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Conserved domains on  [gi|1216916590|gb|ASM51685|]
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GTP cyclohydrolase I [Pseudoalteromonas espejiana DSM 9414]

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 2.10e-111

GTP cyclohydrolase I FolE2;


:

Pssm-ID: 237466  Cd Length: 271  Bit Score: 323.29  E-value: 2.10e-111
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216916590   1 MNAKSHLPDITSQPNSLNArPLQWVGMEEVSLPLHILNNKGEQLHTHAKAGIFVSLDkANAKGIHMSRLYLLLNEqLANK 80
Cdd:PRK13674    3 PMMKATMPDVQSTPDTRLI-PIDWVGIKNIRLPVRVDTRDGGTQTTVARVDLTVSLP-ADFKGIHMSRLYELLEE-HAEQ 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216916590  81 PLNGQVLTTLVEDMLSSQQglSLSAKVDLAFELVINKPALLSNQSGFQAYPVAISKTITNGVIKTELSLTIPYSSTCPCS 160
Cdd:PRK13674   80 ELSPASLEQLLRDMLESLE--SRAARIEVSFPYFLRKPAPVSGLSGWKDYPVTLEAELRDGVFRLELKVEVPVSSLCPCS 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216916590 161 AALSRQalsdavaeqfteqqldknallewltsqqgsvaTPHSQRSYAYINMSLQGEQLPDLPTLITQMEQAIGTPVQTAV 240
Cdd:PRK13674  158 KAISRY--------------------------------TAHSQRSVATVKVRLAADAQLWIEDLIDLAEAAASTPLQTLL 205
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1216916590 241 KREDEQAFAKLNAENLLFCEDAARRLKHALEQNTDICDYHFKVEHQESLHAHNAV 295
Cdd:PRK13674  206 KRPDEKAVTELAYENPMFVEDAARRVAAALEADPRISAFRVEVEHFESIHNHDAV 260
 
Name Accession Description Interval E-value
PRK13674 PRK13674
GTP cyclohydrolase I FolE2;
1-295 2.10e-111

GTP cyclohydrolase I FolE2;


Pssm-ID: 237466  Cd Length: 271  Bit Score: 323.29  E-value: 2.10e-111
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216916590   1 MNAKSHLPDITSQPNSLNArPLQWVGMEEVSLPLHILNNKGEQLHTHAKAGIFVSLDkANAKGIHMSRLYLLLNEqLANK 80
Cdd:PRK13674    3 PMMKATMPDVQSTPDTRLI-PIDWVGIKNIRLPVRVDTRDGGTQTTVARVDLTVSLP-ADFKGIHMSRLYELLEE-HAEQ 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216916590  81 PLNGQVLTTLVEDMLSSQQglSLSAKVDLAFELVINKPALLSNQSGFQAYPVAISKTITNGVIKTELSLTIPYSSTCPCS 160
Cdd:PRK13674   80 ELSPASLEQLLRDMLESLE--SRAARIEVSFPYFLRKPAPVSGLSGWKDYPVTLEAELRDGVFRLELKVEVPVSSLCPCS 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216916590 161 AALSRQalsdavaeqfteqqldknallewltsqqgsvaTPHSQRSYAYINMSLQGEQLPDLPTLITQMEQAIGTPVQTAV 240
Cdd:PRK13674  158 KAISRY--------------------------------TAHSQRSVATVKVRLAADAQLWIEDLIDLAEAAASTPLQTLL 205
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1216916590 241 KREDEQAFAKLNAENLLFCEDAARRLKHALEQNTDICDYHFKVEHQESLHAHNAV 295
Cdd:PRK13674  206 KRPDEKAVTELAYENPMFVEDAARRVAAALEADPRISAFRVEVEHFESIHNHDAV 260
FolE2 COG1469
GTP cyclohydrolase FolE2 [Coenzyme transport and metabolism]; GTP cyclohydrolase FolE2 is part ...
6-295 4.11e-100

