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Conserved domains on  [gi|15600732|ref|NP_254226|]
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GTP cyclohydrolase [Pseudomonas aeruginosa PAO1]

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;
1-295 1.27e-112

GTP cyclohydrolase I FolE2;


:

Pssm-ID: 237466  Cd Length: 271  Bit Score: 326.37  E-value: 1.27e-112
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600732    1 MNALTLPDIARQTTTADLPLDWVGMQGIALPVQI-----GGQRVAAEADAGVSLDdPQARGIHMSRLYLALAELEQGELD 75
Cdd:PRK13674   4 MMKATMPDVQSTPDTRLIPIDWVGIKNIRLPVRVdtrdgGTQTTVARVDLTVSLP-ADFKGIHMSRLYELLEEHAEQELS 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600732   76 LSCLRAVLQRFLDSHAglSRRAYLRLRLAPLLRRPALVSPLSGWKRYPLVLDTRLEGDDFQAEVHLELTYSSTCPCSAAL 155
Cdd:PRK13674  83 PASLEQLLRDMLESLE--SRAARIEVSFPYFLRKPAPVSGLSGWKDYPVTLEAELRDGVFRLELKVEVPVSSLCPCSKAI 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600732  156 ARQliqerfdqdfagqpldhasvlawlgssagivaTPHSQRSSAHLRIGLAEDCiGLPLEELADLGESALGTAVQTAVKR 235
Cdd:PRK13674 161 SRY--------------------------------TAHSQRSVATVKVRLAADA-QLWIEDLIDLAEAAASTPLQTLLKR 207
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600732  236 ADEQAFALANGQNLMFCEDAVRRLHRALQGYPQASRFSIRVVHAESLHAHDAVAESHWQR 295
Cdd:PRK13674 208 PDEKAVTELAYENPMFVEDAARRVAAALEADPRISAFRVEVEHFESIHNHDAVAVIEKDK 267
 
Name Accession Description Interval E-value
PRK13674 PRK13674
GTP cyclohydrolase I FolE2;
1-295 1.27e-112

GTP cyclohydrolase I FolE2;


Pssm-ID: 237466  Cd Length: 271  Bit Score: 326.37  E-value: 1.27e-112
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600732    1 MNALTLPDIARQTTTADLPLDWVGMQGIALPVQI-----GGQRVAAEADAGVSLDdPQARGIHMSRLYLALAELEQGELD 75
Cdd:PRK13674   4 MMKATMPDVQSTPDTRLIPIDWVGIKNIRLPVRVdtrdgGTQTTVARVDLTVSLP-ADFKGIHMSRLYELLEEHAEQELS 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600732   76 LSCLRAVLQRFLDSHAglSRRAYLRLRLAPLLRRPALVSPLSGWKRYPLVLDTRLEGDDFQAEVHLELTYSSTCPCSAAL 155
Cdd:PRK13674  83 PASLEQLLRDMLESLE--SRAARIEVSFPYFLRKPAPVSGLSGWKDYPVTLEAELRDGVFRLELKVEVPVSSLCPCSKAI 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600732  156 ARQliqerfdqdfagqpldhasvlawlgssagivaTPHSQRSSAHLRIGLAEDCiGLPLEELADLGESALGTAVQTAVKR 235
Cdd:PRK13674 161 SRY--------------------------------TAHSQRSVATVKVRLAADA-QLWIEDLIDLAEAAASTPLQTLLKR 207
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600732  236 ADEQAFALANGQNLMFCEDAVRRLHRALQGYPQASRFSIRVVHAESLHAHDAVAESHWQR 295
Cdd:PRK13674 208 PDEKAVTELAYENPMFVEDAARRVAAALEADPRISAFRVEVEHFESIHNHDAVAVIEKDK 267
FolE2 COG1469
GTP cyclohydrolase FolE2 [Coenzyme transport and metabolism]; GTP cyclohydrolase FolE2 is part ...
5-290 1.41e-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: 1.41e-90
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600732   5 TLPDIARQTTTADLPLDWVGMQGIALPVQI-----GGQRVAAEADAGVSLDdPQARGIHMSRLYLALAELEQGELDLSCL 79
Cdd:COG1469   1 TLPDVQSSPDDRNIPLDRVGIKGVRLPVRIadkdgGPQHTVATFDMYVDLP-ADQKGTHMSRFVEVLDEHLEEALSVESL 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600732  80 RAVLQRFLDSHagLSRRAYLRLRLAPLLRRPALVSPLSGWKRYPLVLDTRLEGDD-FQAEVHLELTYSSTCPCSAALARQ 158
Cdd:COG1469  80 EALLEEMAERL--YAERAEVEMRFPYFIRKKAPVSGLSGLEDYDVTLEAELDRDGeFRKTLGVEVPVTSLCPCSKEISRQ 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600732 159 LIQERfdqdfagqpldhasvlawlgssaGIVATPHSQRSSAHLRIGLAEDCIgLPLEELADLGESALGTAVQTAVKRADE 238
Cdd:COG1469 158 LAQER-----------------------GIPYGAHNQRSHATISVELDEDED-VWIEDLIDLAESAASTPVYTLLKRPDE 213
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|..
gi 15600732 239 QAFALANGQNLMFCEDAVRRLHRALQGYPQASRFSIRVVHAESLHAHDAVAE 290
Cdd:COG1469 214 KAVTELAYENPKFVEDAVRDVAAALVEDPRIADFRVEVENFESIHNHDAYAE 265
GCHY-1 pfam02649
Type I GTP cyclohydrolase folE2; This is a family of prokaryotic proteins with type I GTP ...
7-289 4.41e-89

