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Conserved domains on  [gi|4503011|ref|NP_001299|]
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carboxypeptidase N catalytic chain precursor [Homo sapiens]

Protein Classification

M14 family carboxypeptidase N/E( domain architecture ID 10133693)

M14 family zinc carboxypeptidase N/E relies on its substrate specificity and subcellular compartmentalization to prevent inappropriate cleavages that would otherwise damage the cell; it contains an extra C-terminal domain which may assist in folding of the carboxypeptidase domain, regulate enzyme activity, or be involved in interactions with other proteins or with membranes

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
M14_CPN cd03864
Peptidase M14 carboxypeptidase subfamily N/E-like; Carboxypeptidase N subgroup; Peptidase M14 ...
25-337 0e+00

Peptidase M14 carboxypeptidase subfamily N/E-like; Carboxypeptidase N subgroup; Peptidase M14 Carboxypeptidase N (CPN, also known as kininase I, creatine kinase conversion factor, plasma carboxypeptidase B, arginine carboxypeptidase, and protaminase; EC 3.4.17.3) is an extracellular glycoprotein synthesized in the liver and released into the blood, where it is present in high concentrations. CPN belongs to the N/E subfamily 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. CPN plays an important role in protecting the body from excessive buildup of potentially deleterious peptides that normally act as local autocrine or paracrine hormones. It specifically removes C-terminal basic residues. As CPN can cleave lysine more avidly than arginine residues it is also called lysine carboxypeptidase. CPN substrates include peptides found in the bloodstream, such as kinins (e.g. bradykinin, kalinin, met-lys-bradykinin), complement anaphylatoxins and creatine kinase MM (CK-MM). By removing just one amino acid, CPN can alter peptide activity and receptor binding. For example Bradykinin, a nine-residue peptide released from kiningen in response to tissue injury which is inactivated by CPN, anaphylatoxins which are regulated by CPN by the cleaving and removal of their C-terminal arginines resulting in a reduction in their biological activities of 10-100-fold, and creatine kinase MM, a cytosolic enzyme that catalyzes the reversible transfer of a phosphate group from ATP to creatine, and is regulated by CPN by the cleavage of C-terminal lysines. Like the other N/E subfamily members, two surface loops surrounding the active-site groove restrict access to the catalytic center, thus restricting larger protein carboxypeptidase inhibitors from inhibiting CPN.


:

Pssm-ID: 349436 [Multi-domain]  Cd Length: 313  Bit Score: 692.83  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503011   25 HHRYDDLVRTLYKVQNECPGITRVYSIGRSVEGRHLYVLEFSDHPGIHEPLEPEVKYVGNMHGNEALGRELMLQLSEFLC 104
Cdd:cd03864   1 HHRYDDLVRALYAVQNECPYITRIYSIGRSVEGRHLYVLEFSDNPGIHEPLEPEFKYVGNMHGNEVLGRELLIQLSEFLC 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503011  105 EEFRNRNQRIVQLIQDTRIHILPSMNPDGYEVAAAQGPNKPGYLVGRNNANGVDLNRNFPDLNTYIYYNEKYGGPNHHLP 184
Cdd:cd03864  81 EEYRNGNERITRLIQDTRIHILPSMNPDGYEVAARQGPEFNGYLVGRNNANGVDLNRNFPDLNTLMYYNEKYGGPNHHLP 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503011  185 LPDNWKSQVEPETRAVIRWMHSFNFVLSANLHGGAVVANYPYDKSFEHRVRGVRRTASTPTPDDKLFQKLAKVYSYAHGW 264
Cdd:cd03864 161 LPDNWKSQVEPETLAVIQWMQNYNFVLSANLHGGAVVANYPYDKSREPRVRGFRRTAYSPTPDDKLFQKLAKTYSYAHGW 240
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 4503011  265 MFQGWNCGDYFPDGITNGASWYSLSKGMQDFNYLHTNCFEITLELSCDKFPPEEELQREWLGNREALIQFLEQ 337
Cdd:cd03864 241 MHKGWNCGDYFDEGITNGASWYSLSKGMQDFNYLHTNCFEITLELSCDKFPPEEELEREWLGNREALISYMEQ 313
Peptidase_M14NE-CP-C_like cd11308
Peptidase associated domain: C-terminal domain of M14 N/E carboxypeptidase; putative folding, ...
341-415 7.47e-34

Peptidase associated domain: C-terminal domain of M14 N/E carboxypeptidase; putative folding, regulation, or interaction domain; This domain is found C-terminal to the M14 carboxypeptidase (CP) N/E subfamily containing zinc-binding enzymes that 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 enzymatically active members (carboxypeptidase N, E, M, D, and Z), as well as non-active members (carboxypeptidase-like protein 1, -2, aortic CP-like protein, and adipocyte enhancer binding protein-1) which lack the critical active site and substrate-binding residues considered necessary for activity. 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. For M14 CPs, it has been suggested that this domain may assist in folding of the CP domain, regulate enzyme activity, or be involved in interactions with other proteins or with membranes; for carboxypeptidase M, it may interact with the bradykinin 1 receptor at the cell surface. This domain may also be found in other peptidase families.


:

Pssm-ID: 200604 [Multi-domain]  Cd Length: 76  Bit Score: 121.86  E-value: 7.47e-34
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 4503011  341 GIKGMVLDENYNNLANAVISVSGINHDVTSGDHGDYFRLLLPGIYTVSATAPGYDPETVTVTVGP-AEPTLVNFHL 415
Cdd:cd11308   1 GIKGFVTDATGNPIANATISVEGINHDVTTAKDGDYWRLLLPGTYNVTASAPGYQPVTKTVTVPNnFSATVVNFTL 76
 
Name Accession Description Interval E-value
M14_CPN cd03864
Peptidase M14 carboxypeptidase subfamily N/E-like; Carboxypeptidase N subgroup; Peptidase M14 ...
25-337 0e+00

Peptidase M14 carboxypeptidase subfamily N/E-like; Carboxypeptidase N subgroup; Peptidase M14 Carboxypeptidase N (CPN, also known as kininase I, creatine kinase conversion factor, plasma carboxypeptidase B, arginine carboxypeptidase, and protaminase; EC 3.4.17.3) is an extracellular glycoprotein synthesized in the liver and released into the blood, where it is present in high concentrations. CPN belongs to the N/E subfamily 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. CPN plays an important role in protecting the body from excessive buildup of potentially deleterious peptides that normally act as local autocrine or paracrine hormones. It specifically removes C-terminal basic residues. As CPN can cleave lysine more avidly than arginine residues it is also called lysine carboxypeptidase. CPN substrates include peptides found in the bloodstream, such as kinins (e.g. bradykinin, kalinin, met-lys-bradykinin), complement anaphylatoxins and creatine kinase MM (CK-MM). By removing just one amino acid, CPN can alter peptide activity and receptor binding. For example Bradykinin, a nine-residue peptide released from kiningen in response to tissue injury which is inactivated by CPN, anaphylatoxins which are regulated by CPN by the cleaving and removal of their C-terminal arginines resulting in a reduction in their biological activities of 10-100-fold, and creatine kinase MM, a cytosolic enzyme that catalyzes the reversible transfer of a phosphate group from ATP to creatine, and is regulated by CPN by the cleavage of C-terminal lysines. Like the other N/E subfamily members, two surface loops surrounding the active-site groove restrict access to the catalytic center, thus restricting larger protein carboxypeptidase inhibitors from inhibiting CPN.


Pssm-ID: 349436 [Multi-domain]  Cd Length: 313  Bit Score: 692.83  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503011   25 HHRYDDLVRTLYKVQNECPGITRVYSIGRSVEGRHLYVLEFSDHPGIHEPLEPEVKYVGNMHGNEALGRELMLQLSEFLC 104
Cdd:cd03864   1 HHRYDDLVRALYAVQNECPYITRIYSIGRSVEGRHLYVLEFSDNPGIHEPLEPEFKYVGNMHGNEVLGRELLIQLSEFLC 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503011  105 EEFRNRNQRIVQLIQDTRIHILPSMNPDGYEVAAAQGPNKPGYLVGRNNANGVDLNRNFPDLNTYIYYNEKYGGPNHHLP 184
Cdd:cd03864  81 EEYRNGNERITRLIQDTRIHILPSMNPDGYEVAARQGPEFNGYLVGRNNANGVDLNRNFPDLNTLMYYNEKYGGPNHHLP 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503011  185 LPDNWKSQVEPETRAVIRWMHSFNFVLSANLHGGAVVANYPYDKSFEHRVRGVRRTASTPTPDDKLFQKLAKVYSYAHGW 264
Cdd:cd03864 161 LPDNWKSQVEPETLAVIQWMQNYNFVLSANLHGGAVVANYPYDKSREPRVRGFRRTAYSPTPDDKLFQKLAKTYSYAHGW 240
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 4503011  265 MFQGWNCGDYFPDGITNGASWYSLSKGMQDFNYLHTNCFEITLELSCDKFPPEEELQREWLGNREALIQFLEQ 337
Cdd:cd03864 241 MHKGWNCGDYFDEGITNGASWYSLSKGMQDFNYLHTNCFEITLELSCDKFPPEEELEREWLGNREALISYMEQ 313
Peptidase_M14 pfam00246
Zinc carboxypeptidase;
31-330 1.58e-98

Zinc carboxypeptidase;


Pssm-ID: 459730 [Multi-domain]  Cd Length: 287  Bit Score: 297.29  E-value: 1.58e-98
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503011     31 LVRTLYKVQNECPGITRVYSIGRSVEGRHLYVLEFSDHPGIHEPLEPEVKYVGNMHGNEALGRELMLQLSEFLCEEFrNR 110
Cdd:pfam00246   1 IEAWLDALAARYPDLVRLVSIGKSVEGRPLKVLKISSGPGEHNPGKPAVFIDGGIHAREWIGPATALYLIHQLLTNY-GR 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503011    111 NQRIVQLIQDTRIHILPSMNPDGYEVAAAQgpnKPGYLVGRNNAN-----GVDLNRNFPDL-----NTYIYYNEKYGGPN 180
Cdd:pfam00246  80 DPEITELLDDTDIYILPVVNPDGYEYTHTT---DRLWRKNRSNANgssciGVDLNRNFPDHwnevgASSNPCSETYRGPA 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503011    181 HHLplpdnwksqvEPETRAVIRWMHSF-NFVLSANLHGGAVVANYPYDKsfehrvrgvrrTASTPTPDDKLFQKLAKVYS 259
Cdd:pfam00246 157 PFS----------EPETRAVADFIRSKkPFVLYISLHSYSQVLLYPYGY-----------TRDEPPPDDEELKSLARAAA 215
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 4503011    260 YAHGWMFQGWncgdYFPDGITNGASWYSLSKGMQDFNYLHTNC-FEITLELSCDK----FPPEEELQREWLGNREA 330
Cdd:pfam00246 216 KALQKMVRGT----SYTYGITNGATIYPASGGSDDWAYGRLGIkYSYTIELRDTGrygfLLPASQIIPTAEETWEA 287
Zn_pept smart00631
Zn_pept domain;
25-323 5.33e-92

