NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1120828165|gb|APP77505|]
View 

GTP cyclohydrolase [Xanthomonas vesicatoria ATCC 35937]

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

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

Name Accession Description Interval E-value
PRK13674 PRK13674
GTP cyclohydrolase I FolE2;
1-298 1.93e-114

GTP cyclohydrolase I FolE2;


:

Pssm-ID: 237466  Cd Length: 271  Bit Score: 331.38  E-value: 1.93e-114
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1120828165   1 MSATLPDVAVTElPTLSAPLRWVGMHDIAIPVRLDEAE-PSGTVGARASMQVDLPrPEIKGIHMSRLYRLLDRHLEQPVS 79
Cdd:PRK13674    5 MKATMPDVQSTP-DTRLIPIDWVGIKNIRLPVRVDTRDgGTQTTVARVDLTVSLP-ADFKGIHMSRLYELLEEHAEQELS 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1120828165  80 PAMVSQLLQALIDSHadcGSRAARVTLSFEVMLRTPALLSeGLAGWRAYPVRIDAQCREGRSQVQLQIDVLYASTCPCSA 159
Cdd:PRK13674   83 PASLEQLLRDMLESL---ESRAARIEVSFPYFLRKPAPVS-GLSGWKDYPVTLEAELRDGVFRLELKVEVPVSSLCPCSK 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1120828165 160 ALSRQllsdafvqhhagramvpvdeiaqwlqlhgshaTPHSQRSVAQVRVDlLACLQRLEIRTLIGVCEQALATPVQAAV 239
Cdd:PRK13674  159 AISRY--------------------------------TAHSQRSVATVKVR-LAADAQLWIEDLIDLAEAAASTPLQTLL 205
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1120828165 240 RRIDEQAFARLNGANLMYVEDAARRLRMALAE--RYTAFDVAVRHLESLHAHDAVAETGSD 298
Cdd:PRK13674  206 KRPDEKAVTELAYENPMFVEDAARRVAAALEAdpRISAFRVEVEHFESIHNHDAVAVIEKD 266
 
Name Accession Description Interval E-value
PRK13674 PRK13674
GTP cyclohydrolase I FolE2;
1-298 1.93e-114

GTP cyclohydrolase I FolE2;


Pssm-ID: 237466  Cd Length: 271  Bit Score: 331.38  E-value: 1.93e-114
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1120828165   1 MSATLPDVAVTElPTLSAPLRWVGMHDIAIPVRLDEAE-PSGTVGARASMQVDLPrPEIKGIHMSRLYRLLDRHLEQPVS 79
Cdd:PRK13674    5 MKATMPDVQSTP-DTRLIPIDWVGIKNIRLPVRVDTRDgGTQTTVARVDLTVSLP-ADFKGIHMSRLYELLEEHAEQELS 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1120828165  80 PAMVSQLLQALIDSHadcGSRAARVTLSFEVMLRTPALLSeGLAGWRAYPVRIDAQCREGRSQVQLQIDVLYASTCPCSA 159
Cdd:PRK13674   83 PASLEQLLRDMLESL---ESRAARIEVSFPYFLRKPAPVS-GLSGWKDYPVTLEAELRDGVFRLELKVEVPVSSLCPCSK 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1120828165 160 ALSRQllsdafvqhhagramvpvdeiaqwlqlhgshaTPHSQRSVAQVRVDlLACLQRLEIRTLIGVCEQALATPVQAAV 239
Cdd:PRK13674  159 AISRY--------------------------------TAHSQRSVATVKVR-LAADAQLWIEDLIDLAEAAASTPLQTLL 205
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1120828165 240 RRIDEQAFARLNGANLMYVEDAARRLRMALAE--RYTAFDVAVRHLESLHAHDAVAETGSD 298
Cdd:PRK13674  206 KRPDEKAVTELAYENPMFVEDAARRVAAALEAdpRISAFRVEVEHFESIHNHDAVAVIEKD 266
FolE2 COG1469
GTP cyclohydrolase FolE2 [Coenzyme transport and metabolism]; GTP cyclohydrolase FolE2 is part ...
4-294 3.81e-93

