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Conserved domains on  [gi|1644281|emb|CAA93818|]
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Protein Classification

serine protease (domain architecture ID 10076129)

trypsin-like serine protease such as human plasminogen, the precursor of the widely distributed protease plasmin, or granzyme B, a human enzyme necessary for target cell lysis in cell-mediated immune responses

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 ...
27-265 3.16e-89

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: 264.14  E-value: 3.16e-89
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1644281   27 IVGGEEAIAHEFPYQISLQWNYNNdeqdpfHFCGGSLIAEKFVLTAGHCVPSaiSPDGFPEAVAGEHDFSQYDAGVQRRR 106
Cdd:cd00190   1 IVGGSEAKIGSFPWQVSLQYTGGR------HFCGGSLISPRWVLTAAHCVYS--SAPSNYTVRLGSHDLSSNEGGGQVIK 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1644281  107 IAEMYVHEDYEGSVGPNDIAIFRVDKPFHLNRNIQLVSLPEPNAIPTGET--TISGWGSTSFSfePSYPNILMKTTLPIM 184
Cdd:cd00190  73 VKKVIVHPNYNPSTYDNDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTtcTVSGWGRTSEG--GPLPDVLQEVNVPIV 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1644281  185 DLEVCRKIYFT-ETVADSNICAGTMEGTSSVCSGDSGGPLV-QIDDEIVQVGIVSWgGIPCGGYKNPGVFVRVSYFIDWI 262
Cdd:cd00190 151 SNAECKRAYSYgGTITDNMLCAGGLEGGKDACQGDSGGPLVcNDNGRGVLVGIVSW-GSGCARPNYPGVYTRVSSYLDWI 229

                ...
gi 1644281  263 NDK 265
Cdd:cd00190 230 QKT 232
 
Name Accession Description Interval E-value
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
27-265 3.16e-89

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: 264.14  E-value: 3.16e-89
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1644281   27 IVGGEEAIAHEFPYQISLQWNYNNdeqdpfHFCGGSLIAEKFVLTAGHCVPSaiSPDGFPEAVAGEHDFSQYDAGVQRRR 106
Cdd:cd00190   1 IVGGSEAKIGSFPWQVSLQYTGGR------HFCGGSLISPRWVLTAAHCVYS--SAPSNYTVRLGSHDLSSNEGGGQVIK 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1644281  107 IAEMYVHEDYEGSVGPNDIAIFRVDKPFHLNRNIQLVSLPEPNAIPTGET--TISGWGSTSFSfePSYPNILMKTTLPIM 184
Cdd:cd00190  73 VKKVIVHPNYNPSTYDNDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTtcTVSGWGRTSEG--GPLPDVLQEVNVPIV 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1644281  185 DLEVCRKIYFT-ETVADSNICAGTMEGTSSVCSGDSGGPLV-QIDDEIVQVGIVSWgGIPCGGYKNPGVFVRVSYFIDWI 262
Cdd:cd00190 151 SNAECKRAYSYgGTITDNMLCAGGLEGGKDACQGDSGGPLVcNDNGRGVLVGIVSW-GSGCARPNYPGVYTRVSSYLDWI 229

                ...
gi 1644281  263 NDK 265
Cdd:cd00190 230 QKT 232
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
26-262 6.01e-88

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: 260.69  E-value: 6.01e-88
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1644281      26 KIVGGEEAIAHEFPYQISLQWNynndeqDPFHFCGGSLIAEKFVLTAGHCVPSaiSPDGFPEAVAGEHDFSQYDaGVQRR 105
Cdd:smart00020   1 RIVGGSEANIGSFPWQVSLQYG------GGRHFCGGSLISPRWVLTAAHCVRG--SDPSNIRVRLGSHDLSSGE-EGQVI 71
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1644281     106 RIAEMYVHEDYEGSVGPNDIAIFRVDKPFHLNRNIQLVSLPEPNAIPTGET--TISGWGSTSFSfEPSYPNILMKTTLPI 183
Cdd:smart00020  72 KVSKVIIHPNYNPSTYDNDIALLKLKEPVTLSDNVRPICLPSSNYNVPAGTtcTVSGWGRTSEG-AGSLPDTLQEVNVPI 150
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1644281     184 MDLEVCRKIYF-TETVADSNICAGTMEGTSSVCSGDSGGPLVQIDDEIVQVGIVSWgGIPCGGYKNPGVFVRVSYFIDWI 262
Cdd:smart00020 151 VSNATCRRAYSgGGAITDNMLCAGGLEGGKDACQGDSGGPLVCNDGRWVLVGIVSW-GSGCARPGKPGVYTRVSSYLDWI 229
Trypsin pfam00089
Trypsin;
27-262 4.87e-62

