHAREWISLEVALYFADYLLENYG------------------------------------------------ 86

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663499727 222 gvdedfSEQFITDLINTREIYLIPMLNTDGNRYDREEYcgetawencYRSGWRKNLRDNTvtgvtpipdvdeEVDEGCDG 301
Cdd:cd03859   87 ------TDPRITNLVDNREIWIIPVVNPDGYEYNRETG---------GGRLWRKNRRPNN------------GNNPGSDG 139

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663499727 302 VDLNRNYQFEWGaplgatgplfpgmCYADGANN----DVYNGPvnyedndddglvnedhvdgkdddadgqvdedwmGGNS 377
Cdd:cd03859  140 VDLNRNYGYHWG-------------GDNGGSSPdpssETYRGP---------------------------------APFS 173

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663499727 378 EPETKFIQDMTEMNDddgdgasdFKVTLTWHSFSELVLWPWGHCTNCYTPDDEYLVYHGNVMGQMTD--YAPMQSSELYP 455
Cdd:cd03859  174 EPETQAIRDLVESHD--------FKVAISYHSYGELVLYPWGYTSDAPTPDEDVFEELAEEMASYNGggYTPQQSSDLYP 245

                        410       420       430       440
                 ....*....|....*....|....*....|....*....|....
gi 663499727 456 TTGDFCDWHYGVHESYCYTIEIGNAFH---ELPEDIAHIAVRNL 496
Cdd:cd03859  246 TNGDTDDWMYGEKGIIAFTPELGPEFYpfyPPPSQIDPLAEENL 289
Zn_pept smart00631
Zn_pept domain;
62-478 8.19e-26

Zn_pept domain;


Pssm-ID: 214748 [Multi-domain]  Cd Length: 277  Bit Score: 107.81  E-value: 8.19e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663499727    62 YHDYFSMKQRMQTLAAYYPDFLQYHEGllgGVNARGDEMTSedyegwfykhsspwMKITgnvqggdyndfnddDGNYADR 141
Cdd:smart00631   1 YHSYEEIEAWLKELAARYPDLVRLVSI---GKSVEGRPIWV--------------LKIS--------------NGGSHDK 49

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663499727   142 PDVMLVGNHHAREWMSYEVPMFFLETIayyygkagidndgdglvdedgwdgidndgdcsllnatnqdsngdgtpcgpgdl 221
Cdd:smart00631  50 PAIFIDAGIHAREWIGPATALYLINQL----------------------------------------------------- 76

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663499727   222 gVDEDFSEQFITDLINTREIYLIPMLNTDGNRYDREEYCGetawencyrsgWRKNLRDNTvtgvtpipdvdeevdeGCDG 301
Cdd:smart00631  77 -LENYGRDPRVTNLLDKTDIYIVPVLNPDGYEYTHTGDRL-----------WRKNRSPNS----------------NCRG 128

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663499727   302 VDLNRNYQFEWGAPlgatgplfpgmcyaDGANNDVYNGPvnyedndddglvnedhvdgkdddadgqvdedwmGGNSEPET 381
Cdd:smart00631 129 VDLNRNFPFHWGET--------------GNPCSETYAGP---------------------------------SPFSEPET 161

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663499727   382 KFIQDMTEMNDDdgdgasdFKVTLTWHSFSELVLWPWGHCTNCYTPDDEYLVYHGNVMGQM------TDYAPMQSSE-LY 454
Cdd:smart00631 162 KAVRDFIRSNRR-------FKLYIDLHSYSQLILYPYGYTKNDLPPNVDDLDAVAKALAKAlasvhgTRYTYGISNGaIY 234

                          410       420
                   ....*....|....*....|....*
gi 663499727   455 PTTGDFCDWHYGVH-ESYCYTIEIG 478
Cdd:smart00631 235 PASGGSDDWAYGVLgIPFSFTLELR 259
Peptidase_M14 pfam00246
Zinc carboxypeptidase;
132-496 9.96e-22

Zinc carboxypeptidase;


Pssm-ID: 459730 [Multi-domain]  Cd Length: 287  Bit Score: 95.83  E-value: 9.96e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663499727  132 NDDDGNYADRPDVMLVGNHHAREWMSYEVPMFFLETiayyygkagidndgdglvdedgwdgidndgdcsLLNATNQDSNg 211
Cdd:pfam00246  37 SGPGEHNPGKPAVFIDGGIHAREWIGPATALYLIHQ---------------------------------LLTNYGRDPE- 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663499727  212 dgtpcgpgdlgvdedfseqfITDLINTREIYLIPMLNTDGNRYDREEYCGetawencyrsgWRKNLRDNTVTGvtpipdv 291
Cdd:pfam00246  83 --------------------ITELLDDTDIYILPVVNPDGYEYTHTTDRL-----------WRKNRSNANGSS------- 124