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: 277.03  E-value: 3.81e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1120828165   4 TLPDVAVTElPTLSAPLRWVGMHDIAIPVRLDEAEPSG-TVGARASMQVDLPrPEIKGIHMSRLYRLLDRHLEQPVSPAM 82
Cdd:COG1469     1 TLPDVQSSP-DDRNIPLDRVGIKGVRLPVRIADKDGGPqHTVATFDMYVDLP-ADQKGTHMSRFVEVLDEHLEEALSVES 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1120828165  83 VSQLLQALIDSHadcGSRAARVTLSFEVMLRTPALLSeGLAGWRAYPVRIDAQC-REGRSQVQLQIDVLYASTCPCSAAL 161
Cdd:COG1469    79 LEALLEEMAERL---YAERAEVEMRFPYFIRKKAPVS-GLSGLEDYDVTLEAELdRDGEFRKTLGVEVPVTSLCPCSKEI 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1120828165 162 SRQLLSDafvqhhagramvpvdeiaqwlqlHGSHATPHSQRSVAQVRVDLlACLQRLEIRTLIGVCEQALATPVQAAVRR 241
Cdd:COG1469   155 SRQLAQE-----------------------RGIPYGAHNQRSHATISVEL-DEDEDVWIEDLIDLAESAASTPVYTLLKR 210
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1120828165 242 IDEQAFARLNGANLMYVEDAARRLRMALAE--RYTAFDVAVRHLESLHAHDAVAE 294
Cdd:COG1469   211 PDEKAVTELAYENPKFVEDAVRDVAAALVEdpRIADFRVEVENFESIHNHDAYAE 265
GCHY-1 pfam02649
Type I GTP cyclohydrolase folE2; This is a family of prokaryotic proteins with type I GTP ...
6-293 3.11e-86

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: 259.35  E-value: 3.11e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1120828165   6 PDVAVTElPTLSAPLRWVGMHDIAIPVRL-DEAEPSGTVGARASMQVDLPrPEIKGIHMSRLYRLLDRHlEQPVSPAMVS 84
Cdd:pfam02649   1 PDVQSEP-PDRNIPLDRVGVKGVRKPVRVkDKDGRPQHLVATFDLFVDLP-ADRKGIHMSRFVEALDEH-EEVLSEESLE 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1120828165  85 QLLQALIDSHADcgSRAARVTLSFEVMLRTPALLSeGLAGWRAYPVRIDAQCREGRS-QVQLQIDVLYASTCPCSAALSR 163
Cdd:pfam02649  78 DILEELLERHEY--AERAEVEMRFPYFIEKKAPVS-GVKGLEDYDVTLEAELDRGGGvRKELGVEVPVTTLCPCSKEISR 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1120828165 164 QLLsdafvqhhagramvpvdeiaqwlQLHGSHATPHSQRSVAQVRVDLlACLQRLEIRTLIGVCEQALATPVQAAVRRID 243
Cdd:pfam02649 155 QLI-----------------------QLDGIPYGAHNQRSHATITVEL-KDGKFVWIEDLIDIAESSASSPVYTLLKRPD 210
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1120828165 244 EQAFARLNGANLMYVEDAARRLRMALAE--RYTAFDVAVRHLESLHAHDAVA 293
Cdd:pfam02649 211 EKAVTERAYENPKFVEDVVRDVAARLNAdpRVEAFRVEVENFESIHNHNAYA 262
TIGR00294 TIGR00294
GTP cyclohydrolase, MptA/FolE2 family; This family includes type I GTP cyclohydrolases ...
51-294 1.62e-09

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: 57.95  E-value: 1.62e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1120828165  51 VDLPRPEiKGIHMSRLYRLLDRHLEQPV-SPAMVSQLLQALIDSHADCGSRAAR---VTLSFEVML--RTPAL------L 118
Cdd:TIGR00294  45 VDLPSHQ-KGVHMSRNPEVITSVLEEAEeTTAANFEMLCNEIVNQLLKKHRYATlaeVYMNSDFILskRSPKTgqftqeL 123
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1120828165 119 SEGLAGWRAYpvridaqcREGRSQVQLQI---DVLYASTCPCSAALSRQllSDAFVQHHAGRAMVPVDEIaqwlqLHGSH 195
Cdd:TIGR00294 124 AKIMGTASGT--------RDDDFIFERKMvgaEVVGITACPCAQELVKE--KSQPFLQEAGFSDETIPKI-----LDIVE 188
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1120828165 196 ATPHSQRSVAQVRVDLlACLQRLEIRTLIGVCEQALATPVQAAVRRIDEQAFARLNGANLMYVEDAARRLRMALAERY-- 273
Cdd:TIGR00294 189 FATHNQRGRGRIFTEV-PSLPSIVIADLIDIAESSMSAELHEILKRPDEKAVVETAHENPRFVEDCVRLMAARLVELFph 267
                         250       260
                  ....*....|....*....|....*
gi 1120828165 274 --TAFDVAVRHL--ESLHAHDAVAE 294
Cdd:TIGR00294 268 lpDDTEVECRQIneESIHRHNAFAE 292
 
