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Conserved domains on  [gi|1931206609|ref|XP_037299514|]
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serine protease persephone [Manduca sexta]

Protein Classification

CLIP and Tryp_SPc domain-containing protein (domain architecture ID 11643046)

CLIP and Tryp_SPc domain-containing protein

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 ...
161-399 1.20e-75

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: 234.49  E-value: 1.20e-75
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931206609  161 IVGGVNASRNEFPHMVLLgfnTTTGISWMCGGSLISEKFILTAGHCVMHKDFGDVKyASIGVLSRGEVTPENTYKVKRSV 240
Cdd:smart00020   2 IVGGSEANIGSFPWQVSL---QYGGGRHFCGGSLISPRWVLTAAHCVRGSDPSNIR-VRLGSHDLSSGEEGQVIKVSKVI 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931206609  241 RHPQYRIDVY-NDIAVIELEKEVTLDAFTVPACLHVGD--PIDYSRAIATGWGLLEDRGATPSDVMQKVIVKKIRKATCQ 317
Cdd:smart00020  78 IHPNYNPSTYdNDIALLKLKEPVTLSDNVRPICLPSSNynVPAGTTCTVSGWGRTSEGAGSLPDTLQEVNVPIVSNATCR 157
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931206609  318 RDYPGDTstiaakYDSESQLCYGDRQEKKDTCQGDSGGPLQLKHKkincMYLVIGVTSGGKGCALRNKPGLYSKVSHYLD 397
Cdd:smart00020 158 RAYSGGG------AITDNMLCAGGLEGGKDACQGDSGGPLVCNDG----RWVLVGIVSWGSGCARPGKPGVYTRVSSYLD 227

                   ..
gi 1931206609  398 WI 399
Cdd:smart00020 228 WI 229
CLIP super family cl02731
Regulatory CLIP domain of proteinases; CLIP is a regulatory domain which controls the ...
26-66 1.17e-03

Regulatory CLIP domain of proteinases; CLIP is a regulatory domain which controls the proteinase action of various proteins of the trypsin family, e.g. easter and pap2. The CLIP domain remains linked to the protease domain after cleavage of a conserved residue which retains the protein in zymogen form. It is named CLIP because it can be drawn in the shape of a paper clip. It has many disulphide bonds and highly conserved cysteine residues, and so it folds extensively.


The actual alignment was detected with superfamily member smart00680:

Pssm-ID: 413454  Cd Length: 52  Bit Score: 36.72  E-value: 1.17e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 1931206609   26 NGVTGKCVPIKKCLSALQniVYKKHP---------QICSFDKVEPTICCV 66
Cdd:smart00680   5 DGERGTCVPISDCPSLLS--LLKKDPpedlnflrkSQCGFGNREPLVCCP 52
 
Name Accession Description Interval E-value
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
161-399 1.20e-75

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: 234.49  E-value: 1.20e-75
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931206609  161 IVGGVNASRNEFPHMVLLgfnTTTGISWMCGGSLISEKFILTAGHCVMHKDFGDVKyASIGVLSRGEVTPENTYKVKRSV 240
Cdd:smart00020   2 IVGGSEANIGSFPWQVSL---QYGGGRHFCGGSLISPRWVLTAAHCVRGSDPSNIR-VRLGSHDLSSGEEGQVIKVSKVI 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931206609  241 RHPQYRIDVY-NDIAVIELEKEVTLDAFTVPACLHVGD--PIDYSRAIATGWGLLEDRGATPSDVMQKVIVKKIRKATCQ 317
Cdd:smart00020  78 IHPNYNPSTYdNDIALLKLKEPVTLSDNVRPICLPSSNynVPAGTTCTVSGWGRTSEGAGSLPDTLQEVNVPIVSNATCR 157
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931206609  318 RDYPGDTstiaakYDSESQLCYGDRQEKKDTCQGDSGGPLQLKHKkincMYLVIGVTSGGKGCALRNKPGLYSKVSHYLD 397
Cdd:smart00020 158 RAYSGGG------AITDNMLCAGGLEGGKDACQGDSGGPLVCNDG----RWVLVGIVSWGSGCARPGKPGVYTRVSSYLD 227

                   ..
gi 1931206609  398 WI 399
Cdd:smart00020 228 WI 229
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
161-402 1.25e-73