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663499727  292 deevdegCDGVDLNRNYQFEWGAPLGATGPlfpgmcyadgaNNDVYNGPVNYedndddglvnedhvdgkdddadgqvded 371
Cdd:pfam00246 125 -------CIGVDLNRNFPDHWNEVGASSNP-----------CSETYRGPAPF---------------------------- 158

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663499727  372 wmggnSEPETK----FIQDMTemndddgdgasDFKVTLTWHSFSELVLWPWGHCTNCYTPDDE---YLVYHG------NV 438
Cdd:pfam00246 159 -----SEPETRavadFIRSKK-----------PFVLYISLHSYSQVLLYPYGYTRDEPPPDDEelkSLARAAakalqkMV 222

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 663499727  439 MGQMTDYAPMQSSELYPTTGDFCDWHYGVHES-YCYTIEIG----NAFHELPEDIAHIAVRNL 496
Cdd:pfam00246 223 RGTSYTYGITNGATIYPASGGSDDWAYGRLGIkYSYTIELRdtgrYGFLLPASQIIPTAEETW 285
MpaA COG2866
Murein tripeptide amidase MpaA [Cell wall/membrane/envelope biogenesis];
139-312 6.60e-05

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


Pssm-ID: 442113 [Multi-domain]  Cd Length: 337  Bit Score: 45.84  E-value: 6.60e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663499727 139 ADRPDVMLVGNHHAREWMSYEVPMFFLETIAYYYGKAgidndgdglvdedgwdgidndgdcsllnatnqdsngdgtpcgp 218
Cdd:COG2866   63 EGKPKVLLNAQQHGNEWTGTEALLGLLEDLLDNYDPL------------------------------------------- 99

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663499727 219 gdlgvdedfseqfITDLINTREIYLIPMLNTDGnrYDReeycgetawencyrsGWRKNLRdntvtgvtpipdvdeevdeg 298
Cdd:COG2866  100 -------------IRALLDNVTLYIVPMLNPDG--AER---------------NTRTNAN-------------------- 129

                        170
                 ....*....|....
gi 663499727 299 cdGVDLNRNYQFEW 312
Cdd:COG2866  130 --GVDLNRDWPAPW 141
Peptidases_S8_Subtilisin_like cd07473
Peptidase S8 family domain in Subtilisin-like proteins; This family is a member of the ...
 176-216 3.69e-03

Peptidase S8 family domain in Subtilisin-like proteins; This family is a member of the Peptidases S8 or Subtilases serine endo- and exo-peptidase clan. They have an Asp/His/Ser catalytic triad similar to that found in trypsin-like proteases, but do not share their three-dimensional structure and are not homologous to trypsin. The stability of subtilases may be enhanced by calcium, some members have been shown to bind up to 4 ions via binding sites with different affinity. Some members of this clan contain disulfide bonds. These enzymes can be intra- and extracellular, some function at extreme temperatures and pH values.


Pssm-ID: 173799 [Multi-domain]  Cd Length: 259  Bit Score: 39.87  E-value: 3.69e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 663499727 176 GIDNDGDGLVDED-GWDGIDNDGDcsllnatNQDSNGDGTPC 216
Cdd:cd07473   35 GIDDDGNGYVDDIyGWNFVNNDND-------PMDDNGHGTHV 69
 
Name Accession Description Interval E-value
M14_CPT cd03859
Peptidase M14 Carboxypeptidase T subfamily; Peptidase M14-like domain of carboxypeptidase (CP) ...
 62-496 2.49e-57

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: 196.32  E-value: 2.49e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663499727  62 YHDYFSMKQRMQTLAAYYPDFLQYHEglLGgvnargdeMTSEDYEGWFYKhsspwmkITGNVQGGDyndfndddgnyaDR 141
Cdd:cd03859    4 YHTYAELVAELDQLAAEYPEITKLIS--IG--------KSVEGRPIWAVK-------ISDNPDEDE------------DE 54

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663499727 142 PDVMLVGNHHAREWMSYEVPMFFLETIAYYYGkagidndgdglvdedgwdgidndgdcsllnatnqdsngdgtpcgpgdl 221
Cdd:cd03859   55 PEVLFMGLHHAREWISLEVALYFADYLLENYG------------------------------------------------ 86

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663499727 222 gvdedfSEQFITDLINTREIYLIPMLNTDGNRYDREEYcgetawencYRSGWRKNLRDNTvtgvtpipdvdeEVDEGCDG 301
Cdd:cd03859   87 ------TDPRITNLVDNREIWIIPVVNPDGYEYNRETG---------GGRLWRKNRRPNN------------GNNPGSDG 139

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663499727 302 VDLNRNYQFEWGaplgatgplfpgmCYADGANN----DVYNGPvnyedndddglvnedhvdgkdddadgqvdedwmGGNS 377
Cdd:cd03859  140 VDLNRNYGYHWG-------------GDNGGSSPdpssETYRGP---------------------------------APFS 173