Trypsin;


Pssm-ID: 395042  Cd Length: 219  Bit Score: 194.58  E-value: 4.87e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1644281     27 IVGGEEAIAHEFPYQISLQWNynndeqDPFHFCGGSLIAEKFVLTAGHCVPSAISPdgfpEAVAGEHDFSQYDAGVQRRR 106
Cdd:pfam00089   1 IVGGDEAQPGSFPWQVSLQLS------SGKHFCGGSLISENWVLTAAHCVSGASDV----KVVLGAHNIVLREGGEQKFD 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1644281    107 IAEMYVHEDYEGSVGPNDIAIFRVDKPFHLNRNIQLVSLPEPNAIPTGETT--ISGWGSTsfsFEPSYPNILMKTTLPIM 184
Cdd:pfam00089  71 VEKIIVHPNYNPDTLDNDIALLKLESPVTLGDTVRPICLPDASSDLPVGTTctVSGWGNT---KTLGPSDTLQEVTVPVV 147
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1644281    185 DLEVCRKIYFTeTVADSNICAGTmeGTSSVCSGDSGGPLVQIDDEivQVGIVSWGGiPCGGYKNPGVFVRVSYFIDWI 262
Cdd:pfam00089 148 SRETCRSAYGG-TVTDTMICAGA--GGKDACQGDSGGPLVCSDGE--LIGIVSWGY-GCASGNYPGVYTPVSSYLDWI 219
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
25-267 2.82e-35

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


Pssm-ID: 227927 [Multi-domain]  Cd Length: 413  Bit Score: 130.38  E-value: 2.82e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1644281   25 PKIVGGEEAIAHEFPYQISLQwNYNNDEQDpFHFCGGSLIAEKFVLTAGHCV--PSAISPDgfPEAVAGE-HDFSQYdag 101
Cdd:COG5640  31 SRIIGGSNANAGEYPSLVALV-DRISDYVS-GTFCGGSKLGGRYVLTAAHCAdaSSPISSD--VNRVVVDlNDSSQA--- 103
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1644281  102 vQRRRIAEMYVHEDY-EGSVGpNDIAIFRVDKPFHLNR-NIQLVSLPEP--NAIPT-GETTISGWGSTSFSFEP-SYPN- 174
Cdd:COG5640 104 -ERGHVRTIYVHEFYsPGNLG-NDIAVLELARAASLPRvKITSFDASDTflNSVTTvSPMTNGTFGVTTPSDVPrSSPKg 181
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1644281  175 -ILMKTTLPIMDLEVCRKIYFTETVADS-----NICAGTMegTSSVCSGDSGGPLV-QIDDEIVQVGIVSWGGIPCGGYK 247
Cdd:COG5640 182 tILHEVAVLFVPLSTCAQYKGCANASDGatgltGFCAGRP--PKDACQGDSGGPIFhKGEEGRVQRGVVSWGDGGCGGTL 259
                       250       260
                ....*....|....*....|
gi 1644281  248 NPGVFVRVSYFIDWINDKIN 267
Cdd:COG5640 260 IPGVYTNVSNYQDWIAAMTN 279
 
Name Accession Description Interval E-value
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
27-265 3.16e-89