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  Cd Length: 232  Bit Score: 229.47  E-value: 1.25e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931206609 161 IVGGVNASRNEFPHMVLLgfnTTTGISWMCGGSLISEKFILTAGHCVMHKDFGDVKyASIGVLSRGEVTP-ENTYKVKRS 239
Cdd:cd00190     1 IVGGSEAKIGSFPWQVSL---QYTGGRHFCGGSLISPRWVLTAAHCVYSSAPSNYT-VRLGSHDLSSNEGgGQVIKVKKV 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931206609 240 VRHPQYRIDVY-NDIAVIELEKEVTLDAFTVPACLHVGD--PIDYSRAIATGWGLLEDRGaTPSDVMQKVIVKKIRKATC 316
Cdd:cd00190    77 IVHPNYNPSTYdNDIALLKLKRPVTLSDNVRPICLPSSGynLPAGTTCTVSGWGRTSEGG-PLPDVLQEVNVPIVSNAEC 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931206609 317 QRDYPGDtstiaaKYDSESQLCYGDRQEKKDTCQGDSGGPLQLKHkkiNCMYLVIGVTSGGKGCALRNKPGLYSKVSHYL 396
Cdd:cd00190   156 KRAYSYG------GTITDNMLCAGGLEGGKDACQGDSGGPLVCND---NGRGVLVGIVSWGSGCARPNYPGVYTRVSSYL 226

                  ....*.
gi 1931206609 397 DWIESI 402
Cdd:cd00190   227 DWIQKT 232
Trypsin pfam00089
Trypsin;
161-399 3.56e-52

Trypsin;


Pssm-ID: 395042  Cd Length: 219  Bit Score: 173.78  E-value: 3.56e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931206609 161 IVGGVNASRNEFPHMVLLGFnttTGISWMCGGSLISEKFILTAGHCVmhKDFGDVK-YASIGVLSRGEVTpENTYKVKRS 239
Cdd:pfam00089   1 IVGGDEAQPGSFPWQVSLQL---SSGKHFCGGSLISENWVLTAAHCV--SGASDVKvVLGAHNIVLREGG-EQKFDVEKI 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931206609 240 VRHPQYRID-VYNDIAVIELEKEVTLDAFTVPACL-------HVGDPIdysraIATGWGLLEDRGatPSDVMQKVIVKKI 311
Cdd:pfam00089  75 IVHPNYNPDtLDNDIALLKLESPVTLGDTVRPICLpdassdlPVGTTC-----TVSGWGNTKTLG--PSDTLQEVTVPVV 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931206609 312 RKATCQRDYPGDTStiaakydsESQLCYGDRqeKKDTCQGDSGGPLQLKHKKincmylVIGVTSGGKGCALRNKPGLYSK 391
Cdd:pfam00089 148 SRETCRSAYGGTVT--------DTMICAGAG--GKDACQGDSGGPLVCSDGE------LIGIVSWGYGCASGNYPGVYTP 211

                  ....*...
gi 1931206609 392 VSHYLDWI 399
Cdd:pfam00089 212 VSSYLDWI 219
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
156-400 1.19e-20

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


Pssm-ID: 227927 [Multi-domain]  Cd Length: 413  Bit Score: 93.02  E-value: 1.19e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931206609 156 NADEL---IVGGVNASRNEFPHMV-LLGFNTTTGISWMCGGSLISEKFILTAGHCVMHKDFGDVKYaSIGVLSRGEVTPE 231
Cdd:COG5640    25 TADEVssrIIGGSNANAGEYPSLVaLVDRISDYVSGTFCGGSKLGGRYVLTAAHCADASSPISSDV-NRVVVDLNDSSQA 103
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931206609 232 NTYKVKRSVRHPQYRIDVY-NDIAVIELEKEVTLDAFTVpaclHVGDPIDYSRAIATGWGLLEDRG---ATPSDV----- 302
Cdd:COG5640   104 ERGHVRTIYVHEFYSPGNLgNDIAVLELARAASLPRVKI----TSFDASDTFLNSVTTVSPMTNGTfgvTTPSDVprssp 179
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931206609 303 ----MQKVIVKKIRKATCQRdYPGDTSTIaakyDSESQL---CYGdrQEKKDTCQGDSGGPLQLKHkkiNCMYLVIGVTS 375
Cdd:COG5640   180 kgtiLHEVAVLFVPLSTCAQ-YKGCANAS----DGATGLtgfCAG--RPPKDACQGDSGGPIFHKG---EEGRVQRGVVS 249
                         250       260
                  ....*....|....*....|....*.
gi 1931206609 376 GGKG-CALRNKPGLYSKVSHYLDWIE 400
Cdd:COG5640   250 WGDGgCGGTLIPGVYTNVSNYQDWIA 275
CLIP smart00680
Clip or disulphide knot domain; Present in horseshoe crab proclotting enzyme N-terminal domain, ...
26-66 1.17e-03

Clip or disulphide knot domain; Present in horseshoe crab proclotting enzyme N-terminal domain, Drosophila Easter and silkworm prophenoloxidase-activating enzyme.


