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Conserved domains on  [gi|4502173|ref|NP_001639|]
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prostate-specific antigen isoform 1 preproprotein [Homo sapiens]

Protein Classification

serine protease( domain architecture ID 10076129)

trypsin-like serine protease such as human plasminogen, the precursor of the widely distributed protease plasmin, or granzyme B, a human enzyme necessary for target cell lysis in cell-mediated immune responses

CATH:  2.40.10.10
EC:  3.4.21.-
PubMed:  18259688

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
25-256 7.10e-92

Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens that are cleaved during limited proteolysis to generate their active forms. Alignment contains also inactive enzymes that have substitutions of the catalytic triad residues.


:

Pssm-ID: 238113 [Multi-domain]  Cd Length: 232  Bit Score: 270.69  E-value: 7.10e-92
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502173   25 IVGGWECEKHSQPWQV-LVASRGRAVCGGVLVHPQWVLTAAHCIRNKSV----ILLGRHSLFHPEDTGQVFQVSHSFPHP 99
Cdd:cd00190   1 IVGGSEAKIGSFPWQVsLQYTGGRHFCGGSLISPRWVLTAAHCVYSSAPsnytVRLGSHDLSSNEGGGQVIKVKKVIVHP 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502173  100 LYDMsllknrflrpgDDSSHDLMLLRLSEPAELTDAVKVMDLPTQ--EPALGTTCYASGWGSIEPEEFLtPKKLQCVDLH 177
Cdd:cd00190  81 NYNP-----------STYDNDIALLKLKRPVTLSDNVRPICLPSSgyNLPAGTTCTVSGWGRTSEGGPL-PDVLQEVNVP 148
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502173  178 VISNDVCAQVHPQ--KVTKFMLCAGRWTGGKSTCSGDSGGPLVCN----GVLQGITSWGSEpCALPERPSLYTKVVHYRK 251
Cdd:cd00190 149 IVSNAECKRAYSYggTITDNMLCAGGLEGGKDACQGDSGGPLVCNdngrGVLVGIVSWGSG-CARPNYPGVYTRVSSYLD 227

                ....*
gi 4502173  252 WIKDT 256
Cdd:cd00190 228 WIQKT 232
 
Name Accession Description Interval E-value
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
25-256 7.10e-92

Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens that are cleaved during limited proteolysis to generate their active forms. Alignment contains also inactive enzymes that have substitutions of the catalytic triad residues.


Pssm-ID: 238113 [Multi-domain]  Cd Length: 232  Bit Score: 270.69  E-value: 7.10e-92
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502173   25 IVGGWECEKHSQPWQV-LVASRGRAVCGGVLVHPQWVLTAAHCIRNKSV----ILLGRHSLFHPEDTGQVFQVSHSFPHP 99
Cdd:cd00190   1 IVGGSEAKIGSFPWQVsLQYTGGRHFCGGSLISPRWVLTAAHCVYSSAPsnytVRLGSHDLSSNEGGGQVIKVKKVIVHP 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502173  100 LYDMsllknrflrpgDDSSHDLMLLRLSEPAELTDAVKVMDLPTQ--EPALGTTCYASGWGSIEPEEFLtPKKLQCVDLH 177
Cdd:cd00190  81 NYNP-----------STYDNDIALLKLKRPVTLSDNVRPICLPSSgyNLPAGTTCTVSGWGRTSEGGPL-PDVLQEVNVP 148
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502173  178 VISNDVCAQVHPQ--KVTKFMLCAGRWTGGKSTCSGDSGGPLVCN----GVLQGITSWGSEpCALPERPSLYTKVVHYRK 251
Cdd:cd00190 149 IVSNAECKRAYSYggTITDNMLCAGGLEGGKDACQGDSGGPLVCNdngrGVLVGIVSWGSG-CARPNYPGVYTRVSSYLD 227

                ....*
gi 4502173  252 WIKDT 256
Cdd:cd00190 228 WIQKT 232
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
24-253 3.60e-91

Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens that are cleaved during limited proteolysis to generate their active forms. A few, however, are active as single chain molecules, and others are inactive due to substitutions of the catalytic triad residues.


