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Conserved domains on  [gi|1237881473|gb|PAJ75302|]
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GTP cyclohydrolase I FolE2 [Pseudoalteromonas sp. NBT06-2]

Protein Classification

GTP cyclohydrolase I FolE2( domain architecture ID 10014323)

GTP cyclohydrolase FolE2, a type Ib GTP cyclohydrolase, converts GTP to 7,8-dihydroneopterin triphosphate

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PRK13674 PRK13674
GTP cyclohydrolase I FolE2;
1-293 3.60e-104

GTP cyclohydrolase I FolE2;


:

Pssm-ID: 237466  Cd Length: 271  Bit Score: 305.19  E-value: 3.60e-104
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237881473   1 MNINLPDITSGQyALTQLPLRWVGMEAIAIPLEVPISDFTILSVNAKADIFVSLDkPEAKGIHMSRLYLKLkDKLTSYNL 80
Cdd:PRK13674    5 MKATMPDVQSTP-DTRLIPIDWVGIKNIRLPVRVDTRDGGTQTTVARVDLTVSLP-ADFKGIHMSRLYELL-EEHAEQEL 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237881473  81 NGEMLTELLHEIISSQEglSEAAKINLSFELTIRKNALLSNEFGYQSYPISISRSYVHGKTVTELSLTIPYSSTCPCSSA 160
Cdd:PRK13674   82 SPASLEQLLRDMLESLE--SRAARIEVSFPYFLRKPAPVSGLSGWKDYPVTLEAELRDGVFRLELKVEVPVSSLCPCSKA 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237881473 161 LSRQalsdkldqsfasinidknellqwiisekntaaTAHSQRSYAYLKFTLKDEHLPNLNDLILKFEQVMGTPVQTAVKR 240
Cdd:PRK13674  160 ISRY--------------------------------TAHSQRSVATVKVRLAADAQLWIEDLIDLAEAAASTPLQTLLKR 207
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1237881473 241 EDEQAFAKLNAENLMFCEDAARRLKQSIENNSNISGYWFKVEHQESLHAHNAV 293
Cdd:PRK13674  208 PDEKAVTELAYENPMFVEDAARRVAAALEADPRISAFRVEVEHFESIHNHDAV 260
 
Name Accession Description Interval E-value
PRK13674 PRK13674
GTP cyclohydrolase I FolE2;
1-293 3.60e-104

GTP cyclohydrolase I FolE2;


Pssm-ID: 237466  Cd Length: 271  Bit Score: 305.19  E-value: 3.60e-104
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237881473   1 MNINLPDITSGQyALTQLPLRWVGMEAIAIPLEVPISDFTILSVNAKADIFVSLDkPEAKGIHMSRLYLKLkDKLTSYNL 80
Cdd:PRK13674    5 MKATMPDVQSTP-DTRLIPIDWVGIKNIRLPVRVDTRDGGTQTTVARVDLTVSLP-ADFKGIHMSRLYELL-EEHAEQEL 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237881473  81 NGEMLTELLHEIISSQEglSEAAKINLSFELTIRKNALLSNEFGYQSYPISISRSYVHGKTVTELSLTIPYSSTCPCSSA 160
Cdd:PRK13674   82 SPASLEQLLRDMLESLE--SRAARIEVSFPYFLRKPAPVSGLSGWKDYPVTLEAELRDGVFRLELKVEVPVSSLCPCSKA 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237881473 161 LSRQalsdkldqsfasinidknellqwiisekntaaTAHSQRSYAYLKFTLKDEHLPNLNDLILKFEQVMGTPVQTAVKR 240
Cdd:PRK13674  160 ISRY--------------------------------TAHSQRSVATVKVRLAADAQLWIEDLIDLAEAAASTPLQTLLKR 207
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1237881473 241 EDEQAFAKLNAENLMFCEDAARRLKQSIENNSNISGYWFKVEHQESLHAHNAV 293
Cdd:PRK13674  208 PDEKAVTELAYENPMFVEDAARRVAAALEADPRISAFRVEVEHFESIHNHDAV 260
FolE2 COG1469
GTP cyclohydrolase FolE2 [Coenzyme transport and metabolism]; GTP cyclohydrolase FolE2 is part ...
5-293 2.00e-90