Pssm-ID: 197829  Cd Length: 52  Bit Score: 36.72  E-value: 1.17e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 1931206609   26 NGVTGKCVPIKKCLSALQniVYKKHP---------QICSFDKVEPTICCV 66
Cdd:smart00680   5 DGERGTCVPISDCPSLLS--LLKKDPpedlnflrkSQCGFGNREPLVCCP 52
 
Name Accession Description Interval E-value
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
161-399 1.20e-75

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: 234.49  E-value: 1.20e-75
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931206609  161 IVGGVNASRNEFPHMVLLgfnTTTGISWMCGGSLISEKFILTAGHCVMHKDFGDVKyASIGVLSRGEVTPENTYKVKRSV 240
Cdd:smart00020   2 IVGGSEANIGSFPWQVSL---QYGGGRHFCGGSLISPRWVLTAAHCVRGSDPSNIR-VRLGSHDLSSGEEGQVIKVSKVI 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931206609  241 RHPQYRIDVY-NDIAVIELEKEVTLDAFTVPACLHVGD--PIDYSRAIATGWGLLEDRGATPSDVMQKVIVKKIRKATCQ 317
Cdd:smart00020  78 IHPNYNPSTYdNDIALLKLKEPVTLSDNVRPICLPSSNynVPAGTTCTVSGWGRTSEGAGSLPDTLQEVNVPIVSNATCR 157
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931206609  318 RDYPGDTstiaakYDSESQLCYGDRQEKKDTCQGDSGGPLQLKHKkincMYLVIGVTSGGKGCALRNKPGLYSKVSHYLD 397
Cdd:smart00020 158 RAYSGGG------AITDNMLCAGGLEGGKDACQGDSGGPLVCNDG----RWVLVGIVSWGSGCARPGKPGVYTRVSSYLD 227

                   ..
gi 1931206609  398 WI 399
Cdd:smart00020 228 WI 229
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
161-402 1.25e-73

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  Cd Length: 232  Bit Score: 229.47  E-value: 1.25e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931206609 161 IVGGVNASRNEFPHMVLLgfnTTTGISWMCGGSLISEKFILTAGHCVMHKDFGDVKyASIGVLSRGEVTP-ENTYKVKRS 239
Cdd:cd00190     1 IVGGSEAKIGSFPWQVSL---QYTGGRHFCGGSLISPRWVLTAAHCVYSSAPSNYT-VRLGSHDLSSNEGgGQVIKVKKV 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931206609 240 VRHPQYRIDVY-NDIAVIELEKEVTLDAFTVPACLHVGD--PIDYSRAIATGWGLLEDRGaTPSDVMQKVIVKKIRKATC 316
Cdd:cd00190    77 IVHPNYNPSTYdNDIALLKLKRPVTLSDNVRPICLPSSGynLPAGTTCTVSGWGRTSEGG-PLPDVLQEVNVPIVSNAEC 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931206609 317 QRDYPGDtstiaaKYDSESQLCYGDRQEKKDTCQGDSGGPLQLKHkkiNCMYLVIGVTSGGKGCALRNKPGLYSKVSHYL 396
Cdd:cd00190   156 KRAYSYG------GTITDNMLCAGGLEGGKDACQGDSGGPLVCND---NGRGVLVGIVSWGSGCARPNYPGVYTRVSSYL 226

                  ....*.
gi 1931206609 397 DWIESI 402
Cdd:cd00190   227 DWIQKT 232
Trypsin pfam00089
Trypsin;
161-399 3.56e-52

Trypsin;


Pssm-ID: 395042  Cd Length: 219  Bit Score: 173.78  E-value: 3.56e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931206609 161 IVGGVNASRNEFPHMVLLGFnttTGISWMCGGSLISEKFILTAGHCVmhKDFGDVK-YASIGVLSRGEVTpENTYKVKRS 239
Cdd:pfam00089   1 IVGGDEAQPGSFPWQVSLQL---SSGKHFCGGSLISENWVLTAAHCV--SGASDVKvVLGAHNIVLREGG-EQKFDVEKI 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931206609 240 VRHPQYRID-VYNDIAVIELEKEVTLDAFTVPACL-------HVGDPIdysraIATGWGLLEDRGatPSDVMQKVIVKKI 311
Cdd:pfam00089  75 IVHPNYNPDtLDNDIALLKLESPVTLGDTVRPICLpdassdlPVGTTC-----TVSGWGNTKTLG--PSDTLQEVTVPVV 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931206609 312 RKATCQRDYPGDTStiaakydsESQLCYGDRqeKKDTCQGDSGGPLQLKHKKincmylVIGVTSGGKGCALRNKPGLYSK 391
Cdd:pfam00089 148 SRETCRSAYGGTVT--------DTMICAGAG--GKDACQGDSGGPLVCSDGE------LIGIVSWGYGCASGNYPGVYTP 211