Pssm-ID: 214473  Cd Length: 229  Bit Score: 268.78  E-value: 3.60e-91
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502173      24 RIVGGWECEKHSQPWQV-LVASRGRAVCGGVLVHPQWVLTAAHCIRNKSV----ILLGRHSLFHPEDtGQVFQVSHSFPH 98
Cdd:smart00020   1 RIVGGSEANIGSFPWQVsLQYGGGRHFCGGSLISPRWVLTAAHCVRGSDPsnirVRLGSHDLSSGEE-GQVIKVSKVIIH 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502173      99 PLYDMSLLknrflrpgddsSHDLMLLRLSEPAELTDAVKVMDLPT--QEPALGTTCYASGWGSIEPEEFLTPKKLQCVDL 176
Cdd:smart00020  80 PNYNPSTY-----------DNDIALLKLKEPVTLSDNVRPICLPSsnYNVPAGTTCTVSGWGRTSEGAGSLPDTLQEVNV 148
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502173     177 HVISNDVCAQVHPQ--KVTKFMLCAGRWTGGKSTCSGDSGGPLVCN---GVLQGITSWGSePCALPERPSLYTKVVHYRK 251
Cdd:smart00020 149 PIVSNATCRRAYSGggAITDNMLCAGGLEGGKDACQGDSGGPLVCNdgrWVLVGIVSWGS-GCARPGKPGVYTRVSSYLD 227

                   ..
gi 4502173     252 WI 253
Cdd:smart00020 228 WI 229
Trypsin pfam00089
Trypsin;
25-253 5.30e-74

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 225.01  E-value: 5.30e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502173     25 IVGGWECEKHSQPWQVLVASRGRAV-CGGVLVHPQWVLTAAHCIRNKS--VILLGRHSLFHPEDTGQVFQVSHSFPHPLY 101
Cdd:pfam00089   1 IVGGDEAQPGSFPWQVSLQLSSGKHfCGGSLISENWVLTAAHCVSGASdvKVVLGAHNIVLREGGEQKFDVEKIIVHPNY 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502173    102 DmsllknrflrpGDDSSHDLMLLRLSEPAELTDAVKVMDLPTQEP--ALGTTCYASGWGSiePEEFLTPKKLQCVDLHVI 179
Cdd:pfam00089  81 N-----------PDTLDNDIALLKLESPVTLGDTVRPICLPDASSdlPVGTTCTVSGWGN--TKTLGPSDTLQEVTVPVV 147
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 4502173    180 SNDVCAQVHPQKVTKFMLCAGrwTGGKSTCSGDSGGPLVC-NGVLQGITSWGsEPCALPERPSLYTKVVHYRKWI 253
Cdd:pfam00089 148 SRETCRSAYGGTVTDTMICAG--AGGKDACQGDSGGPLVCsDGELIGIVSWG-YGCASGNYPGVYTPVSSYLDWI 219
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
23-257 8.80e-57

Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 182.16  E-value: 8.80e-57
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502173   23 SRIVGGWECEKHSQPWQVLVASRG---RAVCGGVLVHPQWVLTAAHCIRNKSV----ILLGRHSLFhpEDTGQVFQVSHS 95
Cdd:COG5640  29 PAIVGGTPATVGEYPWMVALQSSNgpsGQFCGGTLIAPRWVLTAAHCVDGDGPsdlrVVIGSTDLS--TSGGTVVKVARI 106
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502173   96 FPHPLYDMSllknrflrpgdDSSHDLMLLRLSEPAELTDAVKVMDlPTQEPALGTTCYASGWGSIEPEEFLTPKKLQCVD 175
Cdd:COG5640 107 VVHPDYDPA-----------TPGNDIALLKLATPVPGVAPAPLAT-SADAAAPGTPATVAGWGRTSEGPGSQSGTLRKAD 174
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502173  176 LHVISNDVCAqVHPQKVTKFMLCAGRWTGGKSTCSGDSGGPLV----CNGVLQGITSWGSEPCAlPERPSLYTKVVHYRK 251
Cdd:COG5640 175 VPVVSDATCA-AYGGFDGGTMLCAGYPEGGKDACQGDSGGPLVvkdgGGWVLVGVVSWGGGPCA-AGYPGVYTRVSAYRD 252