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: 266.29  E-value: 4.41e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600732     7 PDIARQTTTADLPLDWVGMQGIALPVQI-----GGQRVAAEADAGVSLDdPQARGIHMSRLYLALAELEQgELDLSCLRA 81
Cdd:pfam02649   1 PDVQSEPPDRNIPLDRVGVKGVRKPVRVkdkdgRPQHLVATFDLFVDLP-ADRKGIHMSRFVEALDEHEE-VLSEESLED 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600732    82 VLQRFLDSHAGlSRRAYLRLRLAPLLRRPALVSPLSGWKRYPLVLDTRLE-GDDFQAEVHLELTYSSTCPCSAALARQLI 160
Cdd:pfam02649  79 ILEELLERHEY-AERAEVEMRFPYFIEKKAPVSGVKGLEDYDVTLEAELDrGGGVRKELGVEVPVTTLCPCSKEISRQLI 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600732   161 QERfdqdfagqpldhasvlawlgssaGIVATPHSQRSSAHLRIGLAEDCIgLPLEELADLGESALGTAVQTAVKRADEQA 240
Cdd:pfam02649 158 QLD-----------------------GIPYGAHNQRSHATITVELKDGKF-VWIEDLIDIAESSASSPVYTLLKRPDEKA 213
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 15600732   241 FALANGQNLMFCEDAVRRLHRALQGYPQASRFSIRVVHAESLHAHDAVA 289
Cdd:pfam02649 214 VTERAYENPKFVEDVVRDVAARLNADPRVEAFRVEVENFESIHNHNAYA 262
TIGR00294 TIGR00294
GTP cyclohydrolase, MptA/FolE2 family; This family includes type I GTP cyclohydrolases ...
20-290 1.11e-11

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: 64.11  E-value: 1.11e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600732    20 LDWVGMQGIA--LPVQIGGQR---VAAEADAGVSLDDPQaRGIHMSR-------LYLALAELEQGELDLSCLRAVlQRFL 87
Cdd:TIGR00294  13 LTRVGVTGIKklVPVEREGKRpiiLISTFDVFVDLPSHQ-KGVHMSRnpevitsVLEEAEETTAANFEMLCNEIV-NQLL 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600732    88 DSHaglsRRAYLRLRLAPLLRRPALVSPLSGWKRYPLV--LDTRLEG--DDFQAE---VHLELTYSSTCPCSAALARQLI 160
Cdd:TIGR00294  91 KKH----RYATLAEVYMNSDFILSKRSPKTGQFTQELAkiMGTASGTrdDDFIFErkmVGAEVVGITACPCAQELVKEKS 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600732   161 QER-----FDQDFAGQPLDhasvlawlgssAGIVATpHSQRSSAHLRIGLAEDcIGLPLEELADLGESALGTAVQTAVKR 235
Cdd:TIGR00294 167 QPFlqeagFSDETIPKILD-----------IVEFAT-HNQRGRGRIFTEVPSL-PSIVIADLIDIAESSMSAELHEILKR 233
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 15600732   236 ADEQAFALANGQNLMFCEDAVRRL-HRALQGY---PQASRFSIRVVHAESLHAHDAVAE 290
Cdd:TIGR00294 234 PDEKAVVETAHENPRFVEDCVRLMaARLVELFphlPDDTEVECRQINEESIHRHNAFAE 292
 