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663499727 378 EPETKFIQDMTEMNDddgdgasdFKVTLTWHSFSELVLWPWGHCTNCYTPDDEYLVYHGNVMGQMTD--YAPMQSSELYP 455
Cdd:cd03859  174 EPETQAIRDLVESHD--------FKVAISYHSYGELVLYPWGYTSDAPTPDEDVFEELAEEMASYNGggYTPQQSSDLYP 245

                        410       420       430       440
                 ....*....|....*....|....*....|....*....|....
gi 663499727 456 TTGDFCDWHYGVHESYCYTIEIGNAFH---ELPEDIAHIAVRNL 496
Cdd:cd03859  246 TNGDTDDWMYGEKGIIAFTPELGPEFYpfyPPPSQIDPLAEENL 289
M14_CPT_like cd06226
Peptidase M14-like domain of an uncharacterized group of Peptidase M14 Carboxypeptidase T (CPT) ...
 222-501 8.45e-28

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: 113.32  E-value: 8.45e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663499727 222 GVDEDfseqfITDLINTREIYLIPMLNTDGNRYDREEYCgetawencyrsgWRKNLrdNTVTGVTPIPDVdeevdegcdG 301
Cdd:cd06226   50 GTDAD-----ATWLLDYTELHLVPQVNPDGRKIAETGLL------------WRKNT--NTTPCPASSPTY---------G 101

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663499727 302 VDLNRNYQFEWGAPLGATGPlfpgmCyadganNDVYNGPvnyedndddglvnedhvdgkdddadgqvdedwmGGNSEPET 381
Cdd:cd06226  102 VDLNRNSSFKWGGAGAGGSA-----C------SETYRGP---------------------------------SAASEPET 137

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663499727 382 KFIQD--MTEMNDDDGDGASD------FKVTLTWHSFSELVLWPWGHCTNCyTPDDEYLVYHGNVMGQMTDYAPMQSSEL 453
Cdd:cd06226  138 QAIENyvKQLFPDQRGPGLTDpapddtSGIYIDIHSYGNLVLYPWGWTGTP-APNAAGLRTLGRKFAYFNGYTPQQAVAL 216

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*....
gi 663499727 454 YPTTGDFCDWHYGVHESYCYTIEIGNAFHELPEDIAHIAV-RNLGIPFY 501
Cdd:cd06226  217 YPTDGTTDDFAYGTLGVAAYTFELGTAFFESCSYFENTILpDNLPALYY 265
Zn_pept smart00631
Zn_pept domain;
62-478 8.19e-26

Zn_pept domain;


Pssm-ID: 214748 [Multi-domain]  Cd Length: 277  Bit Score: 107.81  E-value: 8.19e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663499727    62 YHDYFSMKQRMQTLAAYYPDFLQYHEGllgGVNARGDEMTSedyegwfykhsspwMKITgnvqggdyndfnddDGNYADR 141
Cdd:smart00631   1 YHSYEEIEAWLKELAARYPDLVRLVSI---GKSVEGRPIWV--------------LKIS--------------NGGSHDK 49

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663499727   142 PDVMLVGNHHAREWMSYEVPMFFLETIayyygkagidndgdglvdedgwdgidndgdcsllnatnqdsngdgtpcgpgdl 221
Cdd:smart00631  50 PAIFIDAGIHAREWIGPATALYLINQL----------------------------------------------------- 76

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663499727   222 gVDEDFSEQFITDLINTREIYLIPMLNTDGNRYDREEYCGetawencyrsgWRKNLRDNTvtgvtpipdvdeevdeGCDG 301
Cdd:smart00631  77 -LENYGRDPRVTNLLDKTDIYIVPVLNPDGYEYTHTGDRL-----------WRKNRSPNS----------------NCRG 128

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663499727   302 VDLNRNYQFEWGAPlgatgplfpgmcyaDGANNDVYNGPvnyedndddglvnedhvdgkdddadgqvdedwmGGNSEPET 381
Cdd:smart00631 129 VDLNRNFPFHWGET--------------GNPCSETYAGP---------------------------------SPFSEPET 161

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663499727   382 KFIQDMTEMNDDdgdgasdFKVTLTWHSFSELVLWPWGHCTNCYTPDDEYLVYHGNVMGQM------TDYAPMQSSE-LY 454
Cdd:smart00631 162 KAVRDFIRSNRR-------FKLYIDLHSYSQLILYPYGYTKNDLPPNVDDLDAVAKALAKAlasvhgTRYTYGISNGaIY 234

                          410       420
                   ....*....|....*....|....*
gi 663499727   455 PTTGDFCDWHYGVH-ESYCYTIEIG 478
Cdd:smart00631 235 PASGGSDDWAYGVLgIPFSFTLELR 259
Peptidase_M14 pfam00246
Zinc carboxypeptidase;
132-496 9.96e-22