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: 294.75  E-value: 4.11e-100
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216916590   6 HLPDITSQPNSLNaRPLQWVGMEEVSLPLHILNNKGEQLHTHAKAGIFVSLDkANAKGIHMSRLYLLLNEqLANKPLNGQ 85
Cdd:COG1469     1 TLPDVQSSPDDRN-IPLDRVGIKGVRLPVRIADKDGGPQHTVATFDMYVDLP-ADQKGTHMSRFVEVLDE-HLEEALSVE 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216916590  86 VLTTLVEDMLSSQQglSLSAKVDLAFELVINKPALLSNQSGFQAYPVAISKTIT-NGVIKTELSLTIPYSSTCPCSAALS 164
Cdd:COG1469    78 SLEALLEEMAERLY--AERAEVEMRFPYFIRKKAPVSGLSGLEDYDVTLEAELDrDGEFRKTLGVEVPVTSLCPCSKEIS 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216916590 165 RQALSdavaeqfteqqldknallewltsQQGSVATPHSQRSYAYINMSLQGEQLPDLPTLITQMEQAIGTPVQTAVKRED 244
Cdd:COG1469   156 RQLAQ-----------------------ERGIPYGAHNQRSHATISVELDEDEDVWIEDLIDLAESAASTPVYTLLKRPD 212
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1216916590 245 EQAFAKLNAENLLFCEDAARRLKHALEQNTDICDYHFKVEHQESLHAHNAV 295
Cdd:COG1469   213 EKAVTELAYENPKFVEDAVRDVAAALVEDPRIADFRVEVENFESIHNHDAY 263
GCHY-1 pfam02649
Type I GTP cyclohydrolase folE2; This is a family of prokaryotic proteins with type I GTP ...
8-295 1.39e-90

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: 270.14  E-value: 1.39e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216916590   8 PDITSQPNSLNArPLQWVGMEEVSLPLHILNNKGEQLHTHAKAGIFVSLDkANAKGIHMSRLYLLLNEQlaNKPLNGQVL 87
Cdd:pfam02649   1 PDVQSEPPDRNI-PLDRVGVKGVRKPVRVKDKDGRPQHLVATFDLFVDLP-ADRKGIHMSRFVEALDEH--EEVLSEESL 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216916590  88 TTLVEDMLSSQQGlSLSAKVDLAFELVINKPALLSNQSGFQAYPVAISKTIT-NGVIKTELSLTIPYSSTCPCSAALSRQ 166
Cdd:pfam02649  77 EDILEELLERHEY-AERAEVEMRFPYFIEKKAPVSGVKGLEDYDVTLEAELDrGGGVRKELGVEVPVTTLCPCSKEISRQ 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216916590 167 ALSdavaeqfteqqldknallewltsQQGSVATPHSQRSYAYINMSLQGEQLPDLPTLITQMEQAIGTPVQTAVKREDEQ 246
Cdd:pfam02649 156 LIQ-----------------------LDGIPYGAHNQRSHATITVELKDGKFVWIEDLIDIAESSASSPVYTLLKRPDEK 212
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 1216916590 247 AFAKLNAENLLFCEDAARRLKHALEQNTDICDYHFKVEHQESLHAHNAV 295
Cdd:pfam02649 213 AVTERAYENPKFVEDVVRDVAARLNADPRVEAFRVEVENFESIHNHNAY 261
TIGR00294 TIGR00294
GTP cyclohydrolase, MptA/FolE2 family; This family includes type I GTP cyclohydrolases ...
52-295 3.46e-07

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: 50.63  E-value: 3.46e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216916590  52 IFVSLdKANAKGIHMSR----LYLLLNEQLANKPLNGQVLTTLVEDMLSSQQGLSLSAKVDLAFELVINKPALLSNQsgF 127
Cdd:TIGR00294  43 VFVDL-PSHQKGVHMSRnpevITSVLEEAEETTAANFEMLCNEIVNQLLKKHRYATLAEVYMNSDFILSKRSPKTGQ--F 119
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216916590 128 QAYPVAISKTITNGVIKTELSLTIPYS------STCPCSAALSRQALSDAVAEQ-FTEQQLDKnallewltSQQGSVATP 200
Cdd:TIGR00294 120 TQELAKIMGTASGTRDDDFIFERKMVGaevvgiTACPCAQELVKEKSQPFLQEAgFSDETIPK--------ILDIVEFAT 191
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216916590 201 HSQRSYAYINMslqgeQLPDLPT-----LITQMEQAIGTPVQTAVKREDEQAFAKLNAENLLFCEDAARRLKHALEQNTD 275
Cdd:TIGR00294 192 HNQRGRGRIFT-----EVPSLPSiviadLIDIAESSMSAELHEILKRPDEKAVVETAHENPRFVEDCVRLMAARLVELFP 266
                         250       260
                  ....*....|....*....|....
gi 1216916590 276 ICDYHFKVE----HQESLHAHNAV 295
Cdd:TIGR00294 267 HLPDDTEVEcrqiNEESIHRHNAF 290
 