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: 264.14  E-value: 3.16e-89
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1644281   27 IVGGEEAIAHEFPYQISLQWNYNNdeqdpfHFCGGSLIAEKFVLTAGHCVPSaiSPDGFPEAVAGEHDFSQYDAGVQRRR 106
Cdd:cd00190   1 IVGGSEAKIGSFPWQVSLQYTGGR------HFCGGSLISPRWVLTAAHCVYS--SAPSNYTVRLGSHDLSSNEGGGQVIK 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1644281  107 IAEMYVHEDYEGSVGPNDIAIFRVDKPFHLNRNIQLVSLPEPNAIPTGET--TISGWGSTSFSfePSYPNILMKTTLPIM 184
Cdd:cd00190  73 VKKVIVHPNYNPSTYDNDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTtcTVSGWGRTSEG--GPLPDVLQEVNVPIV 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1644281  185 DLEVCRKIYFT-ETVADSNICAGTMEGTSSVCSGDSGGPLV-QIDDEIVQVGIVSWgGIPCGGYKNPGVFVRVSYFIDWI 262
Cdd:cd00190 151 SNAECKRAYSYgGTITDNMLCAGGLEGGKDACQGDSGGPLVcNDNGRGVLVGIVSW-GSGCARPNYPGVYTRVSSYLDWI 229

                ...
gi 1644281  263 NDK 265
Cdd:cd00190 230 QKT 232
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
26-262 6.01e-88

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: 260.69  E-value: 6.01e-88
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1644281      26 KIVGGEEAIAHEFPYQISLQWNynndeqDPFHFCGGSLIAEKFVLTAGHCVPSaiSPDGFPEAVAGEHDFSQYDaGVQRR 105
Cdd:smart00020   1 RIVGGSEANIGSFPWQVSLQYG------GGRHFCGGSLISPRWVLTAAHCVRG--SDPSNIRVRLGSHDLSSGE-EGQVI 71
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1644281     106 RIAEMYVHEDYEGSVGPNDIAIFRVDKPFHLNRNIQLVSLPEPNAIPTGET--TISGWGSTSFSfEPSYPNILMKTTLPI 183
Cdd:smart00020  72 KVSKVIIHPNYNPSTYDNDIALLKLKEPVTLSDNVRPICLPSSNYNVPAGTtcTVSGWGRTSEG-AGSLPDTLQEVNVPI 150
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1644281     184 MDLEVCRKIYF-TETVADSNICAGTMEGTSSVCSGDSGGPLVQIDDEIVQVGIVSWgGIPCGGYKNPGVFVRVSYFIDWI 262
Cdd:smart00020 151 VSNATCRRAYSgGGAITDNMLCAGGLEGGKDACQGDSGGPLVCNDGRWVLVGIVSW-GSGCARPGKPGVYTRVSSYLDWI 229
Trypsin pfam00089
Trypsin;
27-262 4.87e-62

Trypsin;


Pssm-ID: 395042  Cd Length: 219  Bit Score: 194.58  E-value: 4.87e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1644281     27 IVGGEEAIAHEFPYQISLQWNynndeqDPFHFCGGSLIAEKFVLTAGHCVPSAISPdgfpEAVAGEHDFSQYDAGVQRRR 106
Cdd:pfam00089   1 IVGGDEAQPGSFPWQVSLQLS------SGKHFCGGSLISENWVLTAAHCVSGASDV----KVVLGAHNIVLREGGEQKFD 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1644281    107 IAEMYVHEDYEGSVGPNDIAIFRVDKPFHLNRNIQLVSLPEPNAIPTGETT--ISGWGSTsfsFEPSYPNILMKTTLPIM 184
Cdd:pfam00089  71 VEKIIVHPNYNPDTLDNDIALLKLESPVTLGDTVRPICLPDASSDLPVGTTctVSGWGNT---KTLGPSDTLQEVTVPVV 147
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1644281    185 DLEVCRKIYFTeTVADSNICAGTmeGTSSVCSGDSGGPLVQIDDEivQVGIVSWGGiPCGGYKNPGVFVRVSYFIDWI 262
Cdd:pfam00089 148 SRETCRSAYGG-TVTDTMICAGA--GGKDACQGDSGGPLVCSDGE--LIGIVSWGY-GCASGNYPGVYTPVSSYLDWI 219
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
25-267 2.82e-35