Name Accession Description Interval E-value
PRK13674 PRK13674
GTP cyclohydrolase I FolE2;
1-298 1.93e-114

GTP cyclohydrolase I FolE2;


Pssm-ID: 237466  Cd Length: 271  Bit Score: 331.38  E-value: 1.93e-114
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1120828165   1 MSATLPDVAVTElPTLSAPLRWVGMHDIAIPVRLDEAE-PSGTVGARASMQVDLPrPEIKGIHMSRLYRLLDRHLEQPVS 79
Cdd:PRK13674    5 MKATMPDVQSTP-DTRLIPIDWVGIKNIRLPVRVDTRDgGTQTTVARVDLTVSLP-ADFKGIHMSRLYELLEEHAEQELS 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1120828165  80 PAMVSQLLQALIDSHadcGSRAARVTLSFEVMLRTPALLSeGLAGWRAYPVRIDAQCREGRSQVQLQIDVLYASTCPCSA 159
Cdd:PRK13674   83 PASLEQLLRDMLESL---ESRAARIEVSFPYFLRKPAPVS-GLSGWKDYPVTLEAELRDGVFRLELKVEVPVSSLCPCSK 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1120828165 160 ALSRQllsdafvqhhagramvpvdeiaqwlqlhgshaTPHSQRSVAQVRVDlLACLQRLEIRTLIGVCEQALATPVQAAV 239
Cdd:PRK13674  159 AISRY--------------------------------TAHSQRSVATVKVR-LAADAQLWIEDLIDLAEAAASTPLQTLL 205
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1120828165 240 RRIDEQAFARLNGANLMYVEDAARRLRMALAE--RYTAFDVAVRHLESLHAHDAVAETGSD 298
Cdd:PRK13674  206 KRPDEKAVTELAYENPMFVEDAARRVAAALEAdpRISAFRVEVEHFESIHNHDAVAVIEKD 266
FolE2 COG1469
GTP cyclohydrolase FolE2 [Coenzyme transport and metabolism]; GTP cyclohydrolase FolE2 is part ...
4-294 3.81e-93

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: 277.03  E-value: 3.81e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1120828165   4 TLPDVAVTElPTLSAPLRWVGMHDIAIPVRLDEAEPSG-TVGARASMQVDLPrPEIKGIHMSRLYRLLDRHLEQPVSPAM 82
Cdd:COG1469     1 TLPDVQSSP-DDRNIPLDRVGIKGVRLPVRIADKDGGPqHTVATFDMYVDLP-ADQKGTHMSRFVEVLDEHLEEALSVES 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1120828165  83 VSQLLQALIDSHadcGSRAARVTLSFEVMLRTPALLSeGLAGWRAYPVRIDAQC-REGRSQVQLQIDVLYASTCPCSAAL 161
Cdd:COG1469    79 LEALLEEMAERL---YAERAEVEMRFPYFIRKKAPVS-GLSGLEDYDVTLEAELdRDGEFRKTLGVEVPVTSLCPCSKEI 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1120828165 162 SRQLLSDafvqhhagramvpvdeiaqwlqlHGSHATPHSQRSVAQVRVDLlACLQRLEIRTLIGVCEQALATPVQAAVRR 241
Cdd:COG1469   155 SRQLAQE-----------------------RGIPYGAHNQRSHATISVEL-DEDEDVWIEDLIDLAESAASTPVYTLLKR 210
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1120828165 242 IDEQAFARLNGANLMYVEDAARRLRMALAE--RYTAFDVAVRHLESLHAHDAVAE 294
Cdd:COG1469   211 PDEKAVTELAYENPKFVEDAVRDVAAALVEdpRIADFRVEVENFESIHNHDAYAE 265
GCHY-1 pfam02649
Type I GTP cyclohydrolase folE2; This is a family of prokaryotic proteins with type I GTP ...
6-293 3.11e-86