Zinc carboxypeptidase;


Pssm-ID: 459730 [Multi-domain]  Cd Length: 287  Bit Score: 95.83  E-value: 9.96e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663499727  132 NDDDGNYADRPDVMLVGNHHAREWMSYEVPMFFLETiayyygkagidndgdglvdedgwdgidndgdcsLLNATNQDSNg 211
Cdd:pfam00246  37 SGPGEHNPGKPAVFIDGGIHAREWIGPATALYLIHQ---------------------------------LLTNYGRDPE- 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663499727  212 dgtpcgpgdlgvdedfseqfITDLINTREIYLIPMLNTDGNRYDREEYCGetawencyrsgWRKNLRDNTVTGvtpipdv 291
Cdd:pfam00246  83 --------------------ITELLDDTDIYILPVVNPDGYEYTHTTDRL-----------WRKNRSNANGSS------- 124

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663499727  292 deevdegCDGVDLNRNYQFEWGAPLGATGPlfpgmcyadgaNNDVYNGPVNYedndddglvnedhvdgkdddadgqvded 371
Cdd:pfam00246 125 -------CIGVDLNRNFPDHWNEVGASSNP-----------CSETYRGPAPF---------------------------- 158

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663499727  372 wmggnSEPETK----FIQDMTemndddgdgasDFKVTLTWHSFSELVLWPWGHCTNCYTPDDE---YLVYHG------NV 438
Cdd:pfam00246 159 -----SEPETRavadFIRSKK-----------PFVLYISLHSYSQVLLYPYGYTRDEPPPDDEelkSLARAAakalqkMV 222

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 663499727  439 MGQMTDYAPMQSSELYPTTGDFCDWHYGVHES-YCYTIEIG----NAFHELPEDIAHIAVRNL 496
Cdd:pfam00246 223 RGTSYTYGITNGATIYPASGGSDDWAYGRLGIkYSYTIELRdtgrYGFLLPASQIIPTAEETW 285
M14_CP_A-B_like cd03860
Peptidase M14 carboxypeptidase subfamily A/B-like; The Peptidase M14 Carboxypeptidase (CP) A/B ...
 62-476 5.17e-21

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: 94.13  E-value: 5.17e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663499727  62 YHDYFSMKQRMQTLAAYYPDFLQYHEglLGgvnargdemTSedYEGwfykHSSPWMKITGNVQGGDyndfndddgnyadR 141
Cdd:cd03860    1 YHPLDDIVQWLDDLAAAFPDNVEIFT--IG---------KS--YEG----RDITGIHIWGSGGKGG-------------K 50

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663499727 142 PDVMLVGNHHAREWMSyevPMFfLETIAYyygkagidndgdglvdedgwdgidndgdcSLLnaTNQDSNGDgtpcgpgdl 221
Cdd:cd03860   51 PAIVIHGGQHAREWIS---TST-VEYLAH-----------------------------QLL--SGYGSDAT--------- 86

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663499727 222 gvdedfseqfITDLINTREIYLIPMLNTDGnrYdreEYcgetAWENcYRSgWRKNLRDNTVTGvtpipdvdeevdegCDG 301
Cdd:cd03860   87 ----------ITALLDKFDFYIIPVVNPDG--Y---VY----TWTT-DRL-WRKNRQPTGGSS--------------CVG 131

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663499727 302 VDLNRNYQFEWGAPLGATGPlfpgmCyadganNDVYNGPvnyedndddglvnedhvdgkdddadgqvdedwmGGNSEPET 381
Cdd:cd03860  132 IDLNRNWGYKWGGPGASTNP-----C------SETYRGP---------------------------------SAFSAPET 167

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663499727 382 KFIQD-MTEMNDDDGdgasdFKVTLTWHSFSELVLWPWGHCTNCYTPDDEYLVYHGNVMGQM------TDYAPMQSSE-L 453
Cdd:cd03860  168 KALADfINALAAGQG-----IKGFIDLHSYSQLILYPYGYSCDAVPPDLENLMELALGAAKAiravhgTTYTVGPACStL 242

                        410       420
                 ....*....|....*....|....
gi 663499727 454 YPTTGDFCDWHYGVHE-SYCYTIE 476
Cdd:cd03860  243 YPASGSSLDWAYDVAKiKYSYTIE 266
Peptidase_M14_like cd00596
M14 family of metallocarboxypeptidases and related proteins; The M14 family of ...
 144-488 1.54e-20

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: 90.60  E-value: 1.54e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663499727 144 VMLVGNHHAREWMSYEVPMFFLETIAYYYGKagidndgdglvdedgwdgidndgdcsllnatnqdsngdgtpcgpgdlgv 223
Cdd:cd00596    1 ILITGGIHGNEVIGVELALALIEYLLENYGN------------------------------------------------- 31