Zn_pept domain;


Pssm-ID: 214748 [Multi-domain]  Cd Length: 277  Bit Score: 279.99  E-value: 5.33e-92
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503011      25 HHRYDDLVRTLYKVQNECPGITRVYSIGRSVEGRHLYVLEFSDHPGihePLEPEVKYVGNMHGNEALGRELMLQLSEFLC 104
Cdd:smart00631   1 YHSYEEIEAWLKELAARYPDLVRLVSIGKSVEGRPIWVLKISNGGS---HDKPAIFIDAGIHAREWIGPATALYLINQLL 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503011     105 EEFRnRNQRIVQLIQDTRIHILPSMNPDGYEVAAAqgpNKPGYLVGRN---NANGVDLNRNFPDLNTYIYY--NEKYGGP 179
Cdd:smart00631  78 ENYG-RDPRVTNLLDKTDIYIVPVLNPDGYEYTHT---GDRLWRKNRSpnsNCRGVDLNRNFPFHWGETGNpcSETYAGP 153
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503011     180 nhhlplpdnwKSQVEPETRAVIRWMHSF-NFVLSANLHGGAVVANYPYDKSFEHRVRGVRRtastptpDDKLFQKLAKVY 258
Cdd:smart00631 154 ----------SPFSEPETKAVRDFIRSNrRFKLYIDLHSYSQLILYPYGYTKNDLPPNVDD-------LDAVAKALAKAL 216
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 4503011     259 SYAHGWmfqgwncgdYFPDGITNGASWYSlSKGMQDFNYLHTN-CFEITLELSCD-----KFPPEEELQRE 323
Cdd:smart00631 217 ASVHGT---------RYTYGISNGAIYPA-SGGSDDWAYGVLGiPFSFTLELRDDgrygfLLPPSQIIPTG 277
MpaA COG2866
Murein tripeptide amidase MpaA [Cell wall/membrane/envelope biogenesis];
24-227 3.91e-35

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


Pssm-ID: 442113 [Multi-domain]  Cd Length: 337  Bit Score: 133.28  E-value: 3.91e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503011   24 RHHRYDDLVRTLYKVQnECPGITRVYSIGRSVEGRHLYVLEFSDHpgihEPLEPEVKYVGNMHGNEALGRELMLQLSEFL 103
Cdd:COG2866  18 RYYTYEELLALLAKLA-AASPLVELESIGKSVEGRPIYLLKIGDP----AEGKPKVLLNAQQHGNEWTGTEALLGLLEDL 92
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503011  104 CEefrNRNQRIVQLIQDTRIHILPSMNPDGYEVAaaqgpnkpgylvGRNNANGVDLNRNFPDLntyiyynekyggpnhhl 183
Cdd:COG2866  93 LD---NYDPLIRALLDNVTLYIVPMLNPDGAERN------------TRTNANGVDLNRDWPAP----------------- 140
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....
gi 4503011  184 plpdnWKSQvePETRAVIRWMHSFNFVLSANLHGGAVVANYPYD 227
Cdd:COG2866 141 -----WLSE--PETRALRDLLDEHDPDFVLDLHGQGELFYWFVG 177
Peptidase_M14NE-CP-C_like cd11308
Peptidase associated domain: C-terminal domain of M14 N/E carboxypeptidase; putative folding, ...
341-415 7.47e-34

Peptidase associated domain: C-terminal domain of M14 N/E carboxypeptidase; putative folding, regulation, or interaction domain; This domain is found C-terminal to the M14 carboxypeptidase (CP) N/E subfamily containing zinc-binding enzymes that 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 enzymatically active members (carboxypeptidase N, E, M, D, and Z), as well as non-active members (carboxypeptidase-like protein 1, -2, aortic CP-like protein, and adipocyte enhancer binding protein-1) which lack the critical active site and substrate-binding residues considered necessary for activity. 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. For M14 CPs, it has been suggested that this domain may assist in folding of the CP domain, regulate enzyme activity, or be involved in interactions with other proteins or with membranes; for carboxypeptidase M, it may interact with the bradykinin 1 receptor at the cell surface. This domain may also be found in other peptidase families.


Pssm-ID: 200604 [Multi-domain]  Cd Length: 76  Bit Score: 121.86  E-value: 7.47e-34
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 4503011  341 GIKGMVLDENYNNLANAVISVSGINHDVTSGDHGDYFRLLLPGIYTVSATAPGYDPETVTVTVGP-AEPTLVNFHL 415
Cdd:cd11308   1 GIKGFVTDATGNPIANATISVEGINHDVTTAKDGDYWRLLLPGTYNVTASAPGYQPVTKTVTVPNnFSATVVNFTL 76
CarboxypepD_reg pfam13620
Carboxypeptidase regulatory-like domain;
341-415 9.73e-15

Carboxypeptidase regulatory-like domain;


Pssm-ID: 433354 [Multi-domain]  Cd Length: 81  Bit Score: 69.23  E-value: 9.73e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503011    341 GIKGMVLDENYNNLANAVISV----SGINHDVTSGDHGDY-FRLLLPGIYTVSATAPGYDPETVT-VTVGPAEPTLVNFH 414
Cdd:pfam13620   1 TISGTVTDPSGAPVPGATVTVtntdTGTVRTTTTDADGRYrFPGLPPGTYTVTVSAPGFKTATRTgVTVTAGQTTTLDVT 80

                  .
gi 4503011    415 L 415
Cdd:pfam13620  81 L 81
PRK10602 PRK10602
murein tripeptide amidase MpaA;
122-212 1.74e-07

murein tripeptide amidase MpaA;


Pssm-ID: 182582  Cd Length: 237  Bit Score: 51.95  E-value: 1.74e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503011   122 RIHILPSMNPDGyevaaAQgpnkpgyLVGRNNANGVDLNRNFPDLN-----TYIYYNEKygGPNHHLPLPDNWKSQVEPE 196
Cdd:PRK10602  72 RHHVVLAVNPDG-----CQ-------LGLRANANGVDLNRNFPAANwkegeTVYRWNSA--AEERDVVLLTGDKPGSEPE 137
                         90
                 ....*....|....*...
gi 4503011   197 TRAVIRWMHSFN--FVLS 212
Cdd:PRK10602 138 TQALCQLIHRLQpaWVVS 155
ClfA COG4932
Clumping factor A-related surface protein, MSCRAMM (microbial surface components recognizing ...
341-412 2.02e-03

Clumping factor A-related surface protein, MSCRAMM (microbial surface components recognizing adhesive matrix molecules) family, DEv-IgG fold [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 443959 [Multi-domain]  Cd Length: 689  Bit Score: 40.73  E-value: 2.02e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503011  341 GIKGMVLDEN--YNNLANAVISVSGIN----HDVTSGDHGDY-FRLLLPGIYTVSAT-AP-GY--DPETVTVTVGPAEPT 409
Cdd:COG4932 359 SVTLTKVDADdgEAPLAGAEFTLTDADgtvvATITTDADGTAsFKGLAPGTYTLTETkAPeGYtlDSTPITVTVTDGGTG 438

                ...
gi 4503011  410 LVN 412
Cdd:COG4932 439 AID 441
 
Name Accession Description Interval E-value
M14_CPN cd03864
Peptidase M14 carboxypeptidase subfamily N/E-like; Carboxypeptidase N subgroup; Peptidase M14 ...
25-337 0e+00

Peptidase M14 carboxypeptidase subfamily N/E-like; Carboxypeptidase N subgroup; Peptidase M14 Carboxypeptidase N (CPN, also known as kininase I, creatine kinase conversion factor, plasma carboxypeptidase B, arginine carboxypeptidase, and protaminase; EC 3.4.17.3) is an extracellular glycoprotein synthesized in the liver and released into the blood, where it is present in high concentrations. CPN belongs to the N/E subfamily 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. CPN plays an important role in protecting the body from excessive buildup of potentially deleterious peptides that normally act as local autocrine or paracrine hormones. It specifically removes C-terminal basic residues. As CPN can cleave lysine more avidly than arginine residues it is also called lysine carboxypeptidase. CPN substrates include peptides found in the bloodstream, such as kinins (e.g. bradykinin, kalinin, met-lys-bradykinin), complement anaphylatoxins and creatine kinase MM (CK-MM). By removing just one amino acid, CPN can alter peptide activity and receptor binding. For example Bradykinin, a nine-residue peptide released from kiningen in response to tissue injury which is inactivated by CPN, anaphylatoxins which are regulated by CPN by the cleaving and removal of their C-terminal arginines resulting in a reduction in their biological activities of 10-100-fold, and creatine kinase MM, a cytosolic enzyme that catalyzes the reversible transfer of a phosphate group from ATP to creatine, and is regulated by CPN by the cleavage of C-terminal lysines. Like the other N/E subfamily members, two surface loops surrounding the active-site groove restrict access to the catalytic center, thus restricting larger protein carboxypeptidase inhibitors from inhibiting CPN.