GTP cyclohydrolase FolE2 [Coenzyme transport and metabolism]; GTP cyclohydrolase FolE2 is part of the Pathway/BioSystem: Folate biosynthesis


Pssm-ID: 441078  Cd Length: 271  Bit Score: 270.10  E-value: 2.00e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237881473   5 LPDITSGQyALTQLPLRWVGMEAIAIPLEVPISDFTILSVNAKADIFVSLDkPEAKGIHMSRLYLKLkDKLTSYNLNGEM 84
Cdd:COG1469     2 LPDVQSSP-DDRNIPLDRVGIKGVRLPVRIADKDGGPQHTVATFDMYVDLP-ADQKGTHMSRFVEVL-DEHLEEALSVES 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237881473  85 LTELLHEIISSQEglSEAAKINLSFELTIRKNALLSNEFGYQSYPISIS-RSYVHGKTVTELSLTIPYSSTCPCSSALSR 163
Cdd:COG1469    79 LEALLEEMAERLY--AERAEVEMRFPYFIRKKAPVSGLSGLEDYDVTLEaELDRDGEFRKTLGVEVPVTSLCPCSKEISR 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237881473 164 QAlsdkldqsfasinidknellqwiISEKNTAATAHSQRSYAYLKFTLKDEHLPNLNDLILKFEQVMGTPVQTAVKREDE 243
Cdd:COG1469   157 QL-----------------------AQERGIPYGAHNQRSHATISVELDEDEDVWIEDLIDLAESAASTPVYTLLKRPDE 213
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 1237881473 244 QAFAKLNAENLMFCEDAARRLKQSIENNSNISGYWFKVEHQESLHAHNAV 293
Cdd:COG1469   214 KAVTELAYENPKFVEDAVRDVAAALVEDPRIADFRVEVENFESIHNHDAY 263
GCHY-1 pfam02649
Type I GTP cyclohydrolase folE2; This is a family of prokaryotic proteins with type I GTP ...
6-293 1.47e-84

Type I GTP cyclohydrolase folE2; This is a family of prokaryotic proteins with type I GTP cyclohydrolase activity. GTP cyclohydrolase I is the first enzyme of the de novo tetrahydrofolate biosynthetic pathway present in bacteria, fungi, and plants, and encoded in Escherichia coli by the folE gene; it is also the first enzyme of the biopterin (BH4) pathway in Homo sapiens. The invariate, highly conserved glutamate residue at position 216 in Swiss:Q5F9K6 is likely to be the substrate ligand and the metal ligand is likely to be the cysteine at position 147. The enzyme is Zinc 2+ dependent.


Pssm-ID: 460638  Cd Length: 262  Bit Score: 254.73  E-value: 1.47e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237881473   6 PDITSGQyALTQLPLRWVGMEAIAIPLEVPISDFTILSVNAKADIFVSLDkPEAKGIHMSRLYLKLKDKLTsyNLNGEML 85
Cdd:pfam02649   1 PDVQSEP-PDRNIPLDRVGVKGVRKPVRVKDKDGRPQHLVATFDLFVDLP-ADRKGIHMSRFVEALDEHEE--VLSEESL 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237881473  86 TELLHEIISSQEGlSEAAKINLSFELTIRKNALLSNEFGYQSYPISISRSYVHGKTVT-ELSLTIPYSSTCPCSSALSRQ 164
Cdd:pfam02649  77 EDILEELLERHEY-AERAEVEMRFPYFIEKKAPVSGVKGLEDYDVTLEAELDRGGGVRkELGVEVPVTTLCPCSKEISRQ 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237881473 165 AlsdkldqsfasinidknellqwiISEKNTAATAHSQRSYAYLKFTLKDEHLPNLNDLILKFEQVMGTPVQTAVKREDEQ 244
Cdd:pfam02649 156 L-----------------------IQLDGIPYGAHNQRSHATITVELKDGKFVWIEDLIDIAESSASSPVYTLLKRPDEK 212
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 1237881473 245 AFAKLNAENLMFCEDAARRLKQSIENNSNISGYWFKVEHQESLHAHNAV 293
Cdd:pfam02649 213 AVTERAYENPKFVEDVVRDVAARLNADPRVEAFRVEVENFESIHNHNAY 261
TIGR00294 TIGR00294
GTP cyclohydrolase, MptA/FolE2 family; This family includes type I GTP cyclohydrolases ...
49-293 5.81e-08