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663499727 224 dedfseQFITDLINTREIYLIPMLNTDGNRYDReeycgetawencyRSGWRKNLRdntvtgvtpipdvdeevdegcdGVD 303
Cdd:cd00596   32 ------DPLKRLLDNVELWIVPLVNPDGFARVI-------------DSGGRKNAN----------------------GVD 70

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663499727 304 LNRNYQFEWGaplgatgplfpgMCYADGANNDVYNGPvnyedndddglvnedhvdgkdddadgqvdedwmGGNSEPETKF 383
Cdd:cd00596   71 LNRNFPYNWG------------KDGTSGPSSPTYRGP---------------------------------APFSEPETQA 105

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663499727 384 IQDMTEmndddgdgASDFKVTLTWHSFSELVLWPWGHcTNCYTPDDEYLVYHGNVMGQM---TDYAPMQSSELYPTTGDF 460
Cdd:cd00596  106 LRDLAK--------SHRFDLAVSYHSSSEAILYPYGY-TNEPPPDFSEFQELAAGLARAlgaGEYGYGYSYTWYSTTGTA 176

                        330       340
                 ....*....|....*....|....*...
gi 663499727 461 CDWHYGVHESYCYTIEIGNAFHELPEDI 488
Cdd:cd00596  177 DDWLYGELGILAFTVELGTADYPLPGTL 204
M14-like cd06228
Peptidase M14-like domain; uncharacterized subfamily; A functionally uncharacterized subgroup ...
 142-482 3.09e-14

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: 73.96  E-value: 3.09e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663499727 142 PDVMLVGNHHAREWMSYEVPMFFLETiayyygkagidndgdglvdedgwdgidndgdcsLLNATnqdSNGDGTPCGpgdl 221
Cdd:cd06228    1 PGVYFIGGVHAREWGSPDILIYFAAD---------------------------------LLEAY---TNNTGLTYG---- 40

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663499727 222 gvDEDFSEQFITDLINTREIYLIPMLNTDGNRYDREEycgetawencyRSGWRKNLRDNTVTGvtpipdvdeevDEGCDG 301
Cdd:cd06228   41 --GKTFTAAQVKSILENVDLVVFPLVNPDGRWYSQTS-----------ESMWRKNRNPASAGD-----------GGSCIG 96

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663499727 302 VDLNRNYQFEWGAPLGaTGPLFPGMcyADGANNDVYNGPvnyedndddglvnedhvdgkdddadgqvdedwmGGNSEPET 381
Cdd:cd06228   97 VDINRNFDFLWDFPRY-FDPGRVPA--STSPCSETYHGP---------------------------------SAFSEPET 140

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663499727 382 KFIQDMTemndddgDGASDFKVTLTWHSFSELVLWPWGHCTNCYT-----------------------------PDDEYL 432
Cdd:cd06228  141 RNVVWLF-------DAYPNIRWFVDVHSASELILYSWGDDENQSTdpamnflnpaydgkrgiagdtryrefipsDDRTIA 213

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 663499727 433 VYHGNVMGQ-MT-----DYAPMQSSELYPTTGDFCDWHYGVH-------ESYCYTIEIGNAFH 482
Cdd:cd06228  214 VNLANRMALaIAavrgrVYTVQQAFGLYPTSGASDDYAYSRHfvnpakrKVYGFTIEWGTEFQ 276
M14_CP_insect cd06248
Peptidase M14 carboxypeptidase subfamily A/B-like; This family includes peptidase M14 ...
 225-494 8.35e-10

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: 60.55  E-value: 8.35e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663499727 225 EDFSEQfiTDLINTREIYLIPMLNTDGNRY----DREeycgetawencyrsgWRKNLRDNTVTGVTPipdvdeevdegCD 300
Cdd:cd06248   80 EDVETQ--SDLLNNFDWIILPVANPDGYVFthtnDRE---------------WTKNRSTNSNPLGQI-----------CF 131

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663499727 301 GVDLNRNYQFEWGAPLGATGPlfpgmCyadganNDVYNGPVNYedndddglvnedhvdgkdddadgqvdedwmggnSEPE 380
Cdd:cd06248  132 GVNINRNFDYQWNPVLSSESP-----C------SELYAGPSAF---------------------------------SEAE 167

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663499727 381 TKFIQDMTEMNdddgdgASDFKVTLTWHSFSELVLWPWGHCTNcyTPDDeYLVYH--GNVMGQMT------DYAPMQSSE 452
Cdd:cd06248  168 SRAIRDILHEH------GNRIHLYISFHSGGSFILYPWGYDGS--TSSN-ARQLHlaGVAAAAAIssnngrPYVVGQSSV 238

