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Conserved domains on  [gi|767979198|ref|XP_011535778|]
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coagulation factor VII isoform X5 [Homo sapiens]

Protein Classification

FXa_inhibition and Tryp_SPc domain-containing protein( domain architecture ID 10630736)

FXa_inhibition and Tryp_SPc domain-containing protein

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 ...
111-347 5.48e-91

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: 272.61  E-value: 5.48e-91
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979198 111 IVGGKVCPKGECPWQVLLLVN-GAQLCGGTLINTIWVVSAAHCFDKiKNWRNLIAVLGEHDLSEHDGDEQSRRVAQVIIP 189
Cdd:cd00190    1 IVGGSEAKIGSFPWQVSLQYTgGRHFCGGSLISPRWVLTAAHCVYS-SAPSNYTVRLGSHDLSSNEGGGQVIKVKKVIVH 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979198 190 STYVPGTTNHDIALLRLHQPVVLTDHVVPLCLPErtfSERTLAFVRFSLVSGWGQLLDRGATALELMVLNVPRLMTQDCL 269
Cdd:cd00190   80 PNYNPSTYDNDIALLKLKRPVTLSDNVRPICLPS---SGYNLPAGTTCTVSGWGRTSEGGPLPDVLQEVNVPIVSNAECK 156
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767979198 270 QQSRKvgdSPNITEYMFCAGYSDGSKDSCKGDSGGPHATHYRGTWYLTGIVSWGQGCATVGHFGVYTRVSQYIEWLQK 347
Cdd:cd00190  157 RAYSY---GGTITDNMLCAGGLEGGKDACQGDSGGPLVCNDNGRGVLVGIVSWGSGCARPNYPGVYTRVSSYLDWIQK 231
FXa_inhibition pfam14670
Coagulation Factor Xa inhibitory site; This short domain on coagulation enzyme factor Xa is ...
49-85 2.03e-09

Coagulation Factor Xa inhibitory site; This short domain on coagulation enzyme factor Xa is found to be the target for a potent inhibitor of coagulation, TAK-442.


:

Pssm-ID: 464251 [Multi-domain]  Cd Length: 36  Bit Score: 52.24  E-value: 2.03e-09
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 767979198   49 CVNENGGCEQYCSDhTGTKRSCRCHEGYSLLADGVSC 85
Cdd:pfam14670   1 CSVNNGGCSHLCLN-TPGGYTCSCPEGYELQDDGRTC 36
 
Name Accession Description Interval E-value
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
111-347 5.48e-91

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: 272.61  E-value: 5.48e-91
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979198 111 IVGGKVCPKGECPWQVLLLVN-GAQLCGGTLINTIWVVSAAHCFDKiKNWRNLIAVLGEHDLSEHDGDEQSRRVAQVIIP 189
Cdd:cd00190    1 IVGGSEAKIGSFPWQVSLQYTgGRHFCGGSLISPRWVLTAAHCVYS-SAPSNYTVRLGSHDLSSNEGGGQVIKVKKVIVH 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979198 190 STYVPGTTNHDIALLRLHQPVVLTDHVVPLCLPErtfSERTLAFVRFSLVSGWGQLLDRGATALELMVLNVPRLMTQDCL 269
Cdd:cd00190   80 PNYNPSTYDNDIALLKLKRPVTLSDNVRPICLPS---SGYNLPAGTTCTVSGWGRTSEGGPLPDVLQEVNVPIVSNAECK 156
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767979198 270 QQSRKvgdSPNITEYMFCAGYSDGSKDSCKGDSGGPHATHYRGTWYLTGIVSWGQGCATVGHFGVYTRVSQYIEWLQK 347
Cdd:cd00190  157 RAYSY---GGTITDNMLCAGGLEGGKDACQGDSGGPLVCNDNGRGVLVGIVSWGSGCARPNYPGVYTRVSSYLDWIQK 231
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
110-344 1.31e-84

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: 256.07  E-value: 1.31e-84
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979198   110 RIVGGKVCPKGECPWQVLLLVNG-AQLCGGTLINTIWVVSAAHCFDKiKNWRNLIAVLGEHDLSEhDGDEQSRRVAQVII 188
Cdd:smart00020   1 RIVGGSEANIGSFPWQVSLQYGGgRHFCGGSLISPRWVLTAAHCVRG-SDPSNIRVRLGSHDLSS-GEEGQVIKVSKVII 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979198   189 PSTYVPGTTNHDIALLRLHQPVVLTDHVVPLCLPErtfSERTLAFVRFSLVSGWGQL-LDRGATALELMVLNVPRLMTQD 267
Cdd:smart00020  79 HPNYNPSTYDNDIALLKLKEPVTLSDNVRPICLPS---SNYNVPAGTTCTVSGWGRTsEGAGSLPDTLQEVNVPIVSNAT 155
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767979198   268 ClqqSRKVGDSPNITEYMFCAGYSDGSKDSCKGDSGGPHATHyRGTWYLTGIVSWGQGCATVGHFGVYTRVSQYIEW 344
Cdd:smart00020 156 C---RRAYSGGGAITDNMLCAGGLEGGKDACQGDSGGPLVCN-DGRWVLVGIVSWGSGCARPGKPGVYTRVSSYLDW 228
Trypsin pfam00089
Trypsin;
111-345 1.73e-58

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 188.81  E-value: 1.73e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979198  111 IVGGKVCPKGECPWQVLLLV-NGAQLCGGTLINTIWVVSAAHCFDKIKNWRnliAVLGEHDLSEHDGDEQSRRVAQVIIP 189
Cdd:pfam00089   1 IVGGDEAQPGSFPWQVSLQLsSGKHFCGGSLISENWVLTAAHCVSGASDVK---VVLGAHNIVLREGGEQKFDVEKIIVH 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979198  190 STYVPGTTNHDIALLRLHQPVVLTDHVVPLCLPE--RTFSERTLAFvrfslVSGWGQLLDRGaTALELMVLNVPRLMTQD 267
Cdd:pfam00089  78 PNYNPDTLDNDIALLKLESPVTLGDTVRPICLPDasSDLPVGTTCT-----VSGWGNTKTLG-PSDTLQEVTVPVVSRET 151
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767979198  268 CLQQSRkvgdsPNITEYMFCAGYsdGSKDSCKGDSGGPHATHYRgtwYLTGIVSWGQGCATVGHFGVYTRVSQYIEWL 345
Cdd:pfam00089 152 CRSAYG-----GTVTDTMICAGA--GGKDACQGDSGGPLVCSDG---ELIGIVSWGYGCASGNYPGVYTPVSSYLDWI 219
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
104-353 4.35e-58

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 189.09  E-value: 4.35e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979198 104 ASKPQGRIVGGKVCPKGECPWQVLLLVNG---AQLCGGTLINTIWVVSAAHCFDKIKNwRNLIAVLGEHDLSEHDGdeQS 180
Cdd:COG5640   24 AADAAPAIVGGTPATVGEYPWMVALQSSNgpsGQFCGGTLIAPRWVLTAAHCVDGDGP-SDLRVVIGSTDLSTSGG--TV 100
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979198 181 RRVAQVIIPSTYVPGTTNHDIALLRLHQPVvltDHVVPLCLPERTFSERTLAFVRfslVSGWGQLL-DRGATALELMVLN 259
Cdd:COG5640  101 VKVARIVVHPDYDPATPGNDIALLKLATPV---PGVAPAPLATSADAAAPGTPAT---VAGWGRTSeGPGSQSGTLRKAD 174
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979198 260 VPRLMTQDCLQQSRkvgdspNITEYMFCAGYSDGSKDSCKGDSGGPHATHYRGTWYLTGIVSWGQG-CATvGHFGVYTRV 338
Cdd:COG5640  175 VPVVSDATCAAYGG------FDGGTMLCAGYPEGGKDACQGDSGGPLVVKDGGGWVLVGVVSWGGGpCAA-GYPGVYTRV 247
                        250
                 ....*....|....*
gi 767979198 339 SQYIEWLQKLMRSEP 353
Cdd:COG5640  248 SAYRDWIKSTAGGLG 262
FXa_inhibition pfam14670
Coagulation Factor Xa inhibitory site; This short domain on coagulation enzyme factor Xa is ...
49-85 2.03e-09

Coagulation Factor Xa inhibitory site; This short domain on coagulation enzyme factor Xa is found to be the target for a potent inhibitor of coagulation, TAK-442.


Pssm-ID: 464251 [Multi-domain]  Cd Length: 36  Bit Score: 52.24  E-value: 2.03e-09
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 767979198   49 CVNENGGCEQYCSDhTGTKRSCRCHEGYSLLADGVSC 85
Cdd:pfam14670   1 CSVNNGGCSHLCLN-TPGGYTCSCPEGYELQDDGRTC 36
 
Name Accession Description Interval E-value
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
111-347 5.48e-91

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: 272.61  E-value: 5.48e-91
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979198 111 IVGGKVCPKGECPWQVLLLVN-GAQLCGGTLINTIWVVSAAHCFDKiKNWRNLIAVLGEHDLSEHDGDEQSRRVAQVIIP 189
Cdd:cd00190    1 IVGGSEAKIGSFPWQVSLQYTgGRHFCGGSLISPRWVLTAAHCVYS-SAPSNYTVRLGSHDLSSNEGGGQVIKVKKVIVH 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979198 190 STYVPGTTNHDIALLRLHQPVVLTDHVVPLCLPErtfSERTLAFVRFSLVSGWGQLLDRGATALELMVLNVPRLMTQDCL 269
Cdd:cd00190   80 PNYNPSTYDNDIALLKLKRPVTLSDNVRPICLPS---SGYNLPAGTTCTVSGWGRTSEGGPLPDVLQEVNVPIVSNAECK 156
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767979198 270 QQSRKvgdSPNITEYMFCAGYSDGSKDSCKGDSGGPHATHYRGTWYLTGIVSWGQGCATVGHFGVYTRVSQYIEWLQK 347
Cdd:cd00190  157 RAYSY---GGTITDNMLCAGGLEGGKDACQGDSGGPLVCNDNGRGVLVGIVSWGSGCARPNYPGVYTRVSSYLDWIQK 231
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
110-344 1.31e-84

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: 256.07  E-value: 1.31e-84
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979198   110 RIVGGKVCPKGECPWQVLLLVNG-AQLCGGTLINTIWVVSAAHCFDKiKNWRNLIAVLGEHDLSEhDGDEQSRRVAQVII 188
Cdd:smart00020   1 RIVGGSEANIGSFPWQVSLQYGGgRHFCGGSLISPRWVLTAAHCVRG-SDPSNIRVRLGSHDLSS-GEEGQVIKVSKVII 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979198   189 PSTYVPGTTNHDIALLRLHQPVVLTDHVVPLCLPErtfSERTLAFVRFSLVSGWGQL-LDRGATALELMVLNVPRLMTQD 267
Cdd:smart00020  79 HPNYNPSTYDNDIALLKLKEPVTLSDNVRPICLPS---SNYNVPAGTTCTVSGWGRTsEGAGSLPDTLQEVNVPIVSNAT 155
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767979198   268 ClqqSRKVGDSPNITEYMFCAGYSDGSKDSCKGDSGGPHATHyRGTWYLTGIVSWGQGCATVGHFGVYTRVSQYIEW 344
Cdd:smart00020 156 C---RRAYSGGGAITDNMLCAGGLEGGKDACQGDSGGPLVCN-DGRWVLVGIVSWGSGCARPGKPGVYTRVSSYLDW 228
Trypsin pfam00089
Trypsin;
111-345 1.73e-58

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 188.81  E-value: 1.73e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979198  111 IVGGKVCPKGECPWQVLLLV-NGAQLCGGTLINTIWVVSAAHCFDKIKNWRnliAVLGEHDLSEHDGDEQSRRVAQVIIP 189
Cdd:pfam00089   1 IVGGDEAQPGSFPWQVSLQLsSGKHFCGGSLISENWVLTAAHCVSGASDVK---VVLGAHNIVLREGGEQKFDVEKIIVH 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979198  190 STYVPGTTNHDIALLRLHQPVVLTDHVVPLCLPE--RTFSERTLAFvrfslVSGWGQLLDRGaTALELMVLNVPRLMTQD 267
Cdd:pfam00089  78 PNYNPDTLDNDIALLKLESPVTLGDTVRPICLPDasSDLPVGTTCT-----VSGWGNTKTLG-PSDTLQEVTVPVVSRET 151
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767979198  268 CLQQSRkvgdsPNITEYMFCAGYsdGSKDSCKGDSGGPHATHYRgtwYLTGIVSWGQGCATVGHFGVYTRVSQYIEWL 345
Cdd:pfam00089 152 CRSAYG-----GTVTDTMICAGA--GGKDACQGDSGGPLVCSDG---ELIGIVSWGYGCASGNYPGVYTPVSSYLDWI 219
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
104-353 4.35e-58

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 189.09  E-value: 4.35e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979198 104 ASKPQGRIVGGKVCPKGECPWQVLLLVNG---AQLCGGTLINTIWVVSAAHCFDKIKNwRNLIAVLGEHDLSEHDGdeQS 180
Cdd:COG5640   24 AADAAPAIVGGTPATVGEYPWMVALQSSNgpsGQFCGGTLIAPRWVLTAAHCVDGDGP-SDLRVVIGSTDLSTSGG--TV 100
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979198 181 RRVAQVIIPSTYVPGTTNHDIALLRLHQPVvltDHVVPLCLPERTFSERTLAFVRfslVSGWGQLL-DRGATALELMVLN 259
Cdd:COG5640  101 VKVARIVVHPDYDPATPGNDIALLKLATPV---PGVAPAPLATSADAAAPGTPAT---VAGWGRTSeGPGSQSGTLRKAD 174
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979198 260 VPRLMTQDCLQQSRkvgdspNITEYMFCAGYSDGSKDSCKGDSGGPHATHYRGTWYLTGIVSWGQG-CATvGHFGVYTRV 338
Cdd:COG5640  175 VPVVSDATCAAYGG------FDGGTMLCAGYPEGGKDACQGDSGGPLVVKDGGGWVLVGVVSWGGGpCAA-GYPGVYTRV 247
                        250
                 ....*....|....*
gi 767979198 339 SQYIEWLQKLMRSEP 353
Cdd:COG5640  248 SAYRDWIKSTAGGLG 262
eMpr COG3591
V8-like Glu-specific endopeptidase [Posttranslational modification, protein turnover, ...
127-351 1.53e-09

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


Pssm-ID: 442810 [Multi-domain]  Cd Length: 194  Bit Score: 56.99  E-value: 1.53e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979198 127 LLLVNGAQLCGGTLINTIWVVSAAHCF---DKIKNWRNLIAVLGehdlsEHDGDEQSRRVAQVIIPSTYVP-GTTNHDIA 202
Cdd:COG3591    5 LETDGGGGVCTGTLIGPNLVLTAGHCVydgAGGGWATNIVFVPG-----YNGGPYGTATATRFRVPPGWVAsGDAGYDYA 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979198 203 LLRLHQPVVLTDHVVPLCLPERTFSERTLAfvrfslVSGWGQllDRGATAlelmvlnvprlmtqdCLQQSRKVGDSPNIT 282
Cdd:COG3591   80 LLRLDEPLGDTTGWLGLAFNDAPLAGEPVT------IIGYPG--DRPKDL---------------SLDCSGRVTGVQGNR 136
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767979198 283 EYMFCagysdgskDSCKGDSGGPHATHYRGTWYLTGIVSWGQgcATVGHFGVYTRvSQYIEWLQKLMRS 351
Cdd:COG3591  137 LSYDC--------DTTGGSSGSPVLDDSDGGGRVVGVHSAGG--ADRANTGVRLT-SAIVAALRAWASA 194
FXa_inhibition pfam14670
Coagulation Factor Xa inhibitory site; This short domain on coagulation enzyme factor Xa is ...
49-85 2.03e-09

Coagulation Factor Xa inhibitory site; This short domain on coagulation enzyme factor Xa is found to be the target for a potent inhibitor of coagulation, TAK-442.


Pssm-ID: 464251 [Multi-domain]  Cd Length: 36  Bit Score: 52.24  E-value: 2.03e-09
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 767979198   49 CVNENGGCEQYCSDhTGTKRSCRCHEGYSLLADGVSC 85
Cdd:pfam14670   1 CSVNNGGCSHLCLN-TPGGYTCSCPEGYELQDDGRTC 36
DUF1986 pfam09342
Domain of unknown function (DUF1986); This domain is found in serine proteases and is ...
122-223 3.57e-05

Domain of unknown function (DUF1986); This domain is found in serine proteases and is predicted to contain disulphide bonds.


Pssm-ID: 286432  Cd Length: 116  Bit Score: 42.53  E-value: 3.57e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979198  122 CPWQVLLLVNGAQLCGGTLINTIWVVSAAHCFDKIKNWRNLIAVL---GEHDLSEHDGDEQSRRVAQViipsTYVPGTtn 198
Cdd:pfam09342   1 WPWIAKVYLDGNMICSGVLIDASWVIVSGSCLRDTNLRHQYISVVlggAKTLKSIEGPYEQIVRVDCR----HDIPES-- 74
                          90       100
                  ....*....|....*....|....*
gi 767979198  199 hDIALLRLHQPVVLTDHVVPLCLPE 223
Cdd:pfam09342  75 -EISLLHLASPASFSNHVLPTFVPE 98
 
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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