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


Pssm-ID: 227927 [Multi-domain]  Cd Length: 413  Bit Score: 130.38  E-value: 2.82e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1644281   25 PKIVGGEEAIAHEFPYQISLQwNYNNDEQDpFHFCGGSLIAEKFVLTAGHCV--PSAISPDgfPEAVAGE-HDFSQYdag 101
Cdd:COG5640  31 SRIIGGSNANAGEYPSLVALV-DRISDYVS-GTFCGGSKLGGRYVLTAAHCAdaSSPISSD--VNRVVVDlNDSSQA--- 103
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1644281  102 vQRRRIAEMYVHEDY-EGSVGpNDIAIFRVDKPFHLNR-NIQLVSLPEP--NAIPT-GETTISGWGSTSFSFEP-SYPN- 174
Cdd:COG5640 104 -ERGHVRTIYVHEFYsPGNLG-NDIAVLELARAASLPRvKITSFDASDTflNSVTTvSPMTNGTFGVTTPSDVPrSSPKg 181
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1644281  175 -ILMKTTLPIMDLEVCRKIYFTETVADS-----NICAGTMegTSSVCSGDSGGPLV-QIDDEIVQVGIVSWGGIPCGGYK 247
Cdd:COG5640 182 tILHEVAVLFVPLSTCAQYKGCANASDGatgltGFCAGRP--PKDACQGDSGGPIFhKGEEGRVQRGVVSWGDGGCGGTL 259
                       250       260
                ....*....|....*....|
gi 1644281  248 NPGVFVRVSYFIDWINDKIN 267
Cdd:COG5640 260 IPGVYTNVSNYQDWIAAMTN 279
alphaLP-like cd21112
alpha-lytic protease (alpha-LP), a bacterial serine protease of the chymotrypsin family, and ...
66-255 1.19e-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: 47.69  E-value: 1.19e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1644281   66 EKFVLTAGHCVP--SAISPDGFPEAVAGEHDFSQYdagvqrrriaemyvhedyegsvGPNDIAIFRVDkpfhlnrNIQLV 143
Cdd:cd21112  27 TPYFLTAGHCGNggGTVYADGALGVPIGTVVASSF----------------------PGNDYALVRVT-------NPGWT 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1644281  144 SLPEPNAIPTGETTISGWGStsfsfepsypnilmkttlPIMDLEVCR----------KIyfTETVADSNICAGTMEG--T 211
Cdd:cd21112  78 PPPEVRTYGGGTVPITGSAE------------------PVVGAPVCKsgrttgwtcgTV--TAVNVTVNYPGGTVTGltR 137
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*.
gi 1644281  212 SSVCS--GDSGGPLVQIDdeiVQVGIVSWGGIPCGGYKNPGVFVRV 255
Cdd:cd21112 138 TNACAepGDSGGPVFSGT---QALGITSGGSGNCGSGGGTSYFQPV 180
eMpr COG3591
V8-like Glu-specific endopeptidase [Posttranslational modification, protein turnover, ...
59-267 6.97e-04

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


Pssm-ID: 226119  Cd Length: 251  Bit Score: 40.06  E-value: 6.97e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1644281   59 CGGSLIAEKFVLTAGHCVPSaiSPDG------FPEAVAGE-HDFSQYDAGVQRRRIAEMYVHEDYEGSVGPNDIaifrvD 131
Cdd:COG3591  66 TAATLIGPNTVLTAGHCIYS--PDYGeddiaaAPPGVNSDgGPFYGITKIEIRVYPGELYKEDGASYDVGEAAL-----E 138
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1644281  132 KPFHLNRNIQLVSLPEPNAIPTGET-TISGWGSTSFSFEPSYPNilmktTLPIMdlevcrkiyftetVADSNIcagtMEG 210
Cdd:COG3591 139 SGINIGDVVNYLKRNTASEAKANDRiTVIGYPGDKPNIGTMWES-----TGKVN-------------SIKGNK----LFY 196
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 1644281  211 TSSVCSGDSGGPLVQIDDEIVQvgiVSWGGIPCGGYKNPGVFVR-VSYFIDWINDKIN 267
Cdd:COG3591 197 DADTLPGSSGSPVLISKDEVIG---VHYNGPGANGGSLANNAVRlTPEILNFIQQNIK 251
 
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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