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*....
gi 663499727 453 LYP----TTGDFCDWHYGVheSYCYTIEI---GNAFHeLPEDIAHIAVR 494
Cdd:cd06248  239 LLYraagTSSDYAMGIAGI--DYTYELPGyssGDPFY-VPPAYIEQVVR 284
M14_CPA cd03870
Peptidase M14 carboxypeptidase subfamily A/B-like; Carboxypeptidase A subgroup; Peptidase M14 ...
 232-477 4.60e-09

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: 58.22  E-value: 4.60e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663499727 232 ITDLINTREIYLIPMLNTDGNRY----DREeycgetawencyrsgWRKNLRDNTvtGVTpipdvdeevdegCDGVDLNRN 307
Cdd:cd03870   90 ITSILDTMDIFLEIVTNPDGYVFthssNRL---------------WRKTRSVNP--GSL------------CIGVDPNRN 140

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663499727 308 YQFEWGAPLGATGPlfpgmCyadganNDVYNGPVnyedndddglvnedhvdgkdddadgqvdedwmgGNSEPETKFIQDM 387
Cdd:cd03870  141 WDAGFGGPGASSNP-----C------SETYHGPH---------------------------------ANSEVEVKSIVDF 176

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663499727 388 TEmndddgdGASDFKVTLTWHSFSELVLWPWGHCTNcYTPDDEYL--------VYHGNVMGQMTDYAPMqSSELYPTTGD 459
Cdd:cd03870  177 IQ-------SHGNFKAFISIHSYSQLLMYPYGYTVE-KAPDQEELdevakkavKALASLHGTEYKVGSI-STTIYQASGS 247

                        250
                 ....*....|....*...
gi 663499727 460 FCDWHYGVHESYCYTIEI 477
Cdd:cd03870  248 SIDWAYDNGIKYAFTFEL 265
M14_Endopeptidase_I cd06229
Peptidase M14 carboxypeptidase family-like domain of Endopeptidase I; Peptidase M14-like ...
 144-498 4.97e-09

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: 57.35  E-value: 4.97e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663499727 144 VMLVGNHHAREWMSyevPMFFLETIAYYygkagidndgdglvdedgwdgidndgdcslLNATNQDSNGDGTPcgpgdlgv 223
Cdd:cd06229    1 VLYNASFHAREYIT---TLLLMKFIEDY------------------------------AKAYVNKSYIRGKD-------- 39

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663499727 224 dedfseqfITDLINTREIYLIPMLNTDGNRY-------DREEYCGETAW-ENCYR-SGWRKNLRdntvtgvtpipdvdee 294
Cdd:cd06229   40 --------VGELLNKVTLHIVPMVNPDGVEIsqngsnaINPYYLRLVAWnKKGTDfTGWKANIR---------------- 95

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663499727 295 vdegcdGVDLNRNYQFEWGAP--LGATGPlfpgmcyadganndvynGPVNYEdndddglvnedhvdGKDDdadgqvdedw 372
Cdd:cd06229   96 ------GVDLNRNFPAGWEKEkrLGPKAP-----------------GPRDYP--------------GKEP---------- 128

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663499727 373 mggNSEPETKFIQDMTEMNdddgdgasDFKVTLTWHSFSELVLWpwghctNCYTPDDEYLVYHGNVMGQMTDYaPMQSSE 452
Cdd:cd06229  129 ---LSEPETKAMAALTRQN--------DFDLVLAYHSQGEEIYW------GYNGLEPEESKAMAEKFASVSGY-EPVEAE 190

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*....
gi 663499727 453 LYPTTGDFCDWhyGVHESYC--YTIEIGNAFHELP-EDIAHIAVRNLGI 498
Cdd:cd06229  191 AIDSYGGFKDW--FIYEFKKpsFTIETGKGNNPLPiSQFDEIYEKNKGV 237
M14_CPO cd06247
Peptidase M14 carboxypeptidase subfamily A/B-like; Carboxypeptidase O subgroup; Peptidase M14 ...
 232-487 9.29e-09

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: 57.55  E-value: 9.29e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663499727 232 ITDLINTREIYLIPMLNTDGNRYdreeycgetAWENcyRSGWRKNlRDNTVTGVtpipdvdeevdegCDGVDLNRNYQFE 311
Cdd:cd06247   89 LNKLLKNLDFYVLPVLNIDGYIY---------SWTT--DRLWRKS-RSPHNNGT-------------CYGTDLNRNFNSQ 143

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663499727 312 WGApLGATgplfpgmcyaDGANNDVYNGPvnyedndddglvnedhvdgkdddadgqvdedwmGGNSEPETKFIQDMTEMN 391
Cdd:cd06247  144 WCS-IGAS----------RNCCSIIFCGT---------------------------------GPESEPETKAVADLIEKK 179

