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Conserved domains on  [gi|7304853|ref|NP_038483|]
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acrosin isoform 1 precursor [Mus musculus]

Protein Classification

S1 family serine peptidase( domain architecture ID 12184331)

S1 family trypsin-like serine peptidase such as snake venom serine proteases and trypsin, which preferentially cleaves peptide bonds after arginine and lysine residues

CATH:  2.40.10.10
EC:  3.4.-.-
Gene Ontology:  GO:0008236|GO:0006508
MEROPS:  S1
SCOP:  3000114

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
42-286 8.37e-99

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: 294.97  E-value: 8.37e-99
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7304853      42 RIVSGQSAQLGAWPWMVSLQIftshnSRRYHACGGSLLNSHWVLTAAHCFDNKKKvYDWRLVFGAQEIEYGrnkpvkEPQ 121
Cdd:smart00020   1 RIVGGSEANIGSFPWQVSLQY-----GGGRHFCGGSLISPRWVLTAAHCVRGSDP-SNIRVRLGSHDLSSG------EEG 68
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7304853     122 QERYVQKIVIHEKYNVVTEGNDIALLKITPPVTCGNFIGPCCLPHFKAGPPQiPHTCYVTGWGYIKEKAPRPSPVLMEAR 201
Cdd:smart00020  69 QVIKVSKVIIHPNYNPSTYDNDIALLKLKEPVTLSDNVRPICLPSSNYNVPA-GTTCTVSGWGRTSEGAGSLPDTLQEVN 147
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7304853     202 VDLIDLDLCNSTQWYNGRVTSTNVCAGYPEGKIDTCQGDSGGPLMCRDNVdspFVVVGITSWGVGCARAKRPGVYTATWD 281
Cdd:smart00020 148 VPIVSNATCRRAYSGGGAITDNMLCAGGLEGGKDACQGDSGGPLVCNDGR---WVLVGIVSWGSGCARPGKPGVYTRVSS 224

                   ....*
gi 7304853     282 YLDWI 286
Cdd:smart00020 225 YLDWI 229
 
Name Accession Description Interval E-value
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
42-286 8.37e-99

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: 294.97  E-value: 8.37e-99
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7304853      42 RIVSGQSAQLGAWPWMVSLQIftshnSRRYHACGGSLLNSHWVLTAAHCFDNKKKvYDWRLVFGAQEIEYGrnkpvkEPQ 121
Cdd:smart00020   1 RIVGGSEANIGSFPWQVSLQY-----GGGRHFCGGSLISPRWVLTAAHCVRGSDP-SNIRVRLGSHDLSSG------EEG 68
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7304853     122 QERYVQKIVIHEKYNVVTEGNDIALLKITPPVTCGNFIGPCCLPHFKAGPPQiPHTCYVTGWGYIKEKAPRPSPVLMEAR 201
Cdd:smart00020  69 QVIKVSKVIIHPNYNPSTYDNDIALLKLKEPVTLSDNVRPICLPSSNYNVPA-GTTCTVSGWGRTSEGAGSLPDTLQEVN 147
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7304853     202 VDLIDLDLCNSTQWYNGRVTSTNVCAGYPEGKIDTCQGDSGGPLMCRDNVdspFVVVGITSWGVGCARAKRPGVYTATWD 281
Cdd:smart00020 148 VPIVSNATCRRAYSGGGAITDNMLCAGGLEGGKDACQGDSGGPLVCNDGR---WVLVGIVSWGSGCARPGKPGVYTRVSS 224

                   ....*
gi 7304853     282 YLDWI 286
Cdd:smart00020 225 YLDWI 229
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
43-289 4.60e-93