GTP cyclohydrolase, MptA/FolE2 family; This family includes type I GTP cyclohydrolases involved in methanopterin in archaea (MptA) and de novo tetrahydrofolate biosynthesis in bacteria (FolE2). [Biosynthesis of cofactors, prosthetic groups, and carriers, Other]


Pssm-ID: 129395  Cd Length: 308  Bit Score: 52.94  E-value: 5.81e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237881473  49 DIFVSLDKPEaKGIHMSRLYLKLKD------KLTSYNLngEMLTELLHEIISSQEGLSEAAKINLSFELTIRKNALLSNE 122
Cdd:TIGR00294  42 DVFVDLPSHQ-KGVHMSRNPEVITSvleeaeETTAANF--EMLCNEIVNQLLKKHRYATLAEVYMNSDFILSKRSPKTGQ 118
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237881473 123 FGYQSYPI-SISRSYVHGKTVTE---LSLTIPYSSTCPCSSALSRQALSDKLDQ-SFASINIDKnellqwiiSEKNTAAT 197
Cdd:TIGR00294 119 FTQELAKImGTASGTRDDDFIFErkmVGAEVVGITACPCAQELVKEKSQPFLQEaGFSDETIPK--------ILDIVEFA 190
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237881473 198 AHSQRSYAYLKFTLKDEHLPNLNDLILKFEQVMGTPVQTAVKREDEQAFAKLNAENLMFCEDAARRLKQSIENNSNISGY 277
Cdd:TIGR00294 191 THNQRGRGRIFTEVPSLPSIVIADLIDIAESSMSAELHEILKRPDEKAVVETAHENPRFVEDCVRLMAARLVELFPHLPD 270
                         250       260
                  ....*....|....*....|
gi 1237881473 278 WFKVE----HQESLHAHNAV 293
Cdd:TIGR00294 271 DTEVEcrqiNEESIHRHNAF 290
 
Name Accession Description Interval E-value
PRK13674 PRK13674
GTP cyclohydrolase I FolE2;
1-293 3.60e-104

GTP cyclohydrolase I FolE2;


Pssm-ID: 237466  Cd Length: 271  Bit Score: 305.19  E-value: 3.60e-104
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237881473   1 MNINLPDITSGQyALTQLPLRWVGMEAIAIPLEVPISDFTILSVNAKADIFVSLDkPEAKGIHMSRLYLKLkDKLTSYNL 80
Cdd:PRK13674    5 MKATMPDVQSTP-DTRLIPIDWVGIKNIRLPVRVDTRDGGTQTTVARVDLTVSLP-ADFKGIHMSRLYELL-EEHAEQEL 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237881473  81 NGEMLTELLHEIISSQEglSEAAKINLSFELTIRKNALLSNEFGYQSYPISISRSYVHGKTVTELSLTIPYSSTCPCSSA 160
Cdd:PRK13674   82 SPASLEQLLRDMLESLE--SRAARIEVSFPYFLRKPAPVSGLSGWKDYPVTLEAELRDGVFRLELKVEVPVSSLCPCSKA 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237881473 161 LSRQalsdkldqsfasinidknellqwiisekntaaTAHSQRSYAYLKFTLKDEHLPNLNDLILKFEQVMGTPVQTAVKR 240
Cdd:PRK13674  160 ISRY--------------------------------TAHSQRSVATVKVRLAADAQLWIEDLIDLAEAAASTPLQTLLKR 207
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1237881473 241 EDEQAFAKLNAENLMFCEDAARRLKQSIENNSNISGYWFKVEHQESLHAHNAV 293
Cdd:PRK13674  208 PDEKAVTELAYENPMFVEDAARRVAAALEADPRISAFRVEVEHFESIHNHDAV 260
FolE2 COG1469
GTP cyclohydrolase FolE2 [Coenzyme transport and metabolism]; GTP cyclohydrolase FolE2 is part ...
5-293 2.00e-90