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663499727 392 DddgdgaSDFKVTLTWHSFSELVLWPWGHCTNCYTPDDEYLVYHGNVMGQM-----TDYAPMQSSE-LYPTTGDFCDWHY 465
Cdd:cd06247  180 K------SDILCYLTIHSYGQLILLPYGYTKEPSPNHEEMMEVGEKAAAALkekhgTSYRVGSSADiLYSNSGSSRDWAR 253

                        250       260
                 ....*....|....*....|....*
gi 663499727 466 GVHESYCYTIEI---GNAFHELPED 487
Cdd:cd06247  254 DIGIPFSYTFELrdtGTYGFVLPED 278
M14_CPB cd03871
Peptidase M14 carboxypeptidase subfamily A/B-like; Carboxypeptidase B subgroup; Peptidase M14 ...
 228-477 1.22e-08

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: 57.08  E-value: 1.22e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663499727 228 SEQFITDLINTREIYLIPMLNTDGNRYdreeycgetAWENcyRSGWRKNLRDNTvtgvtpipdvdeevDEGCDGVDLNRN 307
Cdd:cd03871   86 KEKIMTKLLDRLDFYILPVLNIDGYVY---------TWTK--NRMWRKTRSPNA--------------GSSCIGTDPNRN 140

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663499727 308 YQFEWGAPLGATGPlfpgmCyadganNDVYNGPvnyedndddglvnedhvdgkdddadgqvdedwmGGNSEPETKFIQDM 387
Cdd:cd03871  141 FNAGWCTVGASSNP-----C------SETYCGS---------------------------------APESEKETKALANF 176

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663499727 388 TEMNdddgdgASDFKVTLTWHSFSELVLWPWGHcTNCYTPDDEYL--VYHGNV------MGQMTDYAPMQSSeLYPTTGD 459
Cdd:cd03871  177 IRNN------LSSIKAYLTIHSYSQMLLYPYSY-TYKLAPNHEELnsIAKGAVkelsslYGTKYTYGPGATT-IYPAAGG 248

                        250
                 ....*....|....*...
gi 663499727 460 FCDWHYGVHESYCYTIEI 477
Cdd:cd03871  249 SDDWAYDQGIKYSFTFEL 266
M14-CPA-like cd06227
Peptidase M14 carboxypeptidase A-like domain; uncharacterized subfamily; A functionally ...
 228-485 4.34e-08

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: 54.20  E-value: 4.34e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663499727 228 SEQFITDLINTREIYLIPMLNTDGNRYDRE-EYCgetawencyrsgWRKNLRdntvtgvtpipdvdeevdegcdGVDLNR 306
Cdd:cd06227   40 LRELAREILDNVELKIIPNANPDGRRLVESgDYC------------WRGNEN----------------------GVDLNR 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663499727 307 NYQFEWGAplgatgplfpgmcYADGANNDVYNGPVNYedndddglvnedhvdgkdddadgqvdedwmggnSEPETKFIQD 386
Cdd:cd06227   86 NWGVDWGK-------------GEKGAPSEEYPGPKPF---------------------------------SEPETRALRD 119

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663499727 387 MTEmndddgdgASDFKVTLTWHSFSELVLWPWGHCTNCYTPDDEYLVY-HGNVMGQMT--DYAPMQSSEL--YPTTGDFC 461
Cdd:cd06227  120 LAL--------SFKPHAFVSVHSGMLAIYTPYAYSASVPRPNRAADMDdLLDVVAKAScgDCTVGSAGKLvgYLADGTAM 191

                        250       260
                 ....*....|....*....|....*
gi 663499727 462 DWHYGV-HESYCYTIEIGNAFHELP 485
Cdd:cd06227  192 DYMYGKlKVPYSFTFEIYGDSGKAR 216
M14_CPB2 cd06246
Peptidase M14 carboxypeptidase subfamily A/B-like; Carboxypeptidase B2 subgroup; Peptidase M14 ...
 229-477 1.41e-07

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: 53.66  E-value: 1.41e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663499727 229 EQFITDLINTREIYLIPMLNTDGNRYDreeycgetaWENcyRSGWRKNLRDNTvtgvtpipdvdeevDEGCDGVDLNRNY 308
Cdd:cd06246   87 IGQHTNLLNLVDFYVMPVVNVDGYDYS---------WKK--NRMWRKNRSKHA--------------NNRCIGTDLNRNF 141

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663499727 309 QFEWGAPLGATGPLFPGMCyadganndvyngpvnyedndddglvnedhvdgkdddadGQVDEdwmggnSEPETKFIQDMT 388
Cdd:cd06246  142 DAGWCGKGASSDSCSETYC--------------------------------------GPYPE------SEPEVKAVASFL 177

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663499727 389 EMNDDdgdgasDFKVTLTWHSFSELVLWPWGhCTNCYTPD-DEYLVYHGNVMGQM-----TDYAPMQSSE-LYPTTGDFC 461
Cdd:cd06246  178 RRHKD------TIKAYISMHSYSQMVLFPYS-YTRNKSKDhDELSLLAKEAVTAIrktsrNRYTYGPGAEtIYLAPGGSD 250