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: 280.32  E-value: 4.60e-93
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7304853   43 IVSGQSAQLGAWPWMVSLQiftshNSRRYHACGGSLLNSHWVLTAAHCFDNKKkVYDWRLVFGaqeiEYGRNKPvKEPQQ 122
Cdd:cd00190   1 IVGGSEAKIGSFPWQVSLQ-----YTGGRHFCGGSLISPRWVLTAAHCVYSSA-PSNYTVRLG----SHDLSSN-EGGGQ 69
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7304853  123 ERYVQKIVIHEKYNVVTEGNDIALLKITPPVTCGNFIGPCCLPHFKAGPPQiPHTCYVTGWGYIKEKAPRPSpVLMEARV 202
Cdd:cd00190  70 VIKVKKVIVHPNYNPSTYDNDIALLKLKRPVTLSDNVRPICLPSSGYNLPA-GTTCTVSGWGRTSEGGPLPD-VLQEVNV 147
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7304853  203 DLIDLDLCNSTQWYNGRVTSTNVCAGYPEGKIDTCQGDSGGPLMCRDNvdSPFVVVGITSWGVGCARAKRPGVYTATWDY 282
Cdd:cd00190 148 PIVSNAECKRAYSYGGTITDNMLCAGGLEGGKDACQGDSGGPLVCNDN--GRGVLVGIVSWGSGCARPNYPGVYTRVSSY 225

                ....*..
gi 7304853  283 LDWIASK 289
Cdd:cd00190 226 LDWIQKT 232
Trypsin pfam00089
Trypsin;
43-286 2.24e-79

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 244.66  E-value: 2.24e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7304853     43 IVSGQSAQLGAWPWMVSLQIftshnSRRYHACGGSLLNSHWVLTAAHCFDNKKkvyDWRLVFGAQEIEYGRnkpvkEPQQ 122
Cdd:pfam00089   1 IVGGDEAQPGSFPWQVSLQL-----SSGKHFCGGSLISENWVLTAAHCVSGAS---DVKVVLGAHNIVLRE-----GGEQ 67
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7304853    123 ERYVQKIVIHEKYNVVTEGNDIALLKITPPVTCGNFIGPCCLPHFKAgPPQIPHTCYVTGWGYIKEKapRPSPVLMEARV 202
Cdd:pfam00089  68 KFDVEKIIVHPNYNPDTLDNDIALLKLESPVTLGDTVRPICLPDASS-DLPVGTTCTVSGWGNTKTL--GPSDTLQEVTV 144
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7304853    203 DLIDLDLCNStqWYNGRVTSTNVCAGYpeGKIDTCQGDSGGPLMCRDNvdspfVVVGITSWGVGCARAKRPGVYTATWDY 282
Cdd:pfam00089 145 PVVSRETCRS--AYGGTVTDTMICAGA--GGKDACQGDSGGPLVCSDG-----ELIGIVSWGYGCASGNYPGVYTPVSSY 215

                  ....
gi 7304853    283 LDWI 286
Cdd:pfam00089 216 LDWI 219
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
37-291 1.07e-70

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 224.14  E-value: 1.07e-70
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7304853   37 SQAGTRIVSGQSAQLGAWPWMVSLQiftSHNSRRYHACGGSLLNSHWVLTAAHCFDNKKKVyDWRLVfgaqeieYGRNKP 116
Cdd:COG5640  25 ADAAPAIVGGTPATVGEYPWMVALQ---SSNGPSGQFCGGTLIAPRWVLTAAHCVDGDGPS-DLRVV-------IGSTDL 93
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7304853  117 VKEPQQERYVQKIVIHEKYNVVTEGNDIALLKITPPVTcgnFIGPCCLP----HFKAGPPQIphtcyVTGWGYIKEKAPR 192
Cdd:COG5640  94 STSGGTVVKVARIVVHPDYDPATPGNDIALLKLATPVP---GVAPAPLAtsadAAAPGTPAT-----VAGWGRTSEGPGS 165
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7304853  193 PSPVLMEARVDLIDLDLCNStqwYNGRVTSTNVCAGYPEGKIDTCQGDSGGPLMcrDNVDSPFVVVGITSWGVGCARAKR 272
Cdd:COG5640 166 QSGTLRKADVPVVSDATCAA---YGGFDGGTMLCAGYPEGGKDACQGDSGGPLV--VKDGGGWVLVGVVSWGGGPCAAGY 240
                       250
                ....*....|....*....
gi 7304853  273 PGVYTATWDYLDWIASKIG 291
Cdd:COG5640 241 PGVYTRVSAYRDWIKSTAG 259
 
Name Accession Description Interval E-value
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
42-286 8.37e-99

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: 294.97  E-value: 8.37e-99
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7304853      42 RIVSGQSAQLGAWPWMVSLQIftshnSRRYHACGGSLLNSHWVLTAAHCFDNKKKvYDWRLVFGAQEIEYGrnkpvkEPQ 121
Cdd:smart00020   1 RIVGGSEANIGSFPWQVSLQY-----GGGRHFCGGSLISPRWVLTAAHCVRGSDP-SNIRVRLGSHDLSSG------EEG 68
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7304853     122 QERYVQKIVIHEKYNVVTEGNDIALLKITPPVTCGNFIGPCCLPHFKAGPPQiPHTCYVTGWGYIKEKAPRPSPVLMEAR 201
Cdd:smart00020  69 QVIKVSKVIIHPNYNPSTYDNDIALLKLKEPVTLSDNVRPICLPSSNYNVPA-GTTCTVSGWGRTSEGAGSLPDTLQEVN 147
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7304853     202 VDLIDLDLCNSTQWYNGRVTSTNVCAGYPEGKIDTCQGDSGGPLMCRDNVdspFVVVGITSWGVGCARAKRPGVYTATWD 281
Cdd:smart00020 148 VPIVSNATCRRAYSGGGAITDNMLCAGGLEGGKDACQGDSGGPLVCNDGR---WVLVGIVSWGSGCARPGKPGVYTRVSS 224

                   ....*
gi 7304853     282 YLDWI 286
Cdd:smart00020 225 YLDWI 229
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
43-289 4.60e-93

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: 280.32  E-value: 4.60e-93
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7304853   43 IVSGQSAQLGAWPWMVSLQiftshNSRRYHACGGSLLNSHWVLTAAHCFDNKKkVYDWRLVFGaqeiEYGRNKPvKEPQQ 122
Cdd:cd00190   1 IVGGSEAKIGSFPWQVSLQ-----YTGGRHFCGGSLISPRWVLTAAHCVYSSA-PSNYTVRLG----SHDLSSN-EGGGQ 69
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7304853  123 ERYVQKIVIHEKYNVVTEGNDIALLKITPPVTCGNFIGPCCLPHFKAGPPQiPHTCYVTGWGYIKEKAPRPSpVLMEARV 202
Cdd:cd00190  70 VIKVKKVIVHPNYNPSTYDNDIALLKLKRPVTLSDNVRPICLPSSGYNLPA-GTTCTVSGWGRTSEGGPLPD-VLQEVNV 147
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7304853  203 DLIDLDLCNSTQWYNGRVTSTNVCAGYPEGKIDTCQGDSGGPLMCRDNvdSPFVVVGITSWGVGCARAKRPGVYTATWDY 282
Cdd:cd00190 148 PIVSNAECKRAYSYGGTITDNMLCAGGLEGGKDACQGDSGGPLVCNDN--GRGVLVGIVSWGSGCARPNYPGVYTRVSSY 225

                ....*..
gi 7304853  283 LDWIASK 289
Cdd:cd00190 226 LDWIQKT 232
Trypsin pfam00089
Trypsin;
43-286 2.24e-79

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 244.66  E-value: 2.24e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7304853     43 IVSGQSAQLGAWPWMVSLQIftshnSRRYHACGGSLLNSHWVLTAAHCFDNKKkvyDWRLVFGAQEIEYGRnkpvkEPQQ 122
Cdd:pfam00089   1 IVGGDEAQPGSFPWQVSLQL-----SSGKHFCGGSLISENWVLTAAHCVSGAS---DVKVVLGAHNIVLRE-----GGEQ 67
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7304853    123 ERYVQKIVIHEKYNVVTEGNDIALLKITPPVTCGNFIGPCCLPHFKAgPPQIPHTCYVTGWGYIKEKapRPSPVLMEARV 202
Cdd:pfam00089  68 KFDVEKIIVHPNYNPDTLDNDIALLKLESPVTLGDTVRPICLPDASS-DLPVGTTCTVSGWGNTKTL--GPSDTLQEVTV 144
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7304853    203 DLIDLDLCNStqWYNGRVTSTNVCAGYpeGKIDTCQGDSGGPLMCRDNvdspfVVVGITSWGVGCARAKRPGVYTATWDY 282
Cdd:pfam00089 145 PVVSRETCRS--AYGGTVTDTMICAGA--GGKDACQGDSGGPLVCSDG-----ELIGIVSWGYGCASGNYPGVYTPVSSY 215