GTP cyclohydrolase FolE2 [Coenzyme transport and metabolism]; GTP cyclohydrolase FolE2 is part of the Pathway/BioSystem: Folate biosynthesis


Pssm-ID: 441078  Cd Length: 271  Bit Score: 270.10  E-value: 2.00e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237881473   5 LPDITSGQyALTQLPLRWVGMEAIAIPLEVPISDFTILSVNAKADIFVSLDkPEAKGIHMSRLYLKLkDKLTSYNLNGEM 84
Cdd:COG1469     2 LPDVQSSP-DDRNIPLDRVGIKGVRLPVRIADKDGGPQHTVATFDMYVDLP-ADQKGTHMSRFVEVL-DEHLEEALSVES 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237881473  85 LTELLHEIISSQEglSEAAKINLSFELTIRKNALLSNEFGYQSYPISIS-RSYVHGKTVTELSLTIPYSSTCPCSSALSR 163
Cdd:COG1469    79 LEALLEEMAERLY--AERAEVEMRFPYFIRKKAPVSGLSGLEDYDVTLEaELDRDGEFRKTLGVEVPVTSLCPCSKEISR 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237881473 164 QAlsdkldqsfasinidknellqwiISEKNTAATAHSQRSYAYLKFTLKDEHLPNLNDLILKFEQVMGTPVQTAVKREDE 243
Cdd:COG1469   157 QL-----------------------AQERGIPYGAHNQRSHATISVELDEDEDVWIEDLIDLAESAASTPVYTLLKRPDE 213
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 1237881473 244 QAFAKLNAENLMFCEDAARRLKQSIENNSNISGYWFKVEHQESLHAHNAV 293
Cdd:COG1469   214 KAVTELAYENPKFVEDAVRDVAAALVEDPRIADFRVEVENFESIHNHDAY 263
GCHY-1 pfam02649
Type I GTP cyclohydrolase folE2; This is a family of prokaryotic proteins with type I GTP ...
6-293 1.47e-84

Type I GTP cyclohydrolase folE2; This is a family of prokaryotic proteins with type I GTP cyclohydrolase activity. GTP cyclohydrolase I is the first enzyme of the de novo tetrahydrofolate biosynthetic pathway present in bacteria, fungi, and plants, and encoded in Escherichia coli by the folE gene; it is also the first enzyme of the biopterin (BH4) pathway in Homo sapiens. The invariate, highly conserved glutamate residue at position 216 in Swiss:Q5F9K6 is likely to be the substrate ligand and the metal ligand is likely to be the cysteine at position 147. The enzyme is Zinc 2+ dependent.


Pssm-ID: 460638  Cd Length: 262  Bit Score: 254.73  E-value: 1.47e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237881473   6 PDITSGQyALTQLPLRWVGMEAIAIPLEVPISDFTILSVNAKADIFVSLDkPEAKGIHMSRLYLKLKDKLTsyNLNGEML 85
Cdd:pfam02649   1 PDVQSEP-PDRNIPLDRVGVKGVRKPVRVKDKDGRPQHLVATFDLFVDLP-ADRKGIHMSRFVEALDEHEE--VLSEESL 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237881473  86 TELLHEIISSQEGlSEAAKINLSFELTIRKNALLSNEFGYQSYPISISRSYVHGKTVT-ELSLTIPYSSTCPCSSALSRQ 164
Cdd:pfam02649  77 EDILEELLERHEY-AERAEVEMRFPYFIEKKAPVSGVKGLEDYDVTLEAELDRGGGVRkELGVEVPVTTLCPCSKEISRQ 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237881473 165 AlsdkldqsfasinidknellqwiISEKNTAATAHSQRSYAYLKFTLKDEHLPNLNDLILKFEQVMGTPVQTAVKREDEQ 244
Cdd:pfam02649 156 L-----------------------IQLDGIPYGAHNQRSHATITVELKDGKFVWIEDLIDIAESSASSPVYTLLKRPDEK 212
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 1237881473 245 AFAKLNAENLMFCEDAARRLKQSIENNSNISGYWFKVEHQESLHAHNAV 293
Cdd:pfam02649 213 AVTERAYENPKFVEDVVRDVAARLNADPRVEAFRVEVENFESIHNHNAY 261
PRK13675 PRK13675
GTP cyclohydrolase; Provisional
49-292 7.41e-15