Pssm-ID: 349436 [Multi-domain]  Cd Length: 313  Bit Score: 692.83  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503011   25 HHRYDDLVRTLYKVQNECPGITRVYSIGRSVEGRHLYVLEFSDHPGIHEPLEPEVKYVGNMHGNEALGRELMLQLSEFLC 104
Cdd:cd03864   1 HHRYDDLVRALYAVQNECPYITRIYSIGRSVEGRHLYVLEFSDNPGIHEPLEPEFKYVGNMHGNEVLGRELLIQLSEFLC 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503011  105 EEFRNRNQRIVQLIQDTRIHILPSMNPDGYEVAAAQGPNKPGYLVGRNNANGVDLNRNFPDLNTYIYYNEKYGGPNHHLP 184
Cdd:cd03864  81 EEYRNGNERITRLIQDTRIHILPSMNPDGYEVAARQGPEFNGYLVGRNNANGVDLNRNFPDLNTLMYYNEKYGGPNHHLP 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503011  185 LPDNWKSQVEPETRAVIRWMHSFNFVLSANLHGGAVVANYPYDKSFEHRVRGVRRTASTPTPDDKLFQKLAKVYSYAHGW 264
Cdd:cd03864 161 LPDNWKSQVEPETLAVIQWMQNYNFVLSANLHGGAVVANYPYDKSREPRVRGFRRTAYSPTPDDKLFQKLAKTYSYAHGW 240
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 4503011  265 MFQGWNCGDYFPDGITNGASWYSLSKGMQDFNYLHTNCFEITLELSCDKFPPEEELQREWLGNREALIQFLEQ 337
Cdd:cd03864 241 MHKGWNCGDYFDEGITNGASWYSLSKGMQDFNYLHTNCFEITLELSCDKFPPEEELEREWLGNREALISYMEQ 313
M14_CP_N-E_like cd03858
Peptidase M14 carboxypeptidase subfamily N/E-like; Carboxypeptidase (CP) N/E-like subfamily of ...
25-337 1.21e-180

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: 506.03  E-value: 1.21e-180
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503011   25 HHRYDDLVRTLYKVQNECPGITRVYSIGRSVEGRHLYVLEFSDHPGIHEPLEPEVKYVGNMHGNEALGRELMLQLSEFLC 104
Cdd:cd03858   1 HHNYEELEEFLKQVAKRYPNITRLYSIGKSVEGRELWVLEISDNPGVHEPGEPEFKYVANMHGNEVVGRELLLLLAEYLC 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503011  105 EEFrNRNQRIVQLIQDTRIHILPSMNPDGYEVAAAQGpnkPGYLVGRNNANGVDLNRNFPDLNTYIYYnekyggpnhhlp 184
Cdd:cd03858  81 ENY-GKDPRVTQLVNSTRIHIMPSMNPDGYEKAQEGD---CGGLIGRNNANGVDLNRNFPDQFFQVYS------------ 144
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503011  185 lpdnWKSQVEPETRAVIRWMHSFNFVLSANLHGGAVVANYPYDKSFEHrvrgvRRTASTPTPDDKLFQKLAKVYSYAHGW 264
Cdd:cd03858 145 ----DNNPRQPETKAVMNWLESIPFVLSANLHGGALVANYPYDDTRSG-----KSTEYSPSPDDAVFRMLARSYSDAHPT 215
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 4503011  265 MFQGWNC----GDYFPDGITNGASWYSLSKGMQDFNYLHTNCFEITLELSCDKFPPEEELQREWLGNREALIQFLEQ 337
Cdd:cd03858 216 MSMGKPCccddDENFPNGITNGAAWYSVSGGMQDFNYLHTNCFEITLELGCCKYPPASELPKYWEDNKRSLLNFLEQ 292
M14_CPD_I cd03868
Peptidase M14 carboxypeptidase subfamily N/E-like; Carboxypeptidase D, domain I subgroup; The ...
26-337 1.12e-143

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: 412.41  E-value: 1.12e-143
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503011   26 HRYDDLVRTLYKVQNECPGITRVYSIGRSVEGRHLYVLEFSDHPGIHEPLEPEVKYVGNMHGNEALGRELMLQLSEFLCE 105
Cdd:cd03868   2 HNYDELTDLLHKLAETYPNIAKLHSIGKSVQGRELWVLEISDNVNRREPGKPMFKYVANMHGDETVGRQLLIYLAQYLLE 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503011  106 EFrNRNQRIVQLIQDTRIHILPSMNPDGYEVAAAQGPNKPGYLVGRNNANGVDLNRNFPDlntyiyyneKYGGPNHHLpl 185
Cdd:cd03868  82 NY-GKDERVTRLVNSTDIHLMPSMNPDGFENSKEGDCSGDPGYGGRENANNVDLNRNFPD---------QFEDSDDRL-- 149
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503011  186 pdnwKSQVEPETRAVIRWMHSFNFVLSANLHGGAVVANYPYDKSFEHRVRGVRrtasTPTPDDKLFQKLAKVYSYAHGWM 265
Cdd:cd03868 150 ----LEGRQPETLAMMKWIVENPFVLSANLHGGSVVASYPFDDSPSHIECGVY----SKSPDDAVFRHLAHTYADNHPTM 221
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 4503011  266 FQGWNC-GDYFPDGITNGASWYSLSKGMQDFNYLHTNCFEITLELSCDKFPPEEELQREWLGNREALIQFLEQ 337
Cdd:cd03868 222 HKGNNCcEDSFKDGITNGAEWYDVPGGMQDFNYVHSNCFEITLELSCCKYPPASELPKEWDNNKEALLSYMEQ 294
M14_CPE cd03865
Peptidase M14 carboxypeptidase subfamily N/E-like; Carboxypeptidase E subgroup; Peptidase M14 ...
25-337 7.28e-135

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: 390.88  E-value: 7.28e-135
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503011   25 HHRYDDLVRTLYKVQNECPGITRVYSIGRSVEGRHLYVLEFSDHPGIHEPLEPEVKYVGNMHGNEALGRELMLQLSEFLC 104
Cdd:cd03865   1 YHRYPELREALVSVWLQCPAISRIYTVGRSFEGRELLVIEVSDNPGEHEPGEPEFKYVGNMHGNEAVGRELLIFLAQYLC 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503011  105 EEFRNRNQRIVQLIQDTRIHILPSMNPDGYEVAAAQGPNKPGYLVGRNNANGVDLNRNFPDLNTYIYYNEKYGGPNHHlp 184
Cdd:cd03865  81 NEYQKGNETIINLIHSTRIHIMPSLNPDGFEKAASQPGELKDWFVGRSNAQGIDLNRNFPDLDRIVYVNEKEGGPNNH-- 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503011  185 LPDNWKSQVE------PETRAVIRWMHSFNFVLSANLHGGAVVANYPYDKSfehrvrgvrRTAST----PTPDDKLFQKL 254
Cdd:cd03865 159 LLKNMKKAVDqntklaPETKAVIHWIMDIPFVLSANLHGGDLVANYPYDET---------RSGSAheysSCPDDAIFQSL 229
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503011  255 AKVYSYAHGWMF-------QGWNCGDYFPDGITNGASWYSLSKGMQDFNYLHTNCFEITLELSCDKFPPEEELQREWLGN 327
Cdd:cd03865 230 ARAYSSLNPAMSdpnrppcRKNDDDSSFVDGTTNGGAWYSVPGGMQDFNYLSSNCFEITVELSCEKFPPEETLKGYWEDN 309
                       330
                ....*....|
gi 4503011  328 REALIQFLEQ 337
Cdd:cd03865 310 KNSLINYIEQ 319
M14_CPZ cd03867
Peptidase M14 carboxypeptidase subfamily N/E-like; Carboxypeptidase Z subgroup; Peptidase ...
25-336 2.43e-129

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: 376.92  E-value: 2.43e-129
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503011   25 HHRYDDLVRTLYKVQNECPGITRVYSIGRSVEGRHLYVLEFSDHPGIHEPLEPEVKYVGNMHGNEALGRELMLQLSEFLC 104
Cdd:cd03867   1 HHSYSQMVRVLKKTAARCAHIARTYSIGRSFEGKDLLVIEFSSNPGQHELLEPEVKYIGNMHGNEVVGREMLIYLAQYLC 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503011  105 EEFRNRNQRIVQLIQDTRIHILPSMNPDGYEVAAAQGPNKPGYLVGRNNANGVDLNRNFPDLnTYIYYN--EKYGGPNHH 182
Cdd:cd03867  81 SEYLLGNPRIQTLINTTRIHLLPSMNPDGYEVAAEEGAGYNGWTSGRQNAQNLDLNRNFPDL-TSEAYRlaRTRGARLDH 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503011  183 LPLPDN-WKSQVEPETRAVIRWMHSFNFVLSANLHGGAVVANYPYDKSfEHRvrgVRRTASTPTPDDKLFQKLAKVYSYA 261
Cdd:cd03867 160 IPIPQSyWWGKVAPETKAVMKWMRSIPFVLSASLHGGDLVVSYPYDFS-KHP---LEEKMFSPTPDEKMFKLLAKAYADA 235
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 4503011  262 HGWM-FQGWN-CGDYFPD--GITNGASWYSLSKGMQDFNYLHTNCFEITLELSCDKFPPEEELQREWLGNREALIQFLE 336
Cdd:cd03867 236 HPMMsDRSENrCGGNFLKrgGIINGAEWYSFTGGMADFNYLHTNCFEVTVELGCEKFPPEEELYTIWQENKEALLNFME 314
M14_CPX_like cd03869
Peptidase M14 carboxypeptidase subfamily N/E-like; Carboxypeptidase X subgroup; Peptidase ...
25-337 1.14e-126

Peptidase M14 carboxypeptidase subfamily N/E-like; Carboxypeptidase X subgroup; Peptidase M14-like domain of carboxypeptidase (CP)-like protein X (CPX), CPX forms a distinct subgroup of 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. Proteins belonging to this subgroup include CP-like protein X1 (CPX1), CP-like protein X2 (CPX2), and aortic CP-like protein (ACLP) and its isoform adipocyte enhancer binding protein-1 (AEBP1). AEBP1 is a truncated form of ACLP, which may arise from alternative splicing of the gene. These proteins are inactive towards standard CP substrates because they lack one or more critical active site and substrate-binding residues that are necessary for activity. They may function as binding proteins rather than as active CPs or display catalytic activity toward other substrates. Proteins in this subgroup also contain an N-terminal discoidin domain. The CP domain is important for the function of AEBP1 as a transcriptional repressor. AEBP1 is involved in several biological processes including adipogenesis, macrophage cholesterol homeostasis, and inflammation. In macrophages, AEBP1 promotes the expression of IL-6, TNF-alpha, MCP-1, and iNOS whose expression is tightly regulated by NF-kappaB activity. ACLP, a secreted protein that associates with the extracellular matrix, is essential for abdominal wall development and contributes to dermal wound healing.