                ....*.
gi 4502173  252 WIKDTI 257
Cdd:COG5640 253 WIKSTA 258
 
Name Accession Description Interval E-value
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
25-256 7.10e-92

Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens that are cleaved during limited proteolysis to generate their active forms. Alignment contains also inactive enzymes that have substitutions of the catalytic triad residues.


Pssm-ID: 238113 [Multi-domain]  Cd Length: 232  Bit Score: 270.69  E-value: 7.10e-92
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502173   25 IVGGWECEKHSQPWQV-LVASRGRAVCGGVLVHPQWVLTAAHCIRNKSV----ILLGRHSLFHPEDTGQVFQVSHSFPHP 99
Cdd:cd00190   1 IVGGSEAKIGSFPWQVsLQYTGGRHFCGGSLISPRWVLTAAHCVYSSAPsnytVRLGSHDLSSNEGGGQVIKVKKVIVHP 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502173  100 LYDMsllknrflrpgDDSSHDLMLLRLSEPAELTDAVKVMDLPTQ--EPALGTTCYASGWGSIEPEEFLtPKKLQCVDLH 177
Cdd:cd00190  81 NYNP-----------STYDNDIALLKLKRPVTLSDNVRPICLPSSgyNLPAGTTCTVSGWGRTSEGGPL-PDVLQEVNVP 148
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502173  178 VISNDVCAQVHPQ--KVTKFMLCAGRWTGGKSTCSGDSGGPLVCN----GVLQGITSWGSEpCALPERPSLYTKVVHYRK 251
Cdd:cd00190 149 IVSNAECKRAYSYggTITDNMLCAGGLEGGKDACQGDSGGPLVCNdngrGVLVGIVSWGSG-CARPNYPGVYTRVSSYLD 227

                ....*
gi 4502173  252 WIKDT 256
Cdd:cd00190 228 WIQKT 232
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
24-253 3.60e-91

Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens that are cleaved during limited proteolysis to generate their active forms. A few, however, are active as single chain molecules, and others are inactive due to substitutions of the catalytic triad residues.


Pssm-ID: 214473  Cd Length: 229  Bit Score: 268.78  E-value: 3.60e-91
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502173      24 RIVGGWECEKHSQPWQV-LVASRGRAVCGGVLVHPQWVLTAAHCIRNKSV----ILLGRHSLFHPEDtGQVFQVSHSFPH 98
Cdd:smart00020   1 RIVGGSEANIGSFPWQVsLQYGGGRHFCGGSLISPRWVLTAAHCVRGSDPsnirVRLGSHDLSSGEE-GQVIKVSKVIIH 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502173      99 PLYDMSLLknrflrpgddsSHDLMLLRLSEPAELTDAVKVMDLPT--QEPALGTTCYASGWGSIEPEEFLTPKKLQCVDL 176
Cdd:smart00020  80 PNYNPSTY-----------DNDIALLKLKEPVTLSDNVRPICLPSsnYNVPAGTTCTVSGWGRTSEGAGSLPDTLQEVNV 148
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502173     177 HVISNDVCAQVHPQ--KVTKFMLCAGRWTGGKSTCSGDSGGPLVCN---GVLQGITSWGSePCALPERPSLYTKVVHYRK 251
Cdd:smart00020 149 PIVSNATCRRAYSGggAITDNMLCAGGLEGGKDACQGDSGGPLVCNdgrWVLVGIVSWGS-GCARPGKPGVYTRVSSYLD 227