Name Accession Description Interval E-value
PRK13674 PRK13674
GTP cyclohydrolase I FolE2;
1-295 2.10e-111

GTP cyclohydrolase I FolE2;


Pssm-ID: 237466  Cd Length: 271  Bit Score: 323.29  E-value: 2.10e-111
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216916590   1 MNAKSHLPDITSQPNSLNArPLQWVGMEEVSLPLHILNNKGEQLHTHAKAGIFVSLDkANAKGIHMSRLYLLLNEqLANK 80
Cdd:PRK13674    3 PMMKATMPDVQSTPDTRLI-PIDWVGIKNIRLPVRVDTRDGGTQTTVARVDLTVSLP-ADFKGIHMSRLYELLEE-HAEQ 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216916590  81 PLNGQVLTTLVEDMLSSQQglSLSAKVDLAFELVINKPALLSNQSGFQAYPVAISKTITNGVIKTELSLTIPYSSTCPCS 160
Cdd:PRK13674   80 ELSPASLEQLLRDMLESLE--SRAARIEVSFPYFLRKPAPVSGLSGWKDYPVTLEAELRDGVFRLELKVEVPVSSLCPCS 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216916590 161 AALSRQalsdavaeqfteqqldknallewltsqqgsvaTPHSQRSYAYINMSLQGEQLPDLPTLITQMEQAIGTPVQTAV 240
Cdd:PRK13674  158 KAISRY--------------------------------TAHSQRSVATVKVRLAADAQLWIEDLIDLAEAAASTPLQTLL 205
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1216916590 241 KREDEQAFAKLNAENLLFCEDAARRLKHALEQNTDICDYHFKVEHQESLHAHNAV 295
Cdd:PRK13674  206 KRPDEKAVTELAYENPMFVEDAARRVAAALEADPRISAFRVEVEHFESIHNHDAV 260
FolE2 COG1469
GTP cyclohydrolase FolE2 [Coenzyme transport and metabolism]; GTP cyclohydrolase FolE2 is part ...
6-295 4.11e-100

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: 294.75  E-value: 4.11e-100
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216916590   6 HLPDITSQPNSLNaRPLQWVGMEEVSLPLHILNNKGEQLHTHAKAGIFVSLDkANAKGIHMSRLYLLLNEqLANKPLNGQ 85
Cdd:COG1469     1 TLPDVQSSPDDRN-IPLDRVGIKGVRLPVRIADKDGGPQHTVATFDMYVDLP-ADQKGTHMSRFVEVLDE-HLEEALSVE 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216916590  86 VLTTLVEDMLSSQQglSLSAKVDLAFELVINKPALLSNQSGFQAYPVAISKTIT-NGVIKTELSLTIPYSSTCPCSAALS 164
Cdd:COG1469    78 SLEALLEEMAERLY--AERAEVEMRFPYFIRKKAPVSGLSGLEDYDVTLEAELDrDGEFRKTLGVEVPVTSLCPCSKEIS 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216916590 165 RQALSdavaeqfteqqldknallewltsQQGSVATPHSQRSYAYINMSLQGEQLPDLPTLITQMEQAIGTPVQTAVKRED 244
Cdd:COG1469   156 RQLAQ-----------------------ERGIPYGAHNQRSHATISVELDEDEDVWIEDLIDLAESAASTPVYTLLKRPD 212
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1216916590 245 EQAFAKLNAENLLFCEDAARRLKHALEQNTDICDYHFKVEHQESLHAHNAV 295
Cdd:COG1469   213 EKAVTELAYENPKFVEDAVRDVAAALVEDPRIADFRVEVENFESIHNHDAY 263
GCHY-1 pfam02649
Type I GTP cyclohydrolase folE2; This is a family of prokaryotic proteins with type I GTP ...
8-295 1.39e-90