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: 259.35  E-value: 3.11e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1120828165   6 PDVAVTElPTLSAPLRWVGMHDIAIPVRL-DEAEPSGTVGARASMQVDLPrPEIKGIHMSRLYRLLDRHlEQPVSPAMVS 84
Cdd:pfam02649   1 PDVQSEP-PDRNIPLDRVGVKGVRKPVRVkDKDGRPQHLVATFDLFVDLP-ADRKGIHMSRFVEALDEH-EEVLSEESLE 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1120828165  85 QLLQALIDSHADcgSRAARVTLSFEVMLRTPALLSeGLAGWRAYPVRIDAQCREGRS-QVQLQIDVLYASTCPCSAALSR 163
Cdd:pfam02649  78 DILEELLERHEY--AERAEVEMRFPYFIEKKAPVS-GVKGLEDYDVTLEAELDRGGGvRKELGVEVPVTTLCPCSKEISR 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1120828165 164 QLLsdafvqhhagramvpvdeiaqwlQLHGSHATPHSQRSVAQVRVDLlACLQRLEIRTLIGVCEQALATPVQAAVRRID 243
Cdd:pfam02649 155 QLI-----------------------QLDGIPYGAHNQRSHATITVEL-KDGKFVWIEDLIDIAESSASSPVYTLLKRPD 210
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1120828165 244 EQAFARLNGANLMYVEDAARRLRMALAE--RYTAFDVAVRHLESLHAHDAVA 293
Cdd:pfam02649 211 EKAVTERAYENPKFVEDVVRDVAARLNAdpRVEAFRVEVENFESIHNHNAYA 262
PRK13675 PRK13675
GTP cyclohydrolase; Provisional
5-295 4.10e-14

GTP cyclohydrolase; Provisional


Pssm-ID: 184232  Cd Length: 308  Bit Score: 71.50  E-value: 4.10e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1120828165   5 LPDVAVTElPTLSAPLRWVGMHDIAIPVRL-DEAEPSGTVGARASMQVDLPrPEIKGIHMSRLYRLLDRHLEQPVSPA-- 81
Cdd:PRK13675    4 LPDVQASE-PDIKIGLTRVGVTNVKKLVKIkRKGKRPIVLIPTFEVFVDLP-SDRKGIHMSRNVEVIDEVLEEAVEEEvy 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1120828165  82 ----MVSQLLQALIDSHaDCGSRaARVTLSFEVMLR--TPALlseGLAGWRAYPVRIDAQC-REGRSQVQLQIDVLYAST 154
Cdd:PRK13675   82 eiedLCGDIAKRLLEKH-EYATR-AEVRMRSEYMMRreTPVS---KKKSQEVVDIIAGAIAtRDGNVRKEIGAEVVGMTA 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1120828165 155 CPCSAALSRQ-----LLSDAFVQHHAGRAMvpvDEIAQwlqlhgshATpHSQRSVAQVRVDlLACLQRLEIRTLIGVCEQ 229
Cdd:PRK13675  157 CPCAQEMMKErarkkLAELGVDEETIEKFL---DNVPM--------AT-HNQRGRGTLTIE-VPGDEDVSLEDIIDIIES 223
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1120828165 230 ALATPVQAAVRRIDEQAFARLNGANLMYVEDAARRLRMALAERYTAF-DVAVRHL-----ESLHAHDAVAET 295
Cdd:PRK13675  224 SMSSPIYELLKRPDENAVVYEAHKNPKFVEDCVREMAKKVVEEFPHLpDDAVVTVrqineESIHRHNAFAER 295
TIGR00294 TIGR00294
GTP cyclohydrolase, MptA/FolE2 family; This family includes type I GTP cyclohydrolases ...
51-294 1.62e-09

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: 57.95  E-value: 1.62e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1120828165  51 VDLPRPEiKGIHMSRLYRLLDRHLEQPV-SPAMVSQLLQALIDSHADCGSRAAR---VTLSFEVML--RTPAL------L 118
Cdd:TIGR00294  45 VDLPSHQ-KGVHMSRNPEVITSVLEEAEeTTAANFEMLCNEIVNQLLKKHRYATlaeVYMNSDFILskRSPKTgqftqeL 123
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1120828165 119 SEGLAGWRAYpvridaqcREGRSQVQLQI---DVLYASTCPCSAALSRQllSDAFVQHHAGRAMVPVDEIaqwlqLHGSH 195
Cdd:TIGR00294 124 AKIMGTASGT--------RDDDFIFERKMvgaEVVGITACPCAQELVKE--KSQPFLQEAGFSDETIPKI-----LDIVE 188
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1120828165 196 ATPHSQRSVAQVRVDLlACLQRLEIRTLIGVCEQALATPVQAAVRRIDEQAFARLNGANLMYVEDAARRLRMALAERY-- 273
Cdd:TIGR00294 189 FATHNQRGRGRIFTEV-PSLPSIVIADLIDIAESSMSAELHEILKRPDEKAVVETAHENPRFVEDCVRLMAARLVELFph 267
                         250       260
                  ....*....|....*....|....*
gi 1120828165 274 --TAFDVAVRHL--ESLHAHDAVAE 294
Cdd:TIGR00294 268 lpDDTEVECRQIneESIHRHNAFAE 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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH