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Conserved domains on  [gi|1790135623|ref|WP_158498224|]
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trypsin-like serine protease [Methanospirillum hungatei]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
24-229 1.14e-24

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


:

Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 103.19  E-value: 1.14e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1790135623  24 GTAVQDGELEAVGEVIGSGG-----CTGTLIADNLVLSAAHCFcngKSNCVNQGQFILRNVRTVADPNNRRNVTftgKVR 98
Cdd:COG5640    34 GTPATVGEYPWMVALQSSNGpsgqfCGGTLIAPRWVLTAAHCV---DGDGPSDLRVVIGSTDLSTSGGTVVKVA---RIV 107
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1790135623  99 IFPEYEDRGwQREDYGVLELNSPASSqvlVTPIPVEDPWNIPLVGETLTLVGFGMTGDKCALPGQGKMKIALPVDE---- 174
Cdd:COG5640   108 VHPDYDPAT-PGNDIALLKLATPVPG---VAPAPLATSADAAAPGTPATVAGWGRTSEGPGSQSGTLRKADVPVVSdatc 183
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1790135623 175 SGWGGIS--------FKNNRLYSCPGDSGGPILNKAG---HVVGVASWGD-----NQVSVYRPTSYAYNWI 229
Cdd:COG5640   184 AAYGGFDggtmlcagYPEGGKDACQGDSGGPLVVKDGggwVLVGVVSWGGgpcaaGYPGVYTRVSAYRDWI 254
PAN_4 pfam14295
PAN domain;
469-519 6.32e-19

PAN domain;


:

Pssm-ID: 433846  Cd Length: 51  Bit Score: 80.14  E-value: 6.32e-19
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1790135623 469 TNRPGEDYTVFDLSSPDPEACANACREDEKCMAYSYVKPGFQSEKARCWLK 519
Cdd:pfam14295   1 TDRPGGDYRNGELLVDSPEACCAACDADPRCNAWTFVKPGYQGSYARCWLK 51
 
Name Accession Description Interval E-value
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
24-229 1.14e-24

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 103.19  E-value: 1.14e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1790135623  24 GTAVQDGELEAVGEVIGSGG-----CTGTLIADNLVLSAAHCFcngKSNCVNQGQFILRNVRTVADPNNRRNVTftgKVR 98
Cdd:COG5640    34 GTPATVGEYPWMVALQSSNGpsgqfCGGTLIAPRWVLTAAHCV---DGDGPSDLRVVIGSTDLSTSGGTVVKVA---RIV 107
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1790135623  99 IFPEYEDRGwQREDYGVLELNSPASSqvlVTPIPVEDPWNIPLVGETLTLVGFGMTGDKCALPGQGKMKIALPVDE---- 174
Cdd:COG5640   108 VHPDYDPAT-PGNDIALLKLATPVPG---VAPAPLATSADAAAPGTPATVAGWGRTSEGPGSQSGTLRKADVPVVSdatc 183
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1790135623 175 SGWGGIS--------FKNNRLYSCPGDSGGPILNKAG---HVVGVASWGD-----NQVSVYRPTSYAYNWI 229
Cdd:COG5640   184 AAYGGFDggtmlcagYPEGGKDACQGDSGGPLVVKDGggwVLVGVVSWGGgpcaaGYPGVYTRVSAYRDWI 254
Trypsin pfam00089
Trypsin;
40-229 3.99e-21

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 92.12  E-value: 3.99e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1790135623  40 GSGGCTGTLIADNLVLSAAHCFCNGKSNCVNQGQfilRNVRTVADPNNRRNVTftgKVRIFPEYEDRGWQReDYGVLELN 119
Cdd:pfam00089  23 GKHFCGGSLISENWVLTAAHCVSGASDVKVVLGA---HNIVLREGGEQKFDVE---KIIVHPNYNPDTLDN-DIALLKLE 95
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1790135623 120 SPASSQVLVTPIPVEDPWNIPLVGETLTLVGFGmTGDKCALP---GQGKMKIALPVDESGWGGISFKNNRL-------YS 189
Cdd:pfam00089  96 SPVTLGDTVRPICLPDASSDLPVGTTCTVSGWG-NTKTLGPSdtlQEVTVPVVSRETCRSAYGGTVTDTMIcagaggkDA 174
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1790135623 190 CPGDSGGPILNKAGHVVGVASWGD-----NQVSVYRPTSYAYNWI 229
Cdd:pfam00089 175 CQGDSGGPLVCSDGELIGIVSWGYgcasgNYPGVYTPVSSYLDWI 219
PAN_4 pfam14295
PAN domain;
469-519 6.32e-19

PAN domain;


Pssm-ID: 433846  Cd Length: 51  Bit Score: 80.14  E-value: 6.32e-19
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1790135623 469 TNRPGEDYTVFDLSSPDPEACANACREDEKCMAYSYVKPGFQSEKARCWLK 519
Cdd:pfam14295   1 TDRPGGDYRNGELLVDSPEACCAACDADPRCNAWTFVKPGYQGSYARCWLK 51
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
44-229 3.41e-15

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: 75.02  E-value: 3.41e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1790135623   44 CTGTLIADNLVLSAAHCFCNGksncvNQGQFILR---NVRTVADPNNRRNVTftgKVRIFPEYEDRGWqREDYGVLELNS 120
Cdd:smart00020  28 CGGSLISPRWVLTAAHCVRGS-----DPSNIRVRlgsHDLSSGEEGQVIKVS---KVIIHPNYNPSTY-DNDIALLKLKE 98
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1790135623  121 PASSQVLVTPIPVEDPWNIPLVGETLTLVGFGMTGDKCALPGQGKMKIALPV------DESGWGGISFKNNRL---Y--- 188
Cdd:smart00020  99 PVTLSDNVRPICLPSSNYNVPAGTTCTVSGWGRTSEGAGSLPDTLQEVNVPIvsnatcRRAYSGGGAITDNMLcagGleg 178
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1790135623  189 ---SCPGDSGGPIL--NKAGHVVGVASWGDNQVSVYRPTSYA-----YNWI 229
Cdd:smart00020 179 gkdACQGDSGGPLVcnDGRWVLVGIVSWGSGCARPGKPGVYTrvssyLDWI 229
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
44-229 6.26e-14

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: 71.15  E-value: 6.26e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1790135623  44 CTGTLIADNLVLSAAHCFcngksNCVNQGQFILR----NVRTVADPNNRRNVTftgKVRIFPEYEDRGWqREDYGVLELN 119
Cdd:cd00190    27 CGGSLISPRWVLTAAHCV-----YSSAPSNYTVRlgshDLSSNEGGGQVIKVK---KVIVHPNYNPSTY-DNDIALLKLK 97
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1790135623 120 SPASSQVLVTPIPVEDPWNIPLVGETLTLVGFGMTGDKCALPGQgKMKIALPV-------DESGWGGISFKNNRLY---- 188
Cdd:cd00190    98 RPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRTSEGGPLPDV-LQEVNVPIvsnaeckRAYSYGGTITDNMLCAggle 176
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1790135623 189 ----SCPGDSGGPIL---NKAGHVVGVASWGD-----NQVSVYRPTSYAYNWI 229
Cdd:cd00190   177 ggkdACQGDSGGPLVcndNGRGVLVGIVSWGSgcarpNYPGVYTRVSSYLDWI 229
APPLE_Factor_XI_like cd01100
Subfamily of PAN/APPLE-like domains; present in plasma prekallikrein/coagulation factor XI, ...
469-537 1.69e-04

Subfamily of PAN/APPLE-like domains; present in plasma prekallikrein/coagulation factor XI, microneme antigen proteins, and a few prokaryotic proteins. PAN/APPLE domains fulfill diverse biological functions by mediating protein-protein or protein-carbohydrate interactions.


Pssm-ID: 238533  Cd Length: 73  Bit Score: 40.11  E-value: 1.69e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1790135623 469 TNRPGEDYTVFDLSS---PDPEACANACREDEKCMAYSYVkpgfqSEKARCWLKSGIPDAEPDECCVSGIIR 537
Cdd:cd01100     7 RQGSNVDFRGGDLSTvfaSSAEQCQAACTADPGCLAFTYN-----TKSKKCFLKSSEGTLTKSTGAVSGPRL 73
 
Name Accession Description Interval E-value
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
24-229 1.14e-24

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 103.19  E-value: 1.14e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1790135623  24 GTAVQDGELEAVGEVIGSGG-----CTGTLIADNLVLSAAHCFcngKSNCVNQGQFILRNVRTVADPNNRRNVTftgKVR 98
Cdd:COG5640    34 GTPATVGEYPWMVALQSSNGpsgqfCGGTLIAPRWVLTAAHCV---DGDGPSDLRVVIGSTDLSTSGGTVVKVA---RIV 107
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1790135623  99 IFPEYEDRGwQREDYGVLELNSPASSqvlVTPIPVEDPWNIPLVGETLTLVGFGMTGDKCALPGQGKMKIALPVDE---- 174
Cdd:COG5640   108 VHPDYDPAT-PGNDIALLKLATPVPG---VAPAPLATSADAAAPGTPATVAGWGRTSEGPGSQSGTLRKADVPVVSdatc 183
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1790135623 175 SGWGGIS--------FKNNRLYSCPGDSGGPILNKAG---HVVGVASWGD-----NQVSVYRPTSYAYNWI 229
Cdd:COG5640   184 AAYGGFDggtmlcagYPEGGKDACQGDSGGPLVVKDGggwVLVGVVSWGGgpcaaGYPGVYTRVSAYRDWI 254
eMpr COG3591
V8-like Glu-specific endopeptidase [Posttranslational modification, protein turnover, ...
34-217 1.37e-22

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


Pssm-ID: 442810 [Multi-domain]  Cd Length: 194  Bit Score: 95.51  E-value: 1.37e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1790135623  34 AVGEVI---GSGGCTGTLIADNLVLSAAHCFCNGKSncvnqGQFIlRNVRTVADPNNRRNVTFTG-KVRIFPEYEDRGWQ 109
Cdd:COG3591     1 AVGRLEtdgGGGVCTGTLIGPNLVLTAGHCVYDGAG-----GGWA-TNIVFVPGYNGGPYGTATAtRFRVPPGWVASGDA 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1790135623 110 REDYGVLELNSPASSQvlVTPIPVeDPWNIPLVGETLTLVGFGmtGDKcalPGQGKMKIALPVDESGwggisfkNNRL-Y 188
Cdd:COG3591    75 GYDYALLRLDEPLGDT--TGWLGL-AFNDAPLAGEPVTIIGYP--GDR---PKDLSLDCSGRVTGVQ-------GNRLsY 139
                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1790135623 189 SC---PGDSGGPILNK---AGHVVGVASWGDNQVS 217
Cdd:COG3591   140 DCdttGGSSGSPVLDDsdgGGRVVGVHSAGGADRA 174
Trypsin pfam00089
Trypsin;
40-229 3.99e-21

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 92.12  E-value: 3.99e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1790135623  40 GSGGCTGTLIADNLVLSAAHCFCNGKSNCVNQGQfilRNVRTVADPNNRRNVTftgKVRIFPEYEDRGWQReDYGVLELN 119
Cdd:pfam00089  23 GKHFCGGSLISENWVLTAAHCVSGASDVKVVLGA---HNIVLREGGEQKFDVE---KIIVHPNYNPDTLDN-DIALLKLE 95
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1790135623 120 SPASSQVLVTPIPVEDPWNIPLVGETLTLVGFGmTGDKCALP---GQGKMKIALPVDESGWGGISFKNNRL-------YS 189
Cdd:pfam00089  96 SPVTLGDTVRPICLPDASSDLPVGTTCTVSGWG-NTKTLGPSdtlQEVTVPVVSRETCRSAYGGTVTDTMIcagaggkDA 174
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1790135623 190 CPGDSGGPILNKAGHVVGVASWGD-----NQVSVYRPTSYAYNWI 229
Cdd:pfam00089 175 CQGDSGGPLVCSDGELIGIVSWGYgcasgNYPGVYTPVSSYLDWI 219
PAN_4 pfam14295
PAN domain;
469-519 6.32e-19

PAN domain;


Pssm-ID: 433846  Cd Length: 51  Bit Score: 80.14  E-value: 6.32e-19
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1790135623 469 TNRPGEDYTVFDLSSPDPEACANACREDEKCMAYSYVKPGFQSEKARCWLK 519
Cdd:pfam14295   1 TDRPGGDYRNGELLVDSPEACCAACDADPRCNAWTFVKPGYQGSYARCWLK 51
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
44-229 3.41e-15

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: 75.02  E-value: 3.41e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1790135623   44 CTGTLIADNLVLSAAHCFCNGksncvNQGQFILR---NVRTVADPNNRRNVTftgKVRIFPEYEDRGWqREDYGVLELNS 120
Cdd:smart00020  28 CGGSLISPRWVLTAAHCVRGS-----DPSNIRVRlgsHDLSSGEEGQVIKVS---KVIIHPNYNPSTY-DNDIALLKLKE 98
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1790135623  121 PASSQVLVTPIPVEDPWNIPLVGETLTLVGFGMTGDKCALPGQGKMKIALPV------DESGWGGISFKNNRL---Y--- 188
Cdd:smart00020  99 PVTLSDNVRPICLPSSNYNVPAGTTCTVSGWGRTSEGAGSLPDTLQEVNVPIvsnatcRRAYSGGGAITDNMLcagGleg 178
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1790135623  189 ---SCPGDSGGPIL--NKAGHVVGVASWGDNQVSVYRPTSYA-----YNWI 229
Cdd:smart00020 179 gkdACQGDSGGPLVcnDGRWVLVGIVSWGSGCARPGKPGVYTrvssyLDWI 229
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
44-229 6.26e-14

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: 71.15  E-value: 6.26e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1790135623  44 CTGTLIADNLVLSAAHCFcngksNCVNQGQFILR----NVRTVADPNNRRNVTftgKVRIFPEYEDRGWqREDYGVLELN 119
Cdd:cd00190    27 CGGSLISPRWVLTAAHCV-----YSSAPSNYTVRlgshDLSSNEGGGQVIKVK---KVIVHPNYNPSTY-DNDIALLKLK 97
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1790135623 120 SPASSQVLVTPIPVEDPWNIPLVGETLTLVGFGMTGDKCALPGQgKMKIALPV-------DESGWGGISFKNNRLY---- 188
Cdd:cd00190    98 RPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRTSEGGPLPDV-LQEVNVPIvsnaeckRAYSYGGTITDNMLCAggle 176
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1790135623 189 ----SCPGDSGGPIL---NKAGHVVGVASWGD-----NQVSVYRPTSYAYNWI 229
Cdd:cd00190   177 ggkdACQGDSGGPLVcndNGRGVLVGIVSWGSgcarpNYPGVYTRVSSYLDWI 229
Trypsin_2 pfam13365
Trypsin-like peptidase domain; This family includes trypsin-like peptidase domains.
44-208 6.07e-10

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


Pssm-ID: 433149 [Multi-domain]  Cd Length: 142  Bit Score: 57.43  E-value: 6.07e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1790135623  44 CTGTLIA-DNLVLSAAHCFCNGKSNCVNQGQFILRNVRTVAdpnnrrnvtftgkVRIFPEYEDRgwqreDYGVLELNSPA 122
Cdd:pfam13365   1 GTGFVVSsDGLVLTNAHVVDDAEEAAVELVSVVLADGREYP-------------ATVVARDPDL-----DLALLRVSGDG 62
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1790135623 123 SSqvlVTPIPVEDPwNIPLVGETLTLVGFGMTGDKCALpGQGKMKIALPVDESGWGGISFKnnrlYSC---PGDSGGPIL 199
Cdd:pfam13365  63 RG---LPPLPLGDS-EPLVGGERVYAVGYPLGGEKLSL-SEGIVSGVDEGRDGGDDGRVIQ----TDAalsPGSSGGPVF 133

                  ....*....
gi 1790135623 200 NKAGHVVGV 208
Cdd:pfam13365 134 DADGRVVGI 142
APPLE_Factor_XI_like cd01100
Subfamily of PAN/APPLE-like domains; present in plasma prekallikrein/coagulation factor XI, ...
469-537 1.69e-04

Subfamily of PAN/APPLE-like domains; present in plasma prekallikrein/coagulation factor XI, microneme antigen proteins, and a few prokaryotic proteins. PAN/APPLE domains fulfill diverse biological functions by mediating protein-protein or protein-carbohydrate interactions.


Pssm-ID: 238533  Cd Length: 73  Bit Score: 40.11  E-value: 1.69e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1790135623 469 TNRPGEDYTVFDLSS---PDPEACANACREDEKCMAYSYVkpgfqSEKARCWLKSGIPDAEPDECCVSGIIR 537
Cdd:cd01100     7 RQGSNVDFRGGDLSTvfaSSAEQCQAACTADPGCLAFTYN-----TKSKKCFLKSSEGTLTKSTGAVSGPRL 73
 
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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