                  ....*...
gi 1931206609 392 VSHYLDWI 399
Cdd:pfam00089 212 VSSYLDWI 219
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
156-400 1.19e-20

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


Pssm-ID: 227927 [Multi-domain]  Cd Length: 413  Bit Score: 93.02  E-value: 1.19e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931206609 156 NADEL---IVGGVNASRNEFPHMV-LLGFNTTTGISWMCGGSLISEKFILTAGHCVMHKDFGDVKYaSIGVLSRGEVTPE 231
Cdd:COG5640    25 TADEVssrIIGGSNANAGEYPSLVaLVDRISDYVSGTFCGGSKLGGRYVLTAAHCADASSPISSDV-NRVVVDLNDSSQA 103
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931206609 232 NTYKVKRSVRHPQYRIDVY-NDIAVIELEKEVTLDAFTVpaclHVGDPIDYSRAIATGWGLLEDRG---ATPSDV----- 302
Cdd:COG5640   104 ERGHVRTIYVHEFYSPGNLgNDIAVLELARAASLPRVKI----TSFDASDTFLNSVTTVSPMTNGTfgvTTPSDVprssp 179
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931206609 303 ----MQKVIVKKIRKATCQRdYPGDTSTIaakyDSESQL---CYGdrQEKKDTCQGDSGGPLQLKHkkiNCMYLVIGVTS 375
Cdd:COG5640   180 kgtiLHEVAVLFVPLSTCAQ-YKGCANAS----DGATGLtgfCAG--RPPKDACQGDSGGPIFHKG---EEGRVQRGVVS 249
                         250       260
                  ....*....|....*....|....*.
gi 1931206609 376 GGKG-CALRNKPGLYSKVSHYLDWIE 400
Cdd:COG5640   250 WGDGgCGGTLIPGVYTNVSNYQDWIA 275
eMpr COG3591
V8-like Glu-specific endopeptidase [Posttranslational modification, protein turnover, ...
170-377 6.05e-05

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


Pssm-ID: 226119  Cd Length: 251  Bit Score: 44.30  E-value: 6.05e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931206609 170 NEFPHMVLLGFNTTTGiSWMCGGSLISEKFILTAGHCVMHKDFG--DVKYASIGVLSRGEvtPENTYKVKRSVRHPQYRI 247
Cdd:COG3591    47 TQFPYSAVVQFEAATG-RLCTAATLIGPNTVLTAGHCIYSPDYGedDIAAAPPGVNSDGG--PFYGITKIEIRVYPGELY 123
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931206609 248 DVynDIAVIELEkevtldaftvPACLHVGDPIDysraIATGWGLLEDRGATPSDVMQKVIVKKIRKATCQRDYPgdtSTI 327
Cdd:COG3591   124 KE--DGASYDVG----------EAALESGINIG----DVVNYLKRNTASEAKANDRITVIGYPGDKPNIGTMWE---STG 184
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1931206609 328 AAKYDSESQLCYgdrqeKKDTCQGDSGGPLQLKHKKincmylVIGVTSGG 377
Cdd:COG3591   185 KVNSIKGNKLFY-----DADTLPGSSGSPVLISKDE------VIGVHYNG 223
CLIP smart00680
Clip or disulphide knot domain; Present in horseshoe crab proclotting enzyme N-terminal domain, ...
26-66 1.17e-03

Clip or disulphide knot domain; Present in horseshoe crab proclotting enzyme N-terminal domain, Drosophila Easter and silkworm prophenoloxidase-activating enzyme.


Pssm-ID: 197829  Cd Length: 52  Bit Score: 36.72  E-value: 1.17e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 1931206609   26 NGVTGKCVPIKKCLSALQniVYKKHP---------QICSFDKVEPTICCV 66
Cdd:smart00680   5 DGERGTCVPISDCPSLLS--LLKKDPpedlnflrkSQCGFGNREPLVCCP 52
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.19
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
  • Marchler-Bauer A et al. (2015), "CDD: NCBI's conserved domain database.", Nucleic Acids Res.43(D)222-6.
  • Marchler-Bauer A et al. (2011), "CDD: a Conserved Domain Database for the functional annotation of proteins.", Nucleic Acids Res.39(D)225-9.
  • Marchler-Bauer A, Bryant SH (2004), "CD-Search: protein domain annotations on the fly.", Nucleic Acids Res.32(W)327-331.
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