Name Accession Description Interval E-value
PRK13674 PRK13674
GTP cyclohydrolase I FolE2;
1-295 1.27e-112

GTP cyclohydrolase I FolE2;


Pssm-ID: 237466  Cd Length: 271  Bit Score: 326.37  E-value: 1.27e-112
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600732    1 MNALTLPDIARQTTTADLPLDWVGMQGIALPVQI-----GGQRVAAEADAGVSLDdPQARGIHMSRLYLALAELEQGELD 75
Cdd:PRK13674   4 MMKATMPDVQSTPDTRLIPIDWVGIKNIRLPVRVdtrdgGTQTTVARVDLTVSLP-ADFKGIHMSRLYELLEEHAEQELS 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600732   76 LSCLRAVLQRFLDSHAglSRRAYLRLRLAPLLRRPALVSPLSGWKRYPLVLDTRLEGDDFQAEVHLELTYSSTCPCSAAL 155
Cdd:PRK13674  83 PASLEQLLRDMLESLE--SRAARIEVSFPYFLRKPAPVSGLSGWKDYPVTLEAELRDGVFRLELKVEVPVSSLCPCSKAI 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600732  156 ARQliqerfdqdfagqpldhasvlawlgssagivaTPHSQRSSAHLRIGLAEDCiGLPLEELADLGESALGTAVQTAVKR 235
Cdd:PRK13674 161 SRY--------------------------------TAHSQRSVATVKVRLAADA-QLWIEDLIDLAEAAASTPLQTLLKR 207
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600732  236 ADEQAFALANGQNLMFCEDAVRRLHRALQGYPQASRFSIRVVHAESLHAHDAVAESHWQR 295
Cdd:PRK13674 208 PDEKAVTELAYENPMFVEDAARRVAAALEADPRISAFRVEVEHFESIHNHDAVAVIEKDK 267
FolE2 COG1469
GTP cyclohydrolase FolE2 [Coenzyme transport and metabolism]; GTP cyclohydrolase FolE2 is part ...
5-290 1.41e-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: 1.41e-90
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600732   5 TLPDIARQTTTADLPLDWVGMQGIALPVQI-----GGQRVAAEADAGVSLDdPQARGIHMSRLYLALAELEQGELDLSCL 79
Cdd:COG1469   1 TLPDVQSSPDDRNIPLDRVGIKGVRLPVRIadkdgGPQHTVATFDMYVDLP-ADQKGTHMSRFVEVLDEHLEEALSVESL 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600732  80 RAVLQRFLDSHagLSRRAYLRLRLAPLLRRPALVSPLSGWKRYPLVLDTRLEGDD-FQAEVHLELTYSSTCPCSAALARQ 158
Cdd:COG1469  80 EALLEEMAERL--YAERAEVEMRFPYFIRKKAPVSGLSGLEDYDVTLEAELDRDGeFRKTLGVEVPVTSLCPCSKEISRQ 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600732 159 LIQERfdqdfagqpldhasvlawlgssaGIVATPHSQRSSAHLRIGLAEDCIgLPLEELADLGESALGTAVQTAVKRADE 238
Cdd:COG1469 158 LAQER-----------------------GIPYGAHNQRSHATISVELDEDED-VWIEDLIDLAESAASTPVYTLLKRPDE 213
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|..
gi 15600732 239 QAFALANGQNLMFCEDAVRRLHRALQGYPQASRFSIRVVHAESLHAHDAVAE 290
Cdd:COG1469 214 KAVTELAYENPKFVEDAVRDVAAALVEDPRIADFRVEVENFESIHNHDAYAE 265
GCHY-1 pfam02649
Type I GTP cyclohydrolase folE2; This is a family of prokaryotic proteins with type I GTP ...
7-289 4.41e-89