GTP cyclohydrolase; Provisional


Pssm-ID: 184232  Cd Length: 308  Bit Score: 73.43  E-value: 7.41e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237881473  49 DIFVSLdKPEAKGIHMSRlylklkdkltsynlNGEMLTELLHEIISSQ----EGLSEA--------------AKINLSFE 110
Cdd:PRK13675   47 EVFVDL-PSDRKGIHMSR--------------NVEVIDEVLEEAVEEEvyeiEDLCGDiakrllekheyatrAEVRMRSE 111
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237881473 111 LTIRKNALLSNEFGYQSYPISISRSYVHGKTVTEL------SLTIpysstCPCSSALSRQALSDKLdqsfASINIDKNEL 184
Cdd:PRK13675  112 YMMRRETPVSKKKSQEVVDIIAGAIATRDGNVRKEigaevvGMTA-----CPCAQEMMKERARKKL----AELGVDEETI 182
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237881473 185 LqwIISEKNTAATaHSQRSYAYLKFTLKDEHLPNLNDLILKFEQVMGTPVQTAVKREDEQAFAKLNAENLMFCEDAARRL 264
Cdd:PRK13675  183 E--KFLDNVPMAT-HNQRGRGTLTIEVPGDEDVSLEDIIDIIESSMSSPIYELLKRPDENAVVYEAHKNPKFVEDCVREM 259
                         250       260       270
                  ....*....|....*....|....*....|....*
gi 1237881473 265 KQSI-------ENNSNISgywFKVEHQESLHAHNA 292
Cdd:PRK13675  260 AKKVveefphlPDDAVVT---VRQINEESIHRHNA 291
TIGR00294 TIGR00294
GTP cyclohydrolase, MptA/FolE2 family; This family includes type I GTP cyclohydrolases ...
49-293 5.81e-08

GTP cyclohydrolase, MptA/FolE2 family; This family includes type I GTP cyclohydrolases involved in methanopterin in archaea (MptA) and de novo tetrahydrofolate biosynthesis in bacteria (FolE2). [Biosynthesis of cofactors, prosthetic groups, and carriers, Other]


Pssm-ID: 129395  Cd Length: 308  Bit Score: 52.94  E-value: 5.81e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237881473  49 DIFVSLDKPEaKGIHMSRLYLKLKD------KLTSYNLngEMLTELLHEIISSQEGLSEAAKINLSFELTIRKNALLSNE 122
Cdd:TIGR00294  42 DVFVDLPSHQ-KGVHMSRNPEVITSvleeaeETTAANF--EMLCNEIVNQLLKKHRYATLAEVYMNSDFILSKRSPKTGQ 118
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237881473 123 FGYQSYPI-SISRSYVHGKTVTE---LSLTIPYSSTCPCSSALSRQALSDKLDQ-SFASINIDKnellqwiiSEKNTAAT 197
Cdd:TIGR00294 119 FTQELAKImGTASGTRDDDFIFErkmVGAEVVGITACPCAQELVKEKSQPFLQEaGFSDETIPK--------ILDIVEFA 190
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237881473 198 AHSQRSYAYLKFTLKDEHLPNLNDLILKFEQVMGTPVQTAVKREDEQAFAKLNAENLMFCEDAARRLKQSIENNSNISGY 277
Cdd:TIGR00294 191 THNQRGRGRIFTEVPSLPSIVIADLIDIAESSMSAELHEILKRPDEKAVVETAHENPRFVEDCVRLMAARLVELFPHLPD 270
                         250       260
                  ....*....|....*....|
gi 1237881473 278 WFKVE----HQESLHAHNAV 293
Cdd:TIGR00294 271 DTEVEcrqiNEESIHRHNAF 290
 
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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