                  ....
gi 7304853    283 LDWI 286
Cdd:pfam00089 216 LDWI 219
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
37-291 1.07e-70

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 224.14  E-value: 1.07e-70
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7304853   37 SQAGTRIVSGQSAQLGAWPWMVSLQiftSHNSRRYHACGGSLLNSHWVLTAAHCFDNKKKVyDWRLVfgaqeieYGRNKP 116
Cdd:COG5640  25 ADAAPAIVGGTPATVGEYPWMVALQ---SSNGPSGQFCGGTLIAPRWVLTAAHCVDGDGPS-DLRVV-------IGSTDL 93
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7304853  117 VKEPQQERYVQKIVIHEKYNVVTEGNDIALLKITPPVTcgnFIGPCCLP----HFKAGPPQIphtcyVTGWGYIKEKAPR 192
Cdd:COG5640  94 STSGGTVVKVARIVVHPDYDPATPGNDIALLKLATPVP---GVAPAPLAtsadAAAPGTPAT-----VAGWGRTSEGPGS 165
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7304853  193 PSPVLMEARVDLIDLDLCNStqwYNGRVTSTNVCAGYPEGKIDTCQGDSGGPLMcrDNVDSPFVVVGITSWGVGCARAKR 272
Cdd:COG5640 166 QSGTLRKADVPVVSDATCAA---YGGFDGGTMLCAGYPEGGKDACQGDSGGPLV--VKDGGGWVLVGVVSWGGGPCAAGY 240
                       250
                ....*....|....*....
gi 7304853  273 PGVYTATWDYLDWIASKIG 291
Cdd:COG5640 241 PGVYTRVSAYRDWIKSTAG 259
eMpr COG3591
V8-like Glu-specific endopeptidase [Posttranslational modification, protein turnover, ...
74-266 9.36e-13

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


Pssm-ID: 442810 [Multi-domain]  Cd Length: 194  Bit Score: 66.62  E-value: 9.36e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7304853   74 CGGSLLNSHWVLTAAHCFDNKKK---VYDWRLVFGAQEIEYGRNKpvkepqqeryVQKIVIHEKYNVVT-EGNDIALLKI 149
Cdd:COG3591  14 CTGTLIGPNLVLTAGHCVYDGAGggwATNIVFVPGYNGGPYGTAT----------ATRFRVPPGWVASGdAGYDYALLRL 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7304853  150 TPPVtcGNFIGPccLPHFKAGPPQIPHTCYVTGWGYIKEKAPrpspvlmearvdlidldlcnsTQWYNGRVTSTNvcAGY 229
Cdd:COG3591  84 DEPL--GDTTGW--LGLAFNDAPLAGEPVTIIGYPGDRPKDL---------------------SLDCSGRVTGVQ--GNR 136
                       170       180       190
                ....*....|....*....|....*....|....*..
gi 7304853  230 PEGKIDTCQGDSGGPLMcrDNVDSPFVVVGITSWGVG 266
Cdd:COG3591 137 LSYDCDTTGGSSGSPVL--DDSDGGGRVVGVHSAGGA 171
alphaLP-like cd21112
alpha-lytic protease (alpha-LP), a bacterial serine protease of the chymotrypsin family, and ...
210-285 1.62e-06

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: 48.46  E-value: 1.62e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7304853  210 CNS---TQWYNGRVTSTNVCAGYPEGKI------DTC--QGDSGGPLMcrdnvdSPFVVVGITSWGVG-CARAKRPGVYT 277
Cdd:cd21112 105 CKSgrtTGWTCGTVTAVNVTVNYPGGTVtgltrtNACaePGDSGGPVF------SGTQALGITSGGSGnCGSGGGTSYFQ 178

                ....*...
gi 7304853  278 ATWDYLDW 285
Cdd:cd21112 179 PVNPVLSA 186
 
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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