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: 266.29  E-value: 4.41e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600732     7 PDIARQTTTADLPLDWVGMQGIALPVQI-----GGQRVAAEADAGVSLDdPQARGIHMSRLYLALAELEQgELDLSCLRA 81
Cdd:pfam02649   1 PDVQSEPPDRNIPLDRVGVKGVRKPVRVkdkdgRPQHLVATFDLFVDLP-ADRKGIHMSRFVEALDEHEE-VLSEESLED 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600732    82 VLQRFLDSHAGlSRRAYLRLRLAPLLRRPALVSPLSGWKRYPLVLDTRLE-GDDFQAEVHLELTYSSTCPCSAALARQLI 160
Cdd:pfam02649  79 ILEELLERHEY-AERAEVEMRFPYFIEKKAPVSGVKGLEDYDVTLEAELDrGGGVRKELGVEVPVTTLCPCSKEISRQLI 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600732   161 QERfdqdfagqpldhasvlawlgssaGIVATPHSQRSSAHLRIGLAEDCIgLPLEELADLGESALGTAVQTAVKRADEQA 240
Cdd:pfam02649 158 QLD-----------------------GIPYGAHNQRSHATITVELKDGKF-VWIEDLIDIAESSASSPVYTLLKRPDEKA 213
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 15600732   241 FALANGQNLMFCEDAVRRLHRALQGYPQASRFSIRVVHAESLHAHDAVA 289
Cdd:pfam02649 214 VTERAYENPKFVEDVVRDVAARLNADPRVEAFRVEVENFESIHNHNAYA 262
PRK13675 PRK13675
GTP cyclohydrolase; Provisional
6-290 1.32e-14

GTP cyclohydrolase; Provisional


Pssm-ID: 184232  Cd Length: 308  Bit Score: 72.66  E-value: 1.32e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600732    6 LPDIarQTTTADLP--LDWVGMQGIALPVQIG--GQRVA---AEADAGVSLddPQAR-GIHMSRLYLALAE-LEQG---- 72
Cdd:PRK13675   4 LPDV--QASEPDIKigLTRVGVTNVKKLVKIKrkGKRPIvliPTFEVFVDL--PSDRkGIHMSRNVEVIDEvLEEAveee 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600732   73 --ELDLSCLRAVlQRFLDSHAgLSRRAYLRLRLAPLLRRPALVSPLSGWKRYPLVLDTRLEGDD-FQAEVHLELTYSSTC 149
Cdd:PRK13675  80 vyEIEDLCGDIA-KRLLEKHE-YATRAEVRMRSEYMMRRETPVSKKKSQEVVDIIAGAIATRDGnVRKEIGAEVVGMTAC 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600732  150 PCsaalARQLIQERFDQDFAGQPLDHASVLAWLgsSAGIVATpHSQRSSAHLRIGLAEDcIGLPLEELADLGESALGTAV 229
Cdd:PRK13675 158 PC----AQEMMKERARKKLAELGVDEETIEKFL--DNVPMAT-HNQRGRGTLTIEVPGD-EDVSLEDIIDIIESSMSSPI 229
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15600732  230 QTAVKRADEQAFALANGQNLMFCEDAVRRL-HRALQGYPQAS---RFSIRVVHAESLHAHDAVAE 290
Cdd:PRK13675 230 YELLKRPDENAVVYEAHKNPKFVEDCVREMaKKVVEEFPHLPddaVVTVRQINEESIHRHNAFAE 294
TIGR00294 TIGR00294
GTP cyclohydrolase, MptA/FolE2 family; This family includes type I GTP cyclohydrolases ...
20-290 1.11e-11

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: 64.11  E-value: 1.11e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600732    20 LDWVGMQGIA--LPVQIGGQR---VAAEADAGVSLDDPQaRGIHMSR-------LYLALAELEQGELDLSCLRAVlQRFL 87
Cdd:TIGR00294  13 LTRVGVTGIKklVPVEREGKRpiiLISTFDVFVDLPSHQ-KGVHMSRnpevitsVLEEAEETTAANFEMLCNEIV-NQLL 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600732    88 DSHaglsRRAYLRLRLAPLLRRPALVSPLSGWKRYPLV--LDTRLEG--DDFQAE---VHLELTYSSTCPCSAALARQLI 160
Cdd:TIGR00294  91 KKH----RYATLAEVYMNSDFILSKRSPKTGQFTQELAkiMGTASGTrdDDFIFErkmVGAEVVGITACPCAQELVKEKS 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600732   161 QER-----FDQDFAGQPLDhasvlawlgssAGIVATpHSQRSSAHLRIGLAEDcIGLPLEELADLGESALGTAVQTAVKR 235
Cdd:TIGR00294 167 QPFlqeagFSDETIPKILD-----------IVEFAT-HNQRGRGRIFTEVPSL-PSIVIADLIDIAESSMSAELHEILKR 233
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 15600732   236 ADEQAFALANGQNLMFCEDAVRRL-HRALQGY---PQASRFSIRVVHAESLHAHDAVAE 290
Cdd:TIGR00294 234 PDEKAVVETAHENPRFVEDCVRLMaARLVELFphlPDDTEVECRQINEESIHRHNAFAE 292
 
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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