                   ..
gi 4502173     252 WI 253
Cdd:smart00020 228 WI 229
Trypsin pfam00089
Trypsin;
25-253 5.30e-74

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 225.01  E-value: 5.30e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502173     25 IVGGWECEKHSQPWQVLVASRGRAV-CGGVLVHPQWVLTAAHCIRNKS--VILLGRHSLFHPEDTGQVFQVSHSFPHPLY 101
Cdd:pfam00089   1 IVGGDEAQPGSFPWQVSLQLSSGKHfCGGSLISENWVLTAAHCVSGASdvKVVLGAHNIVLREGGEQKFDVEKIIVHPNY 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502173    102 DmsllknrflrpGDDSSHDLMLLRLSEPAELTDAVKVMDLPTQEP--ALGTTCYASGWGSiePEEFLTPKKLQCVDLHVI 179
Cdd:pfam00089  81 N-----------PDTLDNDIALLKLESPVTLGDTVRPICLPDASSdlPVGTTCTVSGWGN--TKTLGPSDTLQEVTVPVV 147
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 4502173    180 SNDVCAQVHPQKVTKFMLCAGrwTGGKSTCSGDSGGPLVC-NGVLQGITSWGsEPCALPERPSLYTKVVHYRKWI 253
Cdd:pfam00089 148 SRETCRSAYGGTVTDTMICAG--AGGKDACQGDSGGPLVCsDGELIGIVSWG-YGCASGNYPGVYTPVSSYLDWI 219
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
23-257 8.80e-57

Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 182.16  E-value: 8.80e-57
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502173   23 SRIVGGWECEKHSQPWQVLVASRG---RAVCGGVLVHPQWVLTAAHCIRNKSV----ILLGRHSLFhpEDTGQVFQVSHS 95
Cdd:COG5640  29 PAIVGGTPATVGEYPWMVALQSSNgpsGQFCGGTLIAPRWVLTAAHCVDGDGPsdlrVVIGSTDLS--TSGGTVVKVARI 106
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502173   96 FPHPLYDMSllknrflrpgdDSSHDLMLLRLSEPAELTDAVKVMDlPTQEPALGTTCYASGWGSIEPEEFLTPKKLQCVD 175
Cdd:COG5640 107 VVHPDYDPA-----------TPGNDIALLKLATPVPGVAPAPLAT-SADAAAPGTPATVAGWGRTSEGPGSQSGTLRKAD 174
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502173  176 LHVISNDVCAqVHPQKVTKFMLCAGRWTGGKSTCSGDSGGPLV----CNGVLQGITSWGSEPCAlPERPSLYTKVVHYRK 251
Cdd:COG5640 175 VPVVSDATCA-AYGGFDGGTMLCAGYPEGGKDACQGDSGGPLVvkdgGGWVLVGVVSWGGGPCA-AGYPGVYTRVSAYRD 252

                ....*.
gi 4502173  252 WIKDTI 257
Cdd:COG5640 253 WIKSTA 258
eMpr COG3591
V8-like Glu-specific endopeptidase [Posttranslational modification, protein turnover, ...
41-235 4.92e-10

V8-like Glu-specific endopeptidase [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 442810 [Multi-domain]  Cd Length: 194  Bit Score: 57.38  E-value: 4.92e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502173   41 LVASRGRAVCGGVLVHPQWVLTAAHCIRNKSVILLGRHSLFHP---EDTGQVFQVSHSFPHPLYDMSllknrflrpgDDS 117
Cdd:COG3591   5 LETDGGGGVCTGTLIGPNLVLTAGHCVYDGAGGGWATNIVFVPgynGGPYGTATATRFRVPPGWVAS----------GDA 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502173  118 SHDLMLLRLSEPaeLTDAVKVMDL-PTQEPALGTTCYASGWGSIEPEefltpkklqcvDLHVISNDVCAQVHPQKVtkFM 196
Cdd:COG3591  75 GYDYALLRLDEP--LGDTTGWLGLaFNDAPLAGEPVTIIGYPGDRPK-----------DLSLDCSGRVTGVQGNRL--SY 139
                       170       180       190       200
                ....*....|....*....|....*....|....*....|...
gi 4502173  197 LCagrwtggkSTCSGDSGGPLV----CNGVLQGITSWGSEPCA 235
Cdd:COG3591 140 DC--------DTTGGSSGSPVLddsdGGGRVVGVHSAGGADRA 174
alphaLP-like cd21112
alpha-lytic protease (alpha-LP), a bacterial serine protease of the chymotrypsin family, and ...
207-246 1.88e-05