                        250
                 ....*....|....*.
gi 663499727 462 DWHYGVHESYCYTIEI 477
Cdd:cd06246  251 DWAYDLGIKYSFTFEL 266
M14_CP_bacteria cd18173
bacterial peptidase M14 carboxypeptidase, uncharacterized; This family contains only bacterial ...
 62-485 7.04e-07

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: 51.43  E-value: 7.04e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663499727  62 YHDYFSMKQRMQTLAAYYPDFLQYHEglLGGvnargdemTSEDYEGWFykhsspwMKITGNVqggdyndfNDDDgnyaDR 141
Cdd:cd18173    4 YPTYEEYEAMMQSFAANYPNICRLVS--IGT--------SVQGRKLLA-------LKISDNV--------NTEE----AE 54

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663499727 142 PDVMLVGNHHAREWMSYEVPMFFLETIAYYYGkagidndgdglvdedgwdgidndgdcsllnatnqdsngdgtpcgpgdl 221
Cdd:cd18173   55 PEFKYTSTMHGDETTGYELMLRLIDYLLTNYG------------------------------------------------ 86

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663499727 222 gvdedfSEQFITDLINTREIYLIPMLNTDGNrydreeycgetawencYRSGwrknlrDNTVTGVTpipdvdeevDEGCDG 301
Cdd:cd18173   87 ------TDPRITNLVDNTEIWINPLANPDGT----------------YAGG------NNTVSGAT---------RYNANG 129

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663499727 302 VDLNRNyqfewgaplgatgplFPgmcyadganndvyngpvnyedndddglvneDHVDGKDDDadgqvdedwmGGNSEPET 381
Cdd:cd18173  130 VDLNRN---------------FP------------------------------DPVDGDHPD----------GNGWQPET 154

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663499727 382 KFIQDMTEmndddgdgASDFKVTLTWHSFSELVLWPWGHCTNcYTPDDEYLVY-----------HGNVMGqMTDYAP--M 448
Cdd:cd18173  155 QAMMNFAD--------EHNFVLSANFHGGAEVVNYPWDTWYS-RHPDDDWFQDisreyadtnqaNSPPMY-MSEFNNgiT 224

                        410       420       430       440
                 ....*....|....*....|....*....|....*....|.
gi 663499727 449 QSSELYPTTGDFCDWHYGVHESYCYTIEIGN----AFHELP 485
Cdd:cd18173  225 NGYDWYEVYGGRQDYMYYWHGCREVTIELSNtkwpPASQLP 265
MpaA COG2866
Murein tripeptide amidase MpaA [Cell wall/membrane/envelope biogenesis];
139-312 6.60e-05

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


Pssm-ID: 442113 [Multi-domain]  Cd Length: 337  Bit Score: 45.84  E-value: 6.60e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663499727 139 ADRPDVMLVGNHHAREWMSYEVPMFFLETIAYYYGKAgidndgdglvdedgwdgidndgdcsllnatnqdsngdgtpcgp 218
Cdd:COG2866   63 EGKPKVLLNAQQHGNEWTGTEALLGLLEDLLDNYDPL------------------------------------------- 99

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663499727 219 gdlgvdedfseqfITDLINTREIYLIPMLNTDGnrYDReeycgetawencyrsGWRKNLRdntvtgvtpipdvdeevdeg 298
Cdd:COG2866  100 -------------IRALLDNVTLYIVPMLNPDG--AER---------------NTRTNAN-------------------- 129

                        170
                 ....*....|....
gi 663499727 299 cdGVDLNRNYQFEW 312
Cdd:COG2866  130 --GVDLNRDWPAPW 141
Peptidases_S8_Subtilisin_like cd07473
Peptidase S8 family domain in Subtilisin-like proteins; This family is a member of the ...
 176-216 3.69e-03

Peptidase S8 family domain in Subtilisin-like proteins; This family is a member of the Peptidases S8 or Subtilases serine endo- and exo-peptidase clan. They have an Asp/His/Ser catalytic triad similar to that found in trypsin-like proteases, but do not share their three-dimensional structure and are not homologous to trypsin. The stability of subtilases may be enhanced by calcium, some members have been shown to bind up to 4 ions via binding sites with different affinity. Some members of this clan contain disulfide bonds. These enzymes can be intra- and extracellular, some function at extreme temperatures and pH values.


Pssm-ID: 173799 [Multi-domain]  Cd Length: 259  Bit Score: 39.87  E-value: 3.69e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 663499727 176 GIDNDGDGLVDED-GWDGIDNDGDcsllnatNQDSNGDGTPC 216
Cdd:cd07473   35 GIDDDGNGYVDDIyGWNFVNNDND-------PMDDNGHGTHV 69
 
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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