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Conserved domains on  [gi|30722357|emb|CAD91168|]
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hypothetical protein [Homo sapiens]

Protein Classification

SEA and Tryp_SPc domain-containing protein( domain architecture ID 10475933)

SEA 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 ...
185-413 3.59e-98

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: 292.64  E-value: 3.59e-98
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30722357 185 IVNGKSSLEGAWPWQASMQWK-GRHYCGASLISSRWLLSAAHCFAKKNNSkDWTVNFGV----VVNKPYMTRKVQNIIFH 259
Cdd:cd00190   1 IVGGSEAKIGSFPWQVSLQYTgGRHFCGGSLISPRWVLTAAHCVYSSAPS-NYTVRLGShdlsSNEGGGQVIKVKKVIVH 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30722357 260 ENYSSPGLHDDIALVQLAEEVSFTEYIRKICLPEAKMKLSENDNVVVTGWGTLYMNGSFPVILQEAFLKIIDNKICNASY 339
Cdd:cd00190  80 PNYNPSTYDNDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRTSEGGPLPDVLQEVNVPIVSNAECKRAY 159
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 30722357 340 AYSGFVTDSMLCAGFMSGEADACQNDSGGPLAYpDSRNIWHLVGIVSWGDGCGKKNKPGVYTRVTSYRNWITSK 413
Cdd:cd00190 160 SYGGTITDNMLCAGGLEGGKDACQGDSGGPLVC-NDNGRGVLVGIVSWGSGCARPNYPGVYTRVSSYLDWIQKT 232
SEA pfam01390
SEA domain; Domain found in Sea urchin sperm protein, Enterokinase, Agrin (SEA). Proposed ...
45-142 1.10e-21

SEA domain; Domain found in Sea urchin sperm protein, Enterokinase, Agrin (SEA). Proposed function of regulating or binding carbohydrate side chains. Recently a proteolytic activity has been shown for a SEA domain.


:

Pssm-ID: 460188  Cd Length: 100  Bit Score: 88.83  E-value: 1.10e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30722357    45 YYYQGDFHISGVTYNDNCENAASQASTNLSKDIETKMLNAFQNSSIYKEYVKSEVIKLLPNANGSNVQLQLKFKFPPAE- 123
Cdd:pfam01390   1 QYYTGSFKITNLQYTPDLGNPSSQEFKSLSRRIESLLNELFRNSSLRKQYIKSHVLRLRPDGGSVVVDVVLVFRFPSTEp 80
                          90
                  ....*....|....*....
gi 30722357   124 GVSMRTKIKAKLHQMLKNN 142
Cdd:pfam01390  81 ALDREKLIEEILRQTLNNT 99
 
Name Accession Description Interval E-value
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
185-413 3.59e-98

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: 292.64  E-value: 3.59e-98
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30722357 185 IVNGKSSLEGAWPWQASMQWK-GRHYCGASLISSRWLLSAAHCFAKKNNSkDWTVNFGV----VVNKPYMTRKVQNIIFH 259
Cdd:cd00190   1 IVGGSEAKIGSFPWQVSLQYTgGRHFCGGSLISPRWVLTAAHCVYSSAPS-NYTVRLGShdlsSNEGGGQVIKVKKVIVH 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30722357 260 ENYSSPGLHDDIALVQLAEEVSFTEYIRKICLPEAKMKLSENDNVVVTGWGTLYMNGSFPVILQEAFLKIIDNKICNASY 339
Cdd:cd00190  80 PNYNPSTYDNDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRTSEGGPLPDVLQEVNVPIVSNAECKRAY 159
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 30722357 340 AYSGFVTDSMLCAGFMSGEADACQNDSGGPLAYpDSRNIWHLVGIVSWGDGCGKKNKPGVYTRVTSYRNWITSK 413
Cdd:cd00190 160 SYGGTITDNMLCAGGLEGGKDACQGDSGGPLVC-NDNGRGVLVGIVSWGSGCARPNYPGVYTRVSSYLDWIQKT 232
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
184-410 2.34e-97

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: 290.35  E-value: 2.34e-97
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30722357    184 KIVNGKSSLEGAWPWQASMQWKG-RHYCGASLISSRWLLSAAHCFAKKNNSkDWTVNFG---VVVNKPYMTRKVQNIIFH 259
Cdd:smart00020   1 RIVGGSEANIGSFPWQVSLQYGGgRHFCGGSLISPRWVLTAAHCVRGSDPS-NIRVRLGshdLSSGEEGQVIKVSKVIIH 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30722357    260 ENYSSPGLHDDIALVQLAEEVSFTEYIRKICLPEAKMKLSENDNVVVTGWG-TLYMNGSFPVILQEAFLKIIDNKICNAS 338
Cdd:smart00020  80 PNYNPSTYDNDIALLKLKEPVTLSDNVRPICLPSSNYNVPAGTTCTVSGWGrTSEGAGSLPDTLQEVNVPIVSNATCRRA 159
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 30722357    339 YAYSGFVTDSMLCAGFMSGEADACQNDSGGPLAYPDSRniWHLVGIVSWGDGCGKKNKPGVYTRVTSYRNWI 410
Cdd:smart00020 160 YSGGGAITDNMLCAGGLEGGKDACQGDSGGPLVCNDGR--WVLVGIVSWGSGCARPGKPGVYTRVSSYLDWI 229
Trypsin pfam00089
Trypsin;
185-410 2.37e-72

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 226.17  E-value: 2.37e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30722357   185 IVNGKSSLEGAWPWQASMQWK-GRHYCGASLISSRWLLSAAHCFAkknNSKDWTVNFG----VVVNKPYMTRKVQNIIFH 259
Cdd:pfam00089   1 IVGGDEAQPGSFPWQVSLQLSsGKHFCGGSLISENWVLTAAHCVS---GASDVKVVLGahniVLREGGEQKFDVEKIIVH 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30722357   260 ENYSSPGLHDDIALVQLAEEVSFTEYIRKICLPEAKMKLSENDNVVVTGWGTLYMNGSfPVILQEAFLKIIDNKICNAsy 339
Cdd:pfam00089  78 PNYNPDTLDNDIALLKLESPVTLGDTVRPICLPDASSDLPVGTTCTVSGWGNTKTLGP-SDTLQEVTVPVVSRETCRS-- 154
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 30722357   340 AYSGFVTDSMLCAGFmsGEADACQNDSGGPLAYPDSRniwhLVGIVSWGDGCGKKNKPGVYTRVTSYRNWI 410
Cdd:pfam00089 155 AYGGTVTDTMICAGA--GGKDACQGDSGGPLVCSDGE----LIGIVSWGYGCASGNYPGVYTPVSSYLDWI 219
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
184-415 3.60e-70

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 222.22  E-value: 3.60e-70
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30722357 184 KIVNGKSSLEGAWPWQASMQWKG---RHYCGASLISSRWLLSAAHCFAKKNNSkDWTVNFGVV--VNKPYMTRKVQNIIF 258
Cdd:COG5640  30 AIVGGTPATVGEYPWMVALQSSNgpsGQFCGGTLIAPRWVLTAAHCVDGDGPS-DLRVVIGSTdlSTSGGTVVKVARIVV 108
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30722357 259 HENYSSPGLHDDIALVQLAEEVSFTEYIRkicLPEAKMKLSENDNVVVTGWGTLYMN-GSFPVILQEAFLKIIDNKICNA 337
Cdd:COG5640 109 HPDYDPATPGNDIALLKLATPVPGVAPAP---LATSADAAAPGTPATVAGWGRTSEGpGSQSGTLRKADVPVVSDATCAA 185
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 30722357 338 syaYSGFVTDSMLCAGFMSGEADACQNDSGGPLAYPDSRNiWHLVGIVSWGDGCGKKNKPGVYTRVTSYRNWITSKTG 415
Cdd:COG5640 186 ---YGGFDGGTMLCAGYPEGGKDACQGDSGGPLVVKDGGG-WVLVGVVSWGGGPCAAGYPGVYTRVSAYRDWIKSTAG 259
SEA pfam01390
SEA domain; Domain found in Sea urchin sperm protein, Enterokinase, Agrin (SEA). Proposed ...
45-142 1.10e-21

SEA domain; Domain found in Sea urchin sperm protein, Enterokinase, Agrin (SEA). Proposed function of regulating or binding carbohydrate side chains. Recently a proteolytic activity has been shown for a SEA domain.


Pssm-ID: 460188  Cd Length: 100  Bit Score: 88.83  E-value: 1.10e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30722357    45 YYYQGDFHISGVTYNDNCENAASQASTNLSKDIETKMLNAFQNSSIYKEYVKSEVIKLLPNANGSNVQLQLKFKFPPAE- 123
Cdd:pfam01390   1 QYYTGSFKITNLQYTPDLGNPSSQEFKSLSRRIESLLNELFRNSSLRKQYIKSHVLRLRPDGGSVVVDVVLVFRFPSTEp 80
                          90
                  ....*....|....*....
gi 30722357   124 GVSMRTKIKAKLHQMLKNN 142
Cdd:pfam01390  81 ALDREKLIEEILRQTLNNT 99
SEA smart00200
Domain found in sea urchin sperm protein, enterokinase, agrin; Proposed function of regulating ...
51-120 2.02e-04

Domain found in sea urchin sperm protein, enterokinase, agrin; Proposed function of regulating or binding carbohydrate sidechains.


Pssm-ID: 214554  Cd Length: 121  Bit Score: 40.86  E-value: 2.02e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 30722357     51 FHISGVTYNDNCENAASQASTNLSKDIETKMLNAFQNSSIYKEYVKSEVIKLlpnANGS-NVQLQLKFKFP 120
Cdd:smart00200  14 VEGENLQYSPSLEDPSSEEYQELVRDVEKLLEQIYGKTDLKPDFVGTEVIEF---RNGSvVVDLGLLFNEG 81
 
Name Accession Description Interval E-value
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
185-413 3.59e-98

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: 292.64  E-value: 3.59e-98
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30722357 185 IVNGKSSLEGAWPWQASMQWK-GRHYCGASLISSRWLLSAAHCFAKKNNSkDWTVNFGV----VVNKPYMTRKVQNIIFH 259
Cdd:cd00190   1 IVGGSEAKIGSFPWQVSLQYTgGRHFCGGSLISPRWVLTAAHCVYSSAPS-NYTVRLGShdlsSNEGGGQVIKVKKVIVH 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30722357 260 ENYSSPGLHDDIALVQLAEEVSFTEYIRKICLPEAKMKLSENDNVVVTGWGTLYMNGSFPVILQEAFLKIIDNKICNASY 339
Cdd:cd00190  80 PNYNPSTYDNDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRTSEGGPLPDVLQEVNVPIVSNAECKRAY 159
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 30722357 340 AYSGFVTDSMLCAGFMSGEADACQNDSGGPLAYpDSRNIWHLVGIVSWGDGCGKKNKPGVYTRVTSYRNWITSK 413
Cdd:cd00190 160 SYGGTITDNMLCAGGLEGGKDACQGDSGGPLVC-NDNGRGVLVGIVSWGSGCARPNYPGVYTRVSSYLDWIQKT 232
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
184-410 2.34e-97

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: 290.35  E-value: 2.34e-97
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30722357    184 KIVNGKSSLEGAWPWQASMQWKG-RHYCGASLISSRWLLSAAHCFAKKNNSkDWTVNFG---VVVNKPYMTRKVQNIIFH 259
Cdd:smart00020   1 RIVGGSEANIGSFPWQVSLQYGGgRHFCGGSLISPRWVLTAAHCVRGSDPS-NIRVRLGshdLSSGEEGQVIKVSKVIIH 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30722357    260 ENYSSPGLHDDIALVQLAEEVSFTEYIRKICLPEAKMKLSENDNVVVTGWG-TLYMNGSFPVILQEAFLKIIDNKICNAS 338
Cdd:smart00020  80 PNYNPSTYDNDIALLKLKEPVTLSDNVRPICLPSSNYNVPAGTTCTVSGWGrTSEGAGSLPDTLQEVNVPIVSNATCRRA 159
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 30722357    339 YAYSGFVTDSMLCAGFMSGEADACQNDSGGPLAYPDSRniWHLVGIVSWGDGCGKKNKPGVYTRVTSYRNWI 410
Cdd:smart00020 160 YSGGGAITDNMLCAGGLEGGKDACQGDSGGPLVCNDGR--WVLVGIVSWGSGCARPGKPGVYTRVSSYLDWI 229
Trypsin pfam00089
Trypsin;
185-410 2.37e-72

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 226.17  E-value: 2.37e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30722357   185 IVNGKSSLEGAWPWQASMQWK-GRHYCGASLISSRWLLSAAHCFAkknNSKDWTVNFG----VVVNKPYMTRKVQNIIFH 259
Cdd:pfam00089   1 IVGGDEAQPGSFPWQVSLQLSsGKHFCGGSLISENWVLTAAHCVS---GASDVKVVLGahniVLREGGEQKFDVEKIIVH 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30722357   260 ENYSSPGLHDDIALVQLAEEVSFTEYIRKICLPEAKMKLSENDNVVVTGWGTLYMNGSfPVILQEAFLKIIDNKICNAsy 339
Cdd:pfam00089  78 PNYNPDTLDNDIALLKLESPVTLGDTVRPICLPDASSDLPVGTTCTVSGWGNTKTLGP-SDTLQEVTVPVVSRETCRS-- 154
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 30722357   340 AYSGFVTDSMLCAGFmsGEADACQNDSGGPLAYPDSRniwhLVGIVSWGDGCGKKNKPGVYTRVTSYRNWI 410
Cdd:pfam00089 155 AYGGTVTDTMICAGA--GGKDACQGDSGGPLVCSDGE----LIGIVSWGYGCASGNYPGVYTPVSSYLDWI 219
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
184-415 3.60e-70

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 222.22  E-value: 3.60e-70
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30722357 184 KIVNGKSSLEGAWPWQASMQWKG---RHYCGASLISSRWLLSAAHCFAKKNNSkDWTVNFGVV--VNKPYMTRKVQNIIF 258
Cdd:COG5640  30 AIVGGTPATVGEYPWMVALQSSNgpsGQFCGGTLIAPRWVLTAAHCVDGDGPS-DLRVVIGSTdlSTSGGTVVKVARIVV 108
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30722357 259 HENYSSPGLHDDIALVQLAEEVSFTEYIRkicLPEAKMKLSENDNVVVTGWGTLYMN-GSFPVILQEAFLKIIDNKICNA 337
Cdd:COG5640 109 HPDYDPATPGNDIALLKLATPVPGVAPAP---LATSADAAAPGTPATVAGWGRTSEGpGSQSGTLRKADVPVVSDATCAA 185
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 30722357 338 syaYSGFVTDSMLCAGFMSGEADACQNDSGGPLAYPDSRNiWHLVGIVSWGDGCGKKNKPGVYTRVTSYRNWITSKTG 415
Cdd:COG5640 186 ---YGGFDGGTMLCAGYPEGGKDACQGDSGGPLVVKDGGG-WVLVGVVSWGGGPCAAGYPGVYTRVSAYRDWIKSTAG 259
SEA pfam01390
SEA domain; Domain found in Sea urchin sperm protein, Enterokinase, Agrin (SEA). Proposed ...
45-142 1.10e-21

SEA domain; Domain found in Sea urchin sperm protein, Enterokinase, Agrin (SEA). Proposed function of regulating or binding carbohydrate side chains. Recently a proteolytic activity has been shown for a SEA domain.


Pssm-ID: 460188  Cd Length: 100  Bit Score: 88.83  E-value: 1.10e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30722357    45 YYYQGDFHISGVTYNDNCENAASQASTNLSKDIETKMLNAFQNSSIYKEYVKSEVIKLLPNANGSNVQLQLKFKFPPAE- 123
Cdd:pfam01390   1 QYYTGSFKITNLQYTPDLGNPSSQEFKSLSRRIESLLNELFRNSSLRKQYIKSHVLRLRPDGGSVVVDVVLVFRFPSTEp 80
                          90
                  ....*....|....*....
gi 30722357   124 GVSMRTKIKAKLHQMLKNN 142
Cdd:pfam01390  81 ALDREKLIEEILRQTLNNT 99
SEA smart00200
Domain found in sea urchin sperm protein, enterokinase, agrin; Proposed function of regulating ...
51-120 2.02e-04

Domain found in sea urchin sperm protein, enterokinase, agrin; Proposed function of regulating or binding carbohydrate sidechains.


Pssm-ID: 214554  Cd Length: 121  Bit Score: 40.86  E-value: 2.02e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 30722357     51 FHISGVTYNDNCENAASQASTNLSKDIETKMLNAFQNSSIYKEYVKSEVIKLlpnANGS-NVQLQLKFKFP 120
Cdd:smart00200  14 VEGENLQYSPSLEDPSSEEYQELVRDVEKLLEQIYGKTDLKPDFVGTEVIEF---RNGSvVVDLGLLFNEG 81
 
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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