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: 270.14  E-value: 1.39e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216916590   8 PDITSQPNSLNArPLQWVGMEEVSLPLHILNNKGEQLHTHAKAGIFVSLDkANAKGIHMSRLYLLLNEQlaNKPLNGQVL 87
Cdd:pfam02649   1 PDVQSEPPDRNI-PLDRVGVKGVRKPVRVKDKDGRPQHLVATFDLFVDLP-ADRKGIHMSRFVEALDEH--EEVLSEESL 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216916590  88 TTLVEDMLSSQQGlSLSAKVDLAFELVINKPALLSNQSGFQAYPVAISKTIT-NGVIKTELSLTIPYSSTCPCSAALSRQ 166
Cdd:pfam02649  77 EDILEELLERHEY-AERAEVEMRFPYFIEKKAPVSGVKGLEDYDVTLEAELDrGGGVRKELGVEVPVTTLCPCSKEISRQ 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216916590 167 ALSdavaeqfteqqldknallewltsQQGSVATPHSQRSYAYINMSLQGEQLPDLPTLITQMEQAIGTPVQTAVKREDEQ 246
Cdd:pfam02649 156 LIQ-----------------------LDGIPYGAHNQRSHATITVELKDGKFVWIEDLIDIAESSASSPVYTLLKRPDEK 212
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 1216916590 247 AFAKLNAENLLFCEDAARRLKHALEQNTDICDYHFKVEHQESLHAHNAV 295
Cdd:pfam02649 213 AVTERAYENPKFVEDVVRDVAARLNADPRVEAFRVEVENFESIHNHNAY 261
PRK13675 PRK13675
GTP cyclohydrolase; Provisional
52-294 1.14e-12

GTP cyclohydrolase; Provisional


Pssm-ID: 184232  Cd Length: 308  Bit Score: 67.26  E-value: 1.14e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216916590  52 IFVSLdKANAKGIHMSRLYLLLNEQLaNKPLNGQVLTtlVEDM-------LSSQQGLSLSAKVDLAFELVINKPALLSNQ 124
Cdd:PRK13675   48 VFVDL-PSDRKGIHMSRNVEVIDEVL-EEAVEEEVYE--IEDLcgdiakrLLEKHEYATRAEVRMRSEYMMRRETPVSKK 123
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216916590 125 SGFQAYPVAISKTIT-NGVIKTELSLTIPYSSTCPCS----AALSRQALSD-AVAEQFTEQQLDKNallewltsqqgSVA 198
Cdd:PRK13675  124 KSQEVVDIIAGAIATrDGNVRKEIGAEVVGMTACPCAqemmKERARKKLAElGVDEETIEKFLDNV-----------PMA 192
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216916590 199 TpHSQRSYAYINMSLQGEQLPDLPTLITQMEQAIGTPVQTAVKREDEQAFAKLNAENLLFCEDAAR--------RLKHaL 270
Cdd:PRK13675  193 T-HNQRGRGTLTIEVPGDEDVSLEDIIDIIESSMSSPIYELLKRPDENAVVYEAHKNPKFVEDCVRemakkvveEFPH-L 270
                         250       260
                  ....*....|....*....|....
gi 1216916590 271 EQNTDIcdyHFKVEHQESLHAHNA 294
Cdd:PRK13675  271 PDDAVV---TVRQINEESIHRHNA 291
TIGR00294 TIGR00294
GTP cyclohydrolase, MptA/FolE2 family; This family includes type I GTP cyclohydrolases ...
52-295 3.46e-07

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: 50.63  E-value: 3.46e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216916590  52 IFVSLdKANAKGIHMSR----LYLLLNEQLANKPLNGQVLTTLVEDMLSSQQGLSLSAKVDLAFELVINKPALLSNQsgF 127
Cdd:TIGR00294  43 VFVDL-PSHQKGVHMSRnpevITSVLEEAEETTAANFEMLCNEIVNQLLKKHRYATLAEVYMNSDFILSKRSPKTGQ--F 119
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216916590 128 QAYPVAISKTITNGVIKTELSLTIPYS------STCPCSAALSRQALSDAVAEQ-FTEQQLDKnallewltSQQGSVATP 200
Cdd:TIGR00294 120 TQELAKIMGTASGTRDDDFIFERKMVGaevvgiTACPCAQELVKEKSQPFLQEAgFSDETIPK--------ILDIVEFAT 191
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216916590 201 HSQRSYAYINMslqgeQLPDLPT-----LITQMEQAIGTPVQTAVKREDEQAFAKLNAENLLFCEDAARRLKHALEQNTD 275
Cdd:TIGR00294 192 HNQRGRGRIFT-----EVPSLPSiviadLIDIAESSMSAELHEILKRPDEKAVVETAHENPRFVEDCVRLMAARLVELFP 266
                         250       260
                  ....*....|....*....|....
gi 1216916590 276 ICDYHFKVE----HQESLHAHNAV 295
Cdd:TIGR00294 267 HLPDDTEVEcrqiNEESIHRHNAF 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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