Pssm-ID: 349441  Cd Length: 322  Bit Score: 370.32  E-value: 1.14e-126
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503011   25 HHRYDDLVRTLYKVQNECPGITRVYSIGRSVEGRHLYVLEFSDHPGIHEPLEPEVKYVGNMHGNEALGRELMLQLSEFLC 104
Cdd:cd03869   1 HHNYKDMRQLMKVVNEMCPNITRIYNIGKSYQGLKLYAMEISDNPGEHEVGEPEFRYVAGAHGNEVLGRELLLLLMQFLC 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503011  105 EEFRNRNQRIVQLIQDTRIHILPSMNPDGYEVAAAQGPNKPGYLVGRNNANGVDLNRNFPDLNTYIYYNEKYGG-----P 179
Cdd:cd03869  81 QEYLAGNPRIRHLVEETRIHLLPSVNPDGYEKAYEAGSELGGWSLGRWTSDGIDINHNFPDLNSLLWEAEDRKWvprkvP 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503011  180 NHHLPLPDNWKSQ---VEPETRAVIRWMHSFNFVLSANLHGGAVVANYPYDKSfehRVRGVRRTAsTPTPDDKLFQKLAK 256
Cdd:cd03869 161 NHHIPIPEWYLSEnatVAPETRAVIAWMEKIPFVLGGNLQGGELVVSYPYDMT---RTPWKTQEY-TPTPDDHVFRWLAY 236
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503011  257 VYSYAHGWMFQGWNCGDYFPD-----GITNGASWYSLSKGMQDFNYLHTNCFEITLELSCDKFPPEEELQREWLGNREAL 331
Cdd:cd03869 237 SYASTHRLMTDASRRPCHTEDfqkedGTVNGASWHTVAGSMNDFSYLHTNCFELSIYLGCDKFPHESELPEEWENNRESL 316

                ....*.
gi 4503011  332 IQFLEQ 337
Cdd:cd03869 317 LVFMEQ 322
M14_CPD_II cd03863
Peptidase M14 carboxypeptidase subfamily N/E-like; Carboxypeptidase D, domain II subgroup; The ...
20-337 1.36e-121

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: 356.56  E-value: 1.36e-121
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503011   20 PVTFRHHRYDDLVRTLYKVQNECPGITRVYSIGRSVEGRHLYVLEFSDHPGIHEPLEPEVKYVGNMHGNEALGRELMLQL 99
Cdd:cd03863   3 PVDFRHHHFSDMEIFLRRYANEYPSITRLYSVGKSVELRELYVMEISDNPGVHEPGEPEFKYIGNMHGNEVVGRELLLNL 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503011  100 SEFLCEEFrNRNQRIVQLIQDTRIHILPSMNPDGYEVaaAQGPNKPGyLVGRNNANGVDLNRNFPDLNTYIyynekyggp 179
Cdd:cd03863  83 IEYLCKNF-GTDPEVTDLVQNTRIHIMPSMNPDGYEK--SQEGDRGG-TVGRNNSNNYDLNRNFPDQFFQI--------- 149
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503011  180 nhhlplpdnwKSQVEPETRAVIRWMHSFNFVLSANLHGGAVVANYPYDKSFEhrvrGVrrTASTPTPDDKLFQKLAKVYS 259
Cdd:cd03863 150 ----------TDPPQPETLAVMSWLKTYPFVLSANLHGGSLVVNYPFDDDEQ----GL--ATYSKSPDDAVFQQLALSYS 213
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503011  260 YAHGWMFQGWNCGD-----YFPDGITNGASWYSLSKGMQDFNYLHTNCFEITLELSCDKFPPEEELQREWLGNREALIQF 334
Cdd:cd03863 214 KENSKMYQGSPCKElypneYFPHGITNGAQWYNVPGGMQDWNYLNTNCFEVTIELGCVKYPKAEELPKYWEQNRRSLLQF 293

                ...
gi 4503011  335 LEQ 337
Cdd:cd03863 294 IKQ 296
M14_CPM cd03866
Peptidase M14 carboxypeptidase subfamily N/E-like; Carboxypeptidase M subgroup; Peptidase M14 ...
25-337 2.25e-107

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: 319.82  E-value: 2.25e-107
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503011   25 HHRYDDLVRTLYKVQNECPGITRVYSIGRSVEGRHLYVLEFSDHPGIHEPLEPEVKYVGNMHGNEALGRELMLQLSEFLC 104
Cdd:cd03866   1 YHNQEQMETYLKDVNKNYPSITHLHSIGKSVEGRDLWVLVLGRFPTKHRIGIPEFKYVANMHGDEVVGRELLLHLIEFLV 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503011  105 EEFRNrNQRIVQLIQDTRIHILPSMNPDGYEvaAAQGPNkPGYLVGRNNANGVDLNRNFPDLNTYiyynekyggpnhhlp 184
Cdd:cd03866  81 TSYGS-DPVITRLINSTRIHIMPSMNPDGFE--ATKKPD-CYYTKGRYNKNGYDLNRNFPDAFEE--------------- 141
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503011  185 lpdNWkSQVEPETRAVIRWMHSFNFVLSANLHGGAVVANYPYDKSFEHRVRGVRRTAstpTPDDKLFQKLAKVYSYAHGW 264
Cdd:cd03866 142 ---NN-VQRQPETRAVMDWIKNETFVLSANLHGGALVASYPFDNGNSGTGQLGYYSV---SPDDDVFIYLAKTYSYNHTN 214
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 4503011  265 MFQGWNCGDY--FPDGITNGASWYSLSKGMQDFNYLHTNCFEITLELSCDKFPPEEELQREWLGNREALIQFLEQ 337
Cdd:cd03866 215 MYKGIECSNSqsFPGGITNGYQWYPLQGGMQDYNYVWGQCFEITLELSCCKYPPEETLPQFWNDNRVALIEYIKQ 289
M14_CP_plant cd18172
Zinc carboxypeptidase, including SOL1, a carboxypeptidase D in plant; This family includes ...
25-336 1.84e-99

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: 298.94  E-value: 1.84e-99
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503011   25 HHRYDDLVRTLYKVQNECPGITRVYSIGRSVEGRHLYVLEFSDHPGIHEPlEPEVKYVGNMHGNEALGRELMLQLSEFLC 104
Cdd:cd18172   1 YHSNAELEDALKAFTRRCGAISRLIVIGSSVNGFPLWALEISDGPGEDET-EPAFKFVGNMHGDEPVGRELLLRLADWLC 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503011  105 EEFRNRNQRIVQLIQDTRIHILPSMNPDGYEVAAaqgpnkpgylvgRNNANGVDLNRNFPDlntyIYYNekyggpnhhlP 184
Cdd:cd18172  80 ANYKAKDPLAAKIVENAHLHLVPTMNPDGFARRR------------RNNANNVDLNRDFPD----QFFP----------K 133
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503011  185 LPDNWKSQVEPETRAVIRWMHSFNFVLSANLHGGAVVANYPYDKSFEhrvrgvRRTASTPTPDDKLFQKLAKVYSYAHGW 264
Cdd:cd18172 134 NLRNDLAARQPETLAVMNWSRSVRFTASANLHEGALVANYPWDGNAD------GRTKYSASPDDATFRRLASVYAQAHPN 207
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 4503011  265 MfqgWNCGDyFPDGITNGASWYSLSKGMQDFNYLHTNCFEITLELSCDKFPPEEELQREWLGNREALIQFLE 336
Cdd:cd18172 208 M---AKSKE-FPGGITNGAQWYPLYGGMQDWNYLHTGCMDLTLEVNDNKWPPEDRLVQIWAEHRKAMLALAA 275
M14_CP_bacteria cd18173
bacterial peptidase M14 carboxypeptidase, uncharacterized; This family contains only bacterial ...
26-337 1.47e-98

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: 296.80  E-value: 1.47e-98
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503011   26 HRYDDLVRTLYKVQNECPGITRVYSIGRSVEGRHLYVLEFSDHPGIHEPlEPEVKYVGNMHGNEALGRELMLQLSEFLCE 105
Cdd:cd18173   5 PTYEEYEAMMQSFAANYPNICRLVSIGTSVQGRKLLALKISDNVNTEEA-EPEFKYTSTMHGDETTGYELMLRLIDYLLT 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503011  106 EFRNrNQRIVQLIQDTRIHILPSMNPDGYevaaAQGPNKPGYLVGRNNANGVDLNRNFPDLNTYiyynekyggpNHhlPL 185
Cdd:cd18173  84 NYGT-DPRITNLVDNTEIWINPLANPDGT----YAGGNNTVSGATRYNANGVDLNRNFPDPVDG----------DH--PD 146
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503011  186 PDNWksqvEPETRAVIRWMHSFNFVLSANLHGGAVVANYPYDksfehrvrgvrrTASTPTPDDKLFQKLAKVYS-YAHGW 264
Cdd:cd18173 147 GNGW----QPETQAMMNFADEHNFVLSANFHGGAEVVNYPWD------------TWYSRHPDDDWFQDISREYAdTNQAN 210
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 4503011  265 MFQGWNcgDYFPDGITNGASWYSLSKGMQDFNYLHTNCFEITLELSCDKFPPEEELQREWLGNREALIQFLEQ 337
Cdd:cd18173 211 SPPMYM--SEFNNGITNGYDWYEVYGGRQDYMYYWHGCREVTIELSNTKWPPASQLPTYWNYNRESLLNYIEQ 281
Peptidase_M14 pfam00246
Zinc carboxypeptidase;
31-330 1.58e-98

Zinc carboxypeptidase;


Pssm-ID: 459730 [Multi-domain]  Cd Length: 287  Bit Score: 297.29  E-value: 1.58e-98
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503011     31 LVRTLYKVQNECPGITRVYSIGRSVEGRHLYVLEFSDHPGIHEPLEPEVKYVGNMHGNEALGRELMLQLSEFLCEEFrNR 110
Cdd:pfam00246   1 IEAWLDALAARYPDLVRLVSIGKSVEGRPLKVLKISSGPGEHNPGKPAVFIDGGIHAREWIGPATALYLIHQLLTNY-GR 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503011    111 NQRIVQLIQDTRIHILPSMNPDGYEVAAAQgpnKPGYLVGRNNAN-----GVDLNRNFPDL-----NTYIYYNEKYGGPN 180
Cdd:pfam00246  80 DPEITELLDDTDIYILPVVNPDGYEYTHTT---DRLWRKNRSNANgssciGVDLNRNFPDHwnevgASSNPCSETYRGPA 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503011    181 HHLplpdnwksqvEPETRAVIRWMHSF-NFVLSANLHGGAVVANYPYDKsfehrvrgvrrTASTPTPDDKLFQKLAKVYS 259
Cdd:pfam00246 157 PFS----------EPETRAVADFIRSKkPFVLYISLHSYSQVLLYPYGY-----------TRDEPPPDDEELKSLARAAA 215
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 4503011    260 YAHGWMFQGWncgdYFPDGITNGASWYSLSKGMQDFNYLHTNC-FEITLELSCDK----FPPEEELQREWLGNREA 330
Cdd:pfam00246 216 KALQKMVRGT----SYTYGITNGATIYPASGGSDDWAYGRLGIkYSYTIELRDTGrygfLLPASQIIPTAEETWEA 287
Zn_pept smart00631
Zn_pept domain;
25-323 5.33e-92

Zn_pept domain;


Pssm-ID: 214748 [Multi-domain]  Cd Length: 277  Bit Score: 279.99  E-value: 5.33e-92
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503011      25 HHRYDDLVRTLYKVQNECPGITRVYSIGRSVEGRHLYVLEFSDHPGihePLEPEVKYVGNMHGNEALGRELMLQLSEFLC 104
Cdd:smart00631   1 YHSYEEIEAWLKELAARYPDLVRLVSIGKSVEGRPIWVLKISNGGS---HDKPAIFIDAGIHAREWIGPATALYLINQLL 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503011     105 EEFRnRNQRIVQLIQDTRIHILPSMNPDGYEVAAAqgpNKPGYLVGRN---NANGVDLNRNFPDLNTYIYY--NEKYGGP 179
Cdd:smart00631  78 ENYG-RDPRVTNLLDKTDIYIVPVLNPDGYEYTHT---GDRLWRKNRSpnsNCRGVDLNRNFPFHWGETGNpcSETYAGP 153
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503011     180 nhhlplpdnwKSQVEPETRAVIRWMHSF-NFVLSANLHGGAVVANYPYDKSFEHRVRGVRRtastptpDDKLFQKLAKVY 258
Cdd:smart00631 154 ----------SPFSEPETKAVRDFIRSNrRFKLYIDLHSYSQLILYPYGYTKNDLPPNVDD-------LDAVAKALAKAL 216
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 4503011     259 SYAHGWmfqgwncgdYFPDGITNGASWYSlSKGMQDFNYLHTN-CFEITLELSCD-----KFPPEEELQRE 323
Cdd:smart00631 217 ASVHGT---------RYTYGISNGAIYPA-SGGSDDWAYGVLGiPFSFTLELRDDgrygfLLPPSQIIPTG 277
M14_CPD_III cd06245
Peptidase M14 carboxypeptidase subfamily N/E-like; Carboxypeptidase D, domain III subgroup; ...
25-337 1.57e-75

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: 238.11  E-value: 1.57e-75
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503011   25 HHRYDDLVRTLYKVQNECPGITRVYSIGRSVEGRHLYVLEFSDHPGIHEPLEPEVKYVGNMHGNEALGRELMLQLSEFLC 104
Cdd:cd06245   1 YHSYKQLSKFLRGLNSNYPTITNLTSLGQSVEKRDIWVLEIGNKPNESEPSEPKILFVGGIHGNAPVGTELLLLLAHFLC 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503011  105 EEFRNrNQRIVQLIQDTRIHILPSMNPDGYEVAAAQGPNKpgyLVGRNNANGVDLNRNFPDlntyiyynekyggpnhhlp 184
Cdd:cd06245  81 HNYKK-DSAITKLLNRTRIHIVPSLNPDGAEKAEEKKCTS---KIGEKNANGVDLDTDFES------------------- 137
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503011  185 lPDNWKSQV-EPETRAVIRWMHSFNFVLSANLHGGAVVANYPYDKSfehrvrgvRRTAStptpDDKLFQKLAKVYSYAHG 263
Cdd:cd06245 138 -NANNRSGAaQPETKAIMDWLKEKDFTLSVALDGGSLVVTYPYDKP--------VQTVE----NKETLKHLAKVYANNHP 204
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 4503011  264 WMFQG-WNC---GDY-FPDGITNGASWYSLSKGMQDFNYLHTNCFEITLELSCDKFPPEEELQREWLGNREALIQFLEQ 337
Cdd:cd06245 205 TMHAGdPGCcsnSDEnFTNGVIRASEWHSHKGSMLDFSYKFGSCPEITVYTSCCYFPPAEELLTLWAEHKKSLLSMIVE 283
Peptidase_M14_like cd00596
M14 family of metallocarboxypeptidases and related proteins; The M14 family of ...
79-331 5.66e-41

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: 145.68  E-value: 5.66e-41
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503011   79 VKYVGNMHGNEALGRELMLQLSEFLCEEFRNrnQRIVQLIQDTRIHILPSMNPDGYEVAAaqgpnkpgYLVGRNNANGVD 158
Cdd:cd00596   1 ILITGGIHGNEVIGVELALALIEYLLENYGN--DPLKRLLDNVELWIVPLVNPDGFARVI--------DSGGRKNANGVD 70
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503011  159 LNRNFPDLNTYIYYN----EKYGGPNhhlPLPdnwksqvEPETRAVIRWMHSFNFVLSANLHGGAVVANYPYdksfehrv 234
Cdd:cd00596  71 LNRNFPYNWGKDGTSgpssPTYRGPA---PFS-------EPETQALRDLAKSHRFDLAVSYHSSSEAILYPY-------- 132
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503011  235 rgvrRTASTPTPDDKLFQKLAKVYSYAHGwmfqgwncgdYFPDGITNGASWYSLSKGMQDFNYLHTNCFEITLEL-SCDK 313
Cdd:cd00596 133 ----GYTNEPPPDFSEFQELAAGLARALG----------AGEYGYGYSYTWYSTTGTADDWLYGELGILAFTVELgTADY 198
                       250
                ....*....|....*...
gi 4503011  314 FPPEEELQREWLGNREAL 331
Cdd:cd00596 199 PLPGTLLDRRLERNLAAL 216
M14_CPT cd03859
Peptidase M14 Carboxypeptidase T subfamily; Peptidase M14-like domain of carboxypeptidase (CP) ...
26-331 5.69e-40

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: 145.09  E-value: 5.69e-40
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503011   26 HRYDDLVRTLYKVQNECPGITRVYSIGRSVEGRHLYVLEFSDHPGIhEPLEPEVKYVGNMHGNEALGRELMLQLSEFLCE 105
Cdd:cd03859   5 HTYAELVAELDQLAAEYPEITKLISIGKSVEGRPIWAVKISDNPDE-DEDEPEVLFMGLHHAREWISLEVALYFADYLLE 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503011  106 EFrNRNQRIVQLIQDTRIHILPSMNPDGYEVAAAQGpnkpGYLVGRNNAN----------GVDLNRNFP-------DLNT 168
Cdd:cd03859  84 NY-GTDPRITNLVDNREIWIIPVVNPDGYEYNRETG----GGRLWRKNRRpnngnnpgsdGVDLNRNYGyhwggdnGGSS 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503011  169 YIYYNEKYGGPNHHlplpdnwkSqvEPETRAVIRWMHSFNFVLSANLHGGAVVANYPYDksfehrvrgvrRTASTPTPDD 248
Cdd:cd03859 159 PDPSSETYRGPAPF--------S--EPETQAIRDLVESHDFKVAISYHSYGELVLYPWG-----------YTSDAPTPDE 217
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503011  249 KLFQKLAKVYSYahgwmfqgWNCGDYfpdgiTNGASW--YSLSKGMQDFNYLHTNCFEITLEL---SCDKFPPEEELQRE 323
Cdd:cd03859 218 DVFEELAEEMAS--------YNGGGY-----TPQQSSdlYPTNGDTDDWMYGEKGIIAFTPELgpeFYPFYPPPSQIDPL 284

                ....*...
gi 4503011  324 WLGNREAL 331
Cdd:cd03859 285 AEENLPAA 292
MpaA COG2866
Murein tripeptide amidase MpaA [Cell wall/membrane/envelope biogenesis];
24-227 3.91e-35

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


Pssm-ID: 442113 [Multi-domain]  Cd Length: 337  Bit Score: 133.28  E-value: 3.91e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503011   24 RHHRYDDLVRTLYKVQnECPGITRVYSIGRSVEGRHLYVLEFSDHpgihEPLEPEVKYVGNMHGNEALGRELMLQLSEFL 103
Cdd:COG2866  18 RYYTYEELLALLAKLA-AASPLVELESIGKSVEGRPIYLLKIGDP----AEGKPKVLLNAQQHGNEWTGTEALLGLLEDL 92
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503011  104 CEefrNRNQRIVQLIQDTRIHILPSMNPDGYEVAaaqgpnkpgylvGRNNANGVDLNRNFPDLntyiyynekyggpnhhl 183
Cdd:COG2866  93 LD---NYDPLIRALLDNVTLYIVPMLNPDGAERN------------TRTNANGVDLNRDWPAP----------------- 140
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....
gi 4503011  184 plpdnWKSQvePETRAVIRWMHSFNFVLSANLHGGAVVANYPYD 227
Cdd:COG2866 141 -----WLSE--PETRALRDLLDEHDPDFVLDLHGQGELFYWFVG 177
Peptidase_M14NE-CP-C_like cd11308
Peptidase associated domain: C-terminal domain of M14 N/E carboxypeptidase; putative folding, ...
341-415 7.47e-34

Peptidase associated domain: C-terminal domain of M14 N/E carboxypeptidase; putative folding, regulation, or interaction domain; This domain is found C-terminal to the M14 carboxypeptidase (CP) N/E subfamily containing zinc-binding enzymes that 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 enzymatically active members (carboxypeptidase N, E, M, D, and Z), as well as non-active members (carboxypeptidase-like protein 1, -2, aortic CP-like protein, and adipocyte enhancer binding protein-1) which lack the critical active site and substrate-binding residues considered necessary for activity. 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. For M14 CPs, it has been suggested that this domain may assist in folding of the CP domain, regulate enzyme activity, or be involved in interactions with other proteins or with membranes; for carboxypeptidase M, it may interact with the bradykinin 1 receptor at the cell surface. This domain may also be found in other peptidase families.


Pssm-ID: 200604 [Multi-domain]  Cd Length: 76  Bit Score: 121.86  E-value: 7.47e-34
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 4503011  341 GIKGMVLDENYNNLANAVISVSGINHDVTSGDHGDYFRLLLPGIYTVSATAPGYDPETVTVTVGP-AEPTLVNFHL 415
Cdd:cd11308   1 GIKGFVTDATGNPIANATISVEGINHDVTTAKDGDYWRLLLPGTYNVTASAPGYQPVTKTVTVPNnFSATVVNFTL 76
M14-like cd06905
Peptidase M14-like domain; uncharacterized subfamily; A functionally uncharacterized subgroup ...
21-309 3.02e-20

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: 91.91  E-value: 3.02e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503011   21 VTFRH-HRYDDLVRTLYKVQNECPGITRVYSIGRSVEGRHLYVLEFSDHPGIHEPLEPEVKYVGNMHGNEALGRELMLQL 99
Cdd:cd06905   1 LAFDRyYTYAELTARLKALAEAYPNLVRLESIGKSYEGRDIWLLTITNGETGPADEKPALWVDGNIHGNEVTGSEVALYL 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503011  100 SEFLCEEFrNRNQRIVQLIQDTRIHILPSMNPDGYEVAAAQGPN------------------------------------ 143
Cdd:cd06905  81 AEYLLTNY-GKDPEITRLLDTRTFYILPRLNPDGAEAYKLKTERsgrssprdddrdgdgdedgpedlngdglitqmrvkd 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503011  144 ----------------------KPGYLV----------GRNN---ANGVDLNRNFPdLNTYIYYNEKYGGPnhhLPLpdn 188
Cdd:cd06905 160 ptgtwkvdpddprlmvdrekgeKGFYRLypegidndgdGRYNedgPGGVDLNRNFP-YNWQPFYVQPGAGP---YPL--- 232
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503011  189 wkSqvEPETRAVIRWmhsfnfvLSANLHGGAVVANYPYDKSFeHRVRGVRRTASTPTPD----DKLFQKLAKVYSYahgW 264
Cdd:cd06905 233 --S--EPETRAVADF-------LLAHPNIAAVLTFHTSGGMI-LRPPGTGPDSDMPPADrrvyDAIGKKGVELTGY---P 297
                       330       340       350       360
                ....*....|....*....|....*....|....*....|....*
gi 4503011  265 MFQGWNCGDYFPDGITNGAswyslskgMQDFNYLHTNCFEITLEL 309
Cdd:cd06905 298 VSSVYKDFYTVPGGPLDGD--------FFDWAYFHLGIPSFSTEL 334
M14_MpaA-like cd06904
Peptidase M14-like domain of Escherichia coli Murein Peptide Amidase A and related proteins; ...
51-335 8.67e-19

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: 84.63  E-value: 8.67e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503011   51 IGRSVEGRHLYVLEFSDHPGiheplePEVKYVGNMHGNEALGRELMLQLSEFLCEEfrnrnqrivQLIQDTRIHILPSMN 130
Cdd:cd06904   4 YGTSVKGRPILAYKFGPGSR------ARILIIGGIHGDEPEGVSLVEHLLRWLKNH---------PASGDFHIVVVPCLN 68
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503011  131 PDGYevAAAQgpnkpgylvgRNNANGVDLNRNFPDLN----TYIYYNEKY-GGPnhhlplpdnwKSQVEPETRAVIRWMH 205
Cdd:cd06904  69 PDGL--AAGT----------RTNANGVDLNRNFPTKNwepdARKPKDPRYyPGP----------KPASEPETRALVELIE 126
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503011  206 SF--NFVLSanLHGGAVVANYPYDKSfehrvrgvrrtastptpddKLFQKLAKVYSYAHGwmfqgwncGDYfpdGITNGa 283
Cdd:cd06904 127 RFkpDRIIS--LHAPYLVNYDGPAKS-------------------LLAEKLAQATGYPVV--------GDV---GYTPG- 173
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....
gi 4503011  284 swyslSKGmqdfNY--LHTNCFEITLELscdkfPPEEELQREWLGNREALIQFL 335
Cdd:cd06904 174 -----SLG----TYagIERNIPVITLEL-----PEAVSIDELWQDLKRALIEAI 213
M14_Endopeptidase_I cd06229
Peptidase M14 carboxypeptidase family-like domain of Endopeptidase I; Peptidase M14-like ...
79-216 6.53e-15

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: 73.91  E-value: 6.53e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503011   79 VKYVGNMHGNEALGRELMLQLSEFLCEEFRNRN----QRIVQLIQDTRIHILPSMNPDGYEVAAaQGPNK--PGYLVGRN 152
Cdd:cd06229   1 VLYNASFHAREYITTLLLMKFIEDYAKAYVNKSyirgKDVGELLNKVTLHIVPMVNPDGVEISQ-NGSNAinPYYLRLVA 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503011  153 -------------NANGVDLNRNFPDL-NTYIYYNEKYGGPNHH---LPLPdnwksqvEPETRAVIRWMHSFNFVLSANL 215
Cdd:cd06229  80 wnkkgtdftgwkaNIRGVDLNRNFPAGwEKEKRLGPKAPGPRDYpgkEPLS-------EPETKAMAALTRQNDFDLVLAY 152

                .
gi 4503011  216 H 216
Cdd:cd06229 153 H 153
CarboxypepD_reg pfam13620
Carboxypeptidase regulatory-like domain;
341-415 9.73e-15

Carboxypeptidase regulatory-like domain;


Pssm-ID: 433354 [Multi-domain]  Cd Length: 81  Bit Score: 69.23  E-value: 9.73e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503011    341 GIKGMVLDENYNNLANAVISV----SGINHDVTSGDHGDY-FRLLLPGIYTVSATAPGYDPETVT-VTVGPAEPTLVNFH 414
Cdd:pfam13620   1 TISGTVTDPSGAPVPGATVTVtntdTGTVRTTTTDADGRYrFPGLPPGTYTVTVSAPGFKTATRTgVTVTAGQTTTLDVT 80

                  .
gi 4503011    415 L 415
Cdd:pfam13620  81 L 81
M14-CPA-like cd06227
Peptidase M14 carboxypeptidase A-like domain; uncharacterized subfamily; A functionally ...
84-231 1.80e-13

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: 69.61  E-value: 1.80e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503011   84 NMHGNEALGRELMLQLSEFLCEE----FRNRNQRIVQLI-QDTRIHILPSMNPDGYEVAAAqgpnkpGYLVGRNNANGVD 158
Cdd:cd06227   9 GEHARELISVESALRLLRQLCGGlqepAASALRELAREIlDNVELKIIPNANPDGRRLVES------GDYCWRGNENGVD 82
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 4503011  159 LNRNFP-----DLNTyiYYNEKYGGPNhhlPLPdnwksqvEPETRAVIRWMHSFNFVLSANLHGGAVVANYPYDKSFE 231
Cdd:cd06227  83 LNRNWGvdwgkGEKG--APSEEYPGPK---PFS-------EPETRALRDLALSFKPHAFVSVHSGMLAIYTPYAYSAS 148
M14-like cd03857
Peptidase M14-like domain; uncharacterized subfamily; Peptidase M14-like domain of a ...
81-284 1.27e-12

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: 66.71  E-value: 1.27e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503011   81 YVGNMHGNEALGRELMLQLSEFLCEEFRNRNqrivQLIQDTRIHILPSMNPDGYE-VAAAQGPNKPGYLVGRNNANGVDL 159
Cdd:cd03857   4 LAAQIHGNETTGTEALMELIRDLASESDEAA----KLLDNIVILLVPQLNPDGAElFVNFYLDSMNGLPGTRYNANGIDL 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503011  160 NRNFPDLNtyiyynekyggpnhhlplpdnwksqvEPETRA----VIRWMHSFNFvlsaNLHgGAVVANYPYDKSFEHRVR 235
Cdd:cd03857  80 NRDHVKLT--------------------------QPETQAvaenFIHWWPDIFI----DLH-EQVGASIPYPTPPDAPNY 128
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 4503011  236 GVRRTASTPTPDDKLFQKLAKVYSYAHGWMFQ----------GWNCGdYFPDGITNGAS 284
Cdd:cd03857 129 NLVDLRSDAENGQEHIRLIAGEGSGELGKYFSpmrggfddstGGNGI-GRTSGFHGAIS 186
M14_CP_A-B_like cd03860
Peptidase M14 carboxypeptidase subfamily A/B-like; The Peptidase M14 Carboxypeptidase (CP) A/B ...
26-206 1.70e-11

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: 64.86  E-value: 1.70e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503011   26 HRYDDLVRTLYKVQNECPGITRVYSIGRSVEGRHLYVLEFSDHPGIHEPlePEVKYVGNMHgnealGRE-----LMLQLS 100
Cdd:cd03860   2 HPLDDIVQWLDDLAAAFPDNVEIFTIGKSYEGRDITGIHIWGSGGKGGK--PAIVIHGGQH-----AREwistsTVEYLA 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503011  101 EFLCEEFRNRNQrIVQLIQDTRIHILPSMNPDGYEVAAA---------QGPNKPGYLvgrnnanGVDLNRNFPdlntyiy 171
Cdd:cd03860  75 HQLLSGYGSDAT-ITALLDKFDFYIIPVVNPDGYVYTWTtdrlwrknrQPTGGSSCV-------GIDLNRNWG------- 139
                       170       180       190
                ....*....|....*....|....*....|....*...
gi 4503011  172 YNEKYGGPNHHlPLPDNWKSQV---EPETRAVIRWMHS 206
Cdd:cd03860 140 YKWGGPGASTN-PCSETYRGPSafsAPETKALADFINA 176
M14_Nna1-like cd06237
Peptidase M14-like domain of ATP/GTP binding proteins and cytosolic carboxypeptidases; ...
43-204 4.34e-11

Peptidase M14-like domain of ATP/GTP binding proteins and cytosolic carboxypeptidases; uncharacterized bacterial subgroup; A bacterial subgroup of the Peptidase M14-like domain of Nna-1 (Nervous system Nuclear protein induced by Axotomy), also known as ATP/GTP binding protein (AGTPBP-1) and cytosolic carboxypeptidase (CCP),-like proteins. The Peptidase M14 family of metallocarboxypeptidases are zinc-binding carboxypeptidases (CPs) which hydrolyze single, C-terminal amino acids from polypeptide chains, and have a recognition site for the free C-terminal carboxyl group, which is a key determinant of specificity. Nna1-like proteins are active metallopeptidases that are thought to act on cytosolic proteins (such as alpha-tubulin in eukaryotes) to remove a C-terminal tyrosine. Nna1-like proteins from the different phyla are highly diverse, but they all contain a unique N-terminal conserved domain right before the CP domain. It has been suggested that this N-terminal domain might act as a folding domain.


Pssm-ID: 349456 [Multi-domain]  Cd Length: 239  Bit Score: 62.58  E-value: 4.34e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503011   43 PGITRVySIGRSVEGRHLYVLEFSD-------------HPgiheplePEVKyvgnmhGNEALGR--ELMLQLSEfLCEEF 107
Cdd:cd06237  14 PFVKRS-TIGKSVEGRPIEALTIGNpdskelvvllgrqHP-------PEVT------GALAMQAfvETLLADTE-LAKAF 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503011  108 RNRnqrivqliqdTRIHILPSMNPDGyeVAAaqgpnkpgylvG--RNNANGVDLNRnfpdlntyiyynekyggpnhhlpl 185
Cdd:cd06237  79 RAR----------FRVLVVPLLNPDG--VDL-----------GhwRHNAGGVDLNR------------------------ 111
                       170
                ....*....|....*....
gi 4503011  186 pdNWKSQVEPETRAVIRWM 204
Cdd:cd06237 112 --DWGPFTQPETRAVRDFL 128
M14-like cd06238
Peptidase M14-like domain; uncharacterized subgroup; Peptidase M14-like domain of a ...
83-208 7.71e-11

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


Pssm-ID: 349457  Cd Length: 217  Bit Score: 61.60  E-value: 7.71e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503011   83 GNMHGNEALGRELMLQLSEFLCEEfrnRNQRIVQLIQDTRIHILPSMNPDGYEvAAAQGPNKPGYLVGRNNANGVDLNRN 162
Cdd:cd06238   8 YSIHGNELSGSEAAMQVAYHLAAG---QDEATRALLENTVIVIDPNQNPDGRE-RFVNWFNQNRGAVGDPDPQSMEHNEP 83
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*..
gi 4503011  163 FPDlntyiyynekyGGPNHHL-PLPDNWKSQVEPETRAVIRWMHSFN 208
Cdd:cd06238  84 WPG-----------GRTNHYLfDLNRDWLAQTQPESRARAAAIHRWR 119
M14-like cd06242
Peptidase M14-like domain; uncharacterized subgroup; Peptidase M14-like domain of a ...
77-208 1.33e-10

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: 61.16  E-value: 1.33e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503011   77 PEVKYVGNMHGNEALGRELMLQLSEFLCEEFRNRNqrivqLIQDTRIHILPSMNPDGYEvaAAQgpnkpgylvgRNNANG 156
Cdd:cd06242   2 PTVLLVGQQHGNEPAGREAALALARDLAFGDDARE-----LLEKVNVLVVPRANPDGRA--ANT----------RGNANG 64
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|..
gi 4503011  157 VDLNRNfpdlntyiyynekyggpnhHLPLPdnwksqvEPETRAVIRWMHSFN 208
Cdd:cd06242  65 VDLNRD-------------------HLLLS-------TPETRALARVLRDYR 90
M14_CP_insect cd06248
Peptidase M14 carboxypeptidase subfamily A/B-like; This family includes peptidase M14 ...
26-235 1.33e-08

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: 55.93  E-value: 1.33e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503011   26 HRYDDLVRTLYKVQNECPGITRVYSIGRSVEGRHLYVLEFSDHPGIHEPlEPEVKYVGNMHGNEALGRELMLQLSEFLCE 105
Cdd:cd06248   2 HSLDEIDEYLDGLAEESPDVVTVVEGGYTFEGRPIKYVRIRSTNSEDTS-KPTIMIEGGINPREWISPPAALYAIHKLVE 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503011  106 efrnRNQRIVQLIQDTRIHILPSMNPDGYEVAAAQGPN-----KPGYLVGRNNANGVDLNRNF-----PDLNTYIYYNEK 175
Cdd:cd06248  81 ----DVETQSDLLNNFDWIILPVANPDGYVFTHTNDREwtknrSTNSNPLGQICFGVNINRNFdyqwnPVLSSESPCSEL 156
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 4503011  176 YGGPnhhlplpdnwKSQVEPETRAVIRWMHSFN--FVLSANLHGGAVVANYPYD----KSFEHRVR 235
Cdd:cd06248 157 YAGP----------SAFSEAESRAIRDILHEHGnrIHLYISFHSGGSFILYPWGydgsTSSNARQL 212
M14_PaCCP-like cd06234
Peptidase M14-like domain of ATP/GTP binding proteins and cytosolic carboxypeptidases similar ...
27-217 3.11e-08

Peptidase M14-like domain of ATP/GTP binding proteins and cytosolic carboxypeptidases similar to Pseudomonas aerugnosa CCP (PaCCP); A bacterial subgroup of the Peptidase M14-like domain of Nna-1 (Nervous system Nuclear protein induced by Axotomy), also known as ATP/GTP binding protein (AGTPBP-1) and cytosolic carboxypeptidase (CCP)-like proteins. This subgroup includes PaCCP from Pseudomonas aeruginosa, a carboxypeptidase homologous to M14D subfamily of human CCPs. Structural complexes with well-known inhibitors of metallocarboxypeptidases indicate that PaCCP might only possess C-terminal hydrolase activity against cellular substrates of particular specificity. The Peptidase M14 family of metallocarboxypeptidases are zinc-binding carboxypeptidases (CPs) which hydrolyze single, C-terminal amino acids from polypeptide chains, and have a recognition site for the free C-terminal carboxyl group, which is a key determinant of specificity. Nna1-like proteins are active metallopeptidases that are thought to act on cytosolic proteins (such as alpha-tubulin in eukaryotes) to remove a C-terminal tyrosine. Nna1-like proteins from the different phyla are highly diverse, but they all contain a unique N-terminal conserved domain right before the CP domain. It has been suggested that this N-terminal domain might act as a folding domain.


Pssm-ID: 349453 [Multi-domain]  Cd Length: 256  Bit Score: 54.49  E-value: 3.11e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503011   27 RYDDLVRTLykvqnECPGITRVYSIGRSVEGRHLYVLEFSD--------------HPGiheplepevkyvgnmhgnealg 92
Cdd:cd06234   5 RHLDLVARA-----QASPGVRLEVLGQTLDGRDIDLLTIGDpgtgkkkvwiiarqHPG---------------------- 57
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503011   93 rELMlqlSEFLCEEFRNR-----NQRIVQLIQDTRIHILPSMNPDGyevaaaqgpNKPGYLvgRNNANGVDLNRNFPDln 167
Cdd:cd06234  58 -ETM---AEWFMEGLLDRlldedDPVSRALLEKAVFYVVPNMNPDG---------SVRGNL--RTNAAGVNLNREWAN-- 120
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|
gi 4503011  168 tyiyynekyggpnhhlplPDNWKSqvePETRAVIRWMHSFNFVLSANLHG 217
Cdd:cd06234 121 ------------------PSLERS---PEVFAVRQAMDATGVDFFLDVHG 149
M14-like cd06239
Peptidase M14-like domain; uncharacterized subgroup; Peptidase M14-like domain of a ...
85-217 3.30e-08

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


Pssm-ID: 349458 [Multi-domain]  Cd Length: 194  Bit Score: 53.57  E-value: 3.30e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503011   85 MHGNEALGRELMLQLSEFLceefRNRNQRIVQLIQDTRIHILPSMNPDGYEvaaaqgpnkpgyLVGRNNANGVDLNRNFP 164
Cdd:cd06239   8 MHGNEPTGTEALLDLISYL----RRERQEFEKILERLTLVAIPMLNPDGAE------------LFTRHNAEGIDLNRDAR 71
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|...
gi 4503011  165 DLNTyiyynekyggpnhhlplpdnwksqvePETRAVIRWMHSFNFVLSANLHG 217
Cdd:cd06239  72 ALQT--------------------------PESRALKAVLDSFSPKFAFNLHD 98
PRK10602 PRK10602
murein tripeptide amidase MpaA;
122-212 1.74e-07

murein tripeptide amidase MpaA;


Pssm-ID: 182582  Cd Length: 237  Bit Score: 51.95  E-value: 1.74e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503011   122 RIHILPSMNPDGyevaaAQgpnkpgyLVGRNNANGVDLNRNFPDLN-----TYIYYNEKygGPNHHLPLPDNWKSQVEPE 196
Cdd:PRK10602  72 RHHVVLAVNPDG-----CQ-------LGLRANANGVDLNRNFPAANwkegeTVYRWNSA--AEERDVVLLTGDKPGSEPE 137
                         90
                 ....*....|....*...
gi 4503011   197 TRAVIRWMHSFN--FVLS 212
Cdd:PRK10602 138 TQALCQLIHRLQpaWVVS 155
M14-like cd06244
Peptidase M14-like domain; uncharacterized subgroup; Peptidase M14-like domain of a ...
84-217 2.59e-07

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


Pssm-ID: 349463 [Multi-domain]  Cd Length: 223  Bit Score: 51.30  E-value: 2.59e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503011   84 NMHGNEALGRELMLQLSEFLCEE-------------FRNRNQRIVQLIQDTRIHILPSMNPDGYEVAAaqgpnkpgylvg 150
Cdd:cd06244   7 NIHGNEVEGVDALLEFLEMLATEpnvtyntlvkyykVENVDLEVKDLLDDVFFIVVPTENPDGRVANT------------ 74
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 4503011  151 RNNANGVDLNRNfpdlNTYiyynekyggpnhhlplpdnwksQVEPETRAVIRWMHSFNFVLSANLHG 217
Cdd:cd06244  75 RTNANGFDLNRD----NAY----------------------QTQPETRAMQELISKWNPVTFLDMHG 115
CarbopepD_reg_2 pfam13715
CarboxypepD_reg-like domain; This domain family is found in bacteria, archaea and eukaryotes, ...
342-416 5.54e-07

CarboxypepD_reg-like domain; This domain family is found in bacteria, archaea and eukaryotes, and is approximately 90 amino acids in length. The family is found in association with pfam07715 and pfam00593.


Pssm-ID: 433425 [Multi-domain]  Cd Length: 88  Bit Score: 47.20  E-value: 5.54e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 4503011    342 IKGMVLDENYNN-LANAVISVSGINHDVTSGDHGDY-FRLLLPGIYTVSATAPGYDPETVTVTVGPAEPTLVNFHLK 416
Cdd:pfam13715   1 ISGTVVDENTGEpLPGATVYVKGTTKGTVTDADGNFeLKNLPAGTYTLVVSFVGYKTQEKKVTVSNDNTLDVNFLLK 77
M14_CPT_like cd06226
Peptidase M14-like domain of an uncharacterized group of Peptidase M14 Carboxypeptidase T (CPT) ...
83-288 1.53e-06

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: 49.37  E-value: 1.53e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503011   83 GNMHGNEALGRELMLQLSEFLCEEFrNRNQRIVQLIQDTRIHILPSMNPDGYEVAAAqgpnkpGYLvGRNNAN------- 155
Cdd:cd06226  25 AAIHAREYTTAELVARFAEDLVAGY-GTDADATWLLDYTELHLVPQVNPDGRKIAET------GLL-WRKNTNttpcpas 96
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503011  156 ----GVDLNRNFPdlntyiyynEKYGGP---------NHHLPLPDNwksqvEPETRAVIRWMHSF--------------- 207
Cdd:cd06226  97 sptyGVDLNRNSS---------FKWGGAgaggsacseTYRGPSAAS-----EPETQAIENYVKQLfpdqrgpgltdpapd 162
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503011  208 ---NFVLSANLHGGAVVanYPYDksfehrvrgvrrTASTPTPDDKLFQKLAKVYSYAHGWMFQGwNCGDYFPDGITNGAS 284
Cdd:cd06226 163 dtsGIYIDIHSYGNLVL--YPWG------------WTGTPAPNAAGLRTLGRKFAYFNGYTPQQ-AVALYPTDGTTDDFA 227

                ....
gi 4503011  285 WYSL 288
Cdd:cd06226 228 YGTL 231
M14_CPA cd03870
Peptidase M14 carboxypeptidase subfamily A/B-like; Carboxypeptidase A subgroup; Peptidase M14 ...
40-263 1.61e-06

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: 49.74  E-value: 1.61e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503011   40 NECPGITRVYSIGRSVEGRHLYVLEFSDHPgihePLEPEVKYVGNMHGNEALGRELMLQLSEFLCEEFrNRNQRIVQLIQ 119
Cdd:cd03870  21 AEHPNLVSKLQIGSSFENRPMYVLKFSTGG----EERPAIWIDAGIHSREWVTQASAIWTAEKIVSDY-GKDPSITSILD 95
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503011  120 DTRIHILPSMNPDGYevAAAQGPN----KPGYLVGRNNANGVDLNRNFpdlntyiyyNEKYGGP---------NHHLPLP 186
Cdd:cd03870  96 TMDIFLEIVTNPDGY--VFTHSSNrlwrKTRSVNPGSLCIGVDPNRNW---------DAGFGGPgassnpcseTYHGPHA 164
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503011  187 DNwksqvEPETRAVIRWMHSF-NFVLSANLHGGAVVANYPYDKSFEhrvrgvrrtastPTPD----DKLFQKLAKVYSYA 261
Cdd:cd03870 165 NS-----EVEVKSIVDFIQSHgNFKAFISIHSYSQLLMYPYGYTVE------------KAPDqeelDEVAKKAVKALASL 227

                ..
gi 4503011  262 HG 263
Cdd:cd03870 228 HG 229
M14-like cd06228
Peptidase M14-like domain; uncharacterized subfamily; A functionally uncharacterized subgroup ...
77-204 4.26e-06

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: 48.15  E-value: 4.26e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503011   77 PEVKYVGNMHGNEALGRELMLQLSEFLCEEFRNRN-----------QRIVQLIQDTRIHILPSMNPDGYEVAAAQGP--- 142
Cdd:cd06228   1 PGVYFIGGVHAREWGSPDILIYFAADLLEAYTNNTgltyggktftaAQVKSILENVDLVVFPLVNPDGRWYSQTSESmwr 80
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 4503011  143 -NK-PGYLVGRNNANGVDLNRNFPDLNTYiyynEKYGGPNhHLPLPDNWKSQV--------EPETRAViRWM 204
Cdd:cd06228  81 kNRnPASAGDGGSCIGVDINRNFDFLWDF----PRYFDPG-RVPASTSPCSETyhgpsafsEPETRNV-VWL 146
M14_REP34-like cd06231
Peptidase M14-like domain similar to rapid encystment phenotype 34 (REP34); This family ...
53-216 4.45e-06

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


Pssm-ID: 349450 [Multi-domain]  Cd Length: 239  Bit Score: 47.69  E-value: 4.45e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503011   53 RSVEGRHLYVLEFSDHPGIHEPL--------EPEVKYV---GNMHGNEALGRELMLQlseFLCEEFRNRNQRIvqliqdt 121
Cdd:cd06231   8 ERLGARRFKVRELGEVGYQGYPLfalkspnpRGDKPRVlisAGIHGDEPAGVEALLR---FLESLAEKYLRRV------- 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503011  122 RIHILPSMNPDGYEvaaaqgpnkpgyLVGRNNANGVDLNRNFpdlntyiyynekyggpnhhlplpdnWKSQVEPETRAVI 201
Cdd:cd06231  78 NLLVLPCVNPWGFE------------RNTRENADGIDLNRSF-------------------------LKDSPSPEVRALM 120
                       170
                ....*....|....*.
gi 4503011  202 RWM-HSFNFVLSANLH 216
Cdd:cd06231 121 EFLaSLGRFDLHLDLH 136
M14_CPB2 cd06246
Peptidase M14 carboxypeptidase subfamily A/B-like; Carboxypeptidase B2 subgroup; Peptidase M14 ...
24-206 4.41e-05

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: 45.18  E-value: 4.41e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503011   24 RHHRYDDLVRTLYKVQNECPGITRVYSIGRSVEGRHLYVLEFSDHpgiheplEPEVKYV----GNMHGNEALGRELMLQL 99
Cdd:cd06246   4 QYHSLNEIYSWIEFITERHPDMLTKIHIGSSFEKYPLYVLKVSGK-------EQTAKNAiwidCGIHAREWISPAFCLWF 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503011  100 SEFLCeEFRNRNQRIVQLIQDTRIHILPSMNPDGYEVaaAQGPN----KPGYLVGRNNANGVDLNRNFpDLN------TY 169
Cdd:cd06246  77 IGHAS-YFYGIIGQHTNLLNLVDFYVMPVVNVDGYDY--SWKKNrmwrKNRSKHANNRCIGTDLNRNF-DAGwcgkgaSS 152
                       170       180       190
                ....*....|....*....|....*....|....*..
gi 4503011  170 IYYNEKYGGpnhhlPLPDNwksqvEPETRAVIRWMHS 206
Cdd:cd06246 153 DSCSETYCG-----PYPES-----EPEVKAVASFLRR 179
M14_CPA6 cd03872
Peptidase M14 carboxypeptidase subfamily A/B-like; Carboxypeptidase A6 subgroup; ...
25-226 1.19e-03

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: 40.73  E-value: 1.19e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503011   25 HHRYDDLVRTLYKVQNECPGITRVYSIGRSVEGRHLYVLEFSDHPgihEPLEPEVKYVGNMHGNEALGRElmlqlsefLC 104
Cdd:cd03872   2 YHSLEEIESWMFYMNKTHSDLVHMFSIGKSYEGRSLYVLKLGKRS---RSYKKAVWIDCGIHAREWIGPA--------FC 70
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503011  105 EEF-------RNRNQRIVQLIQDTRIHILPSMNPDGYEVAAAQGP--NKPGYLVGRNNANGVDLNRNFP----DLNTYIY 171
Cdd:cd03872  71 QWFvkeainsYQTDPAMKKMLNQLYFYVMPVFNVDGYHYSWTNDRfwRKTRSKNSRFQCRGVDANRNWKvkwcDEGASLH 150
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 4503011  172 -YNEKYGGpnhhlPLPDNwksqvEPETRAVIRWMHSFNFVLSA--NLHGGAVVANYPY 226
Cdd:cd03872 151 pCDDTYCG-----PFPES-----EPEVKAVAQFLRKHRKHVRAylSFHAYAQMLLYPY 198
M14-like cd06241
Peptidase M14-like domain; uncharacterized subgroup; Peptidase M14-like domain of a ...
83-163 1.23e-03

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


Pssm-ID: 349460 [Multi-domain]  Cd Length: 215  Bit Score: 40.32  E-value: 1.23e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503011   83 GNMHGNEALGRELMLQLseflceeFRNrnqrIVQ-----LIQDTRIHILPSMNPDGYE-VAAAQGPNKPG-YLVG-RNNA 154
Cdd:cd06241   8 AGIHPGEVEGKEASLML-------LRD----IAQggkkhLLDNLILLFVPIFNADGNDrRSKGNRPNQNGpLEVGwRTNA 76

                ....*....
gi 4503011  155 NGVDLNRNF 163
Cdd:cd06241  77 QGLDLNRDF 85
DUF2817 pfam10994
Protein of unknown function (DUF2817); This family of proteins has no known function.
151-189 1.75e-03

Protein of unknown function (DUF2817); This family of proteins has no known function.


Pssm-ID: 431588  Cd Length: 340  Bit Score: 40.34  E-value: 1.75e-03
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 4503011    151 RNNANGVDLNRNFPDLNTYIYYNEKYGGPNHHLpLPDNW 189
Cdd:pfam10994 106 RVNENNVDLNRNFLDFDAPLPANPAYAELHPLL-LPDEW 143
ClfA COG4932
Clumping factor A-related surface protein, MSCRAMM (microbial surface components recognizing ...
341-412 2.02e-03

Clumping factor A-related surface protein, MSCRAMM (microbial surface components recognizing adhesive matrix molecules) family, DEv-IgG fold [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 443959 [Multi-domain]  Cd Length: 689  Bit Score: 40.73  E-value: 2.02e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503011  341 GIKGMVLDEN--YNNLANAVISVSGIN----HDVTSGDHGDY-FRLLLPGIYTVSAT-AP-GY--DPETVTVTVGPAEPT 409
Cdd:COG4932 359 SVTLTKVDADdgEAPLAGAEFTLTDADgtvvATITTDADGTAsFKGLAPGTYTLTETkAPeGYtlDSTPITVTVTDGGTG 438

                ...
gi 4503011  410 LVN 412
Cdd:COG4932 439 AID 441
M14-like cd03862
Peptidase M14-like domain; uncharacterized subfamily; A functionally uncharacterized subgroup ...
77-218 3.82e-03

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: 349434  Cd Length: 245  Bit Score: 38.95  E-value: 3.82e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503011   77 PEVKYVGNMHGNEALGRELMLQLSEFLCEEFRnRNQRIVQLIQDTRIHILPSMNPDGyeVAAAQgpnkpgylvgRNNANG 156
Cdd:cd03862   1 PVVGLVGGVHGLERIGTQVILAFLRSLLARLK-WDKLLQELLEEVRLVVIPIVNPGG--MALKT----------RSNPNG 67
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 4503011  157 VDLNRNFPdLNTYIYYNEKYGGP--NHHLPlpdnW---KSQVEPETRAVIRWMHSF----NFVLSANLHGG 218
Cdd:cd03862  68 VDLMRNAP-VEAVEKVPFLVGGQriSPHLP----WyrgRNGLETESQALIRYVNEHllesKMSISLDCHSG 133
 
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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