alpha-lytic protease (alpha-LP), a bacterial serine protease of the chymotrypsin family, and similar proteins; This family represents the catalytic domain of alpha-lytic protease (alpha-LP) and its closely-related homologs. Alpha-lytic protease (EC 3.4.21.12; also called alpha-lytic endopeptidase), originally isolated from the myxobacterium Lysobacter enzymogenes, belongs to the MEROPS peptidase family S1, subfamily S1E (streptogrisin A subfamily). It is synthesized as a pro-enzyme, thus having two domains; the N-terminal pro-domain acts as a foldase, required transiently for the correct folding of the protease domain, and also acts as a potent inhibitor of the mature enzyme, while the C-terminal domain catalyzes the cleavage of peptide bonds. Members of the alpha-lytic protease subfamily include Nocardiopsis alba protease (NAPase), a secreted chymotrypsin from the alkaliphile Cellulomonas bogoriensis, streptogrisins (SPG-A, SPG-B, SPG-C, and SPG-D), and Thermobifida fusca protease A (TFPA). These serine proteases have characteristic kinetic stability, exhibited by their extremely slow unfolding kinetics. The active site, characteristic of serine proteases, contains the catalytic triad consisting of serine acting as a nucleophile, aspartate as an electrophile, and histidine as a base, all required for activity. This model represents the C-terminal catalytic domain of alpha-lytic proteases.


Pssm-ID: 411050  Cd Length: 188  Bit Score: 44.22  E-value: 1.88e-05
                        10        20        30        40
                ....*....|....*....|....*....|....*....|..
gi 4502173  207 STCS--GDSGGPLVCNGVLQGITSWGSEPCALPERPSLYTKV 246
Cdd:cd21112 139 NACAepGDSGGPVFSGTQALGITSGGSGNCGSGGGTSYFQPV 180
Trypsin_2 pfam13365
Trypsin-like peptidase domain; This family includes trypsin-like peptidase domains.
52-226 3.12e-03

Trypsin-like peptidase domain; This family includes trypsin-like peptidase domains.


Pssm-ID: 433149 [Multi-domain]  Cd Length: 142  Bit Score: 37.02  E-value: 3.12e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502173     52 GVLVHPQ-WVLTAAHCIRnksvillgrhslfhPEDTGQVFQVSHSFPhplyDMSLLKNRFLRPgdDSSHDLMLLRLSEPA 130
Cdd:pfam13365   3 GFVVSSDgLVLTNAHVVD--------------DAEEAAVELVSVVLA----DGREYPATVVAR--DPDLDLALLRVSGDG 62
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502173    131 eltDAVKVMDL-PTQEPALGTTCYASGWGSiepeefltPKKLQCVDLHVISnDVCAQVHPQKVTKFMLCAGRWTGgkstc 209
Cdd:pfam13365  63 ---RGLPPLPLgDSEPLVGGERVYAVGYPL--------GGEKLSLSEGIVS-GVDEGRDGGDDGRVIQTDAALSP----- 125
                         170
                  ....*....|....*...
gi 4502173    210 sGDSGGPLV-CNGVLQGI 226
Cdd:pfam13365 126 -GSSGGPVFdADGRVVGI 142
 
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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