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Conserved domains on  [gi|590120203|emb|CDN64260|]
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GTP cyclohydrolase I type 2 [Burkholderia cenocepacia H111]

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

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List of domain hits

Name Accession Description Interval E-value
PRK13674 PRK13674
GTP cyclohydrolase I FolE2;
1-304 5.89e-127

GTP cyclohydrolase I FolE2;


:

Pssm-ID: 237466  Cd Length: 271  Bit Score: 362.97  E-value: 5.89e-127
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 590120203   1 MNAALPDISLTDvAPGHRPLEWVGMQGIDLPVVVAEP-GCRRDVHARADVQVDLPApQVKGIHMSRLYWLLDWLADGEaL 79
Cdd:PRK13674   5 MKATMPDVQSTP-DTRLIPIDWVGIKNIRLPVRVDTRdGGTQTTVARVDLTVSLPA-DFKGIHMSRLYELLEEHAEQE-L 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 590120203  80 SPAGLQRVLRAMVDSHrdcDTRSARVRLHFDLLARRTALVTdGLSGWKAYPVRVDATLAGDAFALRAQVTVVYSSTCPCS 159
Cdd:PRK13674  82 SPASLEQLLRDMLESL---ESRAARIEVSFPYFLRKPAPVS-GLSGWKDYPVTLEAELRDGVFRLELKVEVPVSSLCPCS 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 590120203 160 AALSRHwieqafltafgredrvdpaavaawlkqhataaTPHSQRSEAVVSVALPADgATLGLIGLVDRVEQALGTPVQTA 239
Cdd:PRK13674 158 KAISRY--------------------------------TAHSQRSVATVKVRLAAD-AQLWIEDLIDLAEAAASTPLQTL 204
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 590120203 240 VKRADEQAFAVLNGGNLMFVEDAARRVQAALEGH--HAGPRVRVRHLESLHPHDAVAWAAPLREGGD 304
Cdd:PRK13674 205 LKRPDEKAVTELAYENPMFVEDAARRVAAALEADprISAFRVEVEHFESIHNHDAVAVIEKDKRGAA 271
 
Name Accession Description Interval E-value
PRK13674 PRK13674
GTP cyclohydrolase I FolE2;
1-304 5.89e-127

GTP cyclohydrolase I FolE2;


Pssm-ID: 237466  Cd Length: 271  Bit Score: 362.97  E-value: 5.89e-127
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 590120203   1 MNAALPDISLTDvAPGHRPLEWVGMQGIDLPVVVAEP-GCRRDVHARADVQVDLPApQVKGIHMSRLYWLLDWLADGEaL 79
Cdd:PRK13674   5 MKATMPDVQSTP-DTRLIPIDWVGIKNIRLPVRVDTRdGGTQTTVARVDLTVSLPA-DFKGIHMSRLYELLEEHAEQE-L 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 590120203  80 SPAGLQRVLRAMVDSHrdcDTRSARVRLHFDLLARRTALVTdGLSGWKAYPVRVDATLAGDAFALRAQVTVVYSSTCPCS 159
Cdd:PRK13674  82 SPASLEQLLRDMLESL---ESRAARIEVSFPYFLRKPAPVS-GLSGWKDYPVTLEAELRDGVFRLELKVEVPVSSLCPCS 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 590120203 160 AALSRHwieqafltafgredrvdpaavaawlkqhataaTPHSQRSEAVVSVALPADgATLGLIGLVDRVEQALGTPVQTA 239
Cdd:PRK13674 158 KAISRY--------------------------------TAHSQRSVATVKVRLAAD-AQLWIEDLIDLAEAAASTPLQTL 204
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 590120203 240 VKRADEQAFAVLNGGNLMFVEDAARRVQAALEGH--HAGPRVRVRHLESLHPHDAVAWAAPLREGGD 304
Cdd:PRK13674 205 LKRPDEKAVTELAYENPMFVEDAARRVAAALEADprISAFRVEVEHFESIHNHDAVAVIEKDKRGAA 271
FolE2 COG1469
GTP cyclohydrolase FolE2 [Coenzyme transport and metabolism]; GTP cyclohydrolase FolE2 is part ...
4-295 3.85e-98

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: 289.74  E-value: 3.85e-98
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 590120203   4 ALPDISLTDvAPGHRPLEWVGMQGIDLPVVVAEPGCR-RDVHARADVQVDLPApQVKGIHMSRLYWLLDWLADgEALSPA 82
Cdd:COG1469    1 TLPDVQSSP-DDRNIPLDRVGIKGVRLPVRIADKDGGpQHTVATFDMYVDLPA-DQKGTHMSRFVEVLDEHLE-EALSVE 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 590120203  83 GLQRVLRAMVDSHrdcDTRSARVRLHFDLLARRTALVTdGLSGWKAYPVRVDATL-AGDAFALRAQVTVVYSSTCPCSAA 161
Cdd:COG1469   78 SLEALLEEMAERL---YAERAEVEMRFPYFIRKKAPVS-GLSGLEDYDVTLEAELdRDGEFRKTLGVEVPVTSLCPCSKE 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 590120203 162 LSRHWIeqafltafgredrvdpaavaawlKQHATAATPHSQRSEAVVSVALPaDGATLGLIGLVDRVEQALGTPVQTAVK 241
Cdd:COG1469  154 ISRQLA-----------------------QERGIPYGAHNQRSHATISVELD-EDEDVWIEDLIDLAESAASTPVYTLLK 209
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 590120203 242 RADEQAFAVLNGGNLMFVEDAARRVQAALEGHH--AGPRVRVRHLESLHPHDAVAW 295
Cdd:COG1469  210 RPDEKAVTELAYENPKFVEDAVRDVAAALVEDPriADFRVEVENFESIHNHDAYAE 265
GCHY-1 pfam02649
Type I GTP cyclohydrolase folE2; This is a family of prokaryotic proteins with type I GTP ...
6-294 1.17e-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: 270.53  E-value: 1.17e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 590120203    6 PDISLTDvAPGHRPLEWVGMQGIDLPVVVAEPGCR-RDVHARADVQVDLPApQVKGIHMSRLYWLLDwlADGEALSPAGL 84
Cdd:pfam02649   1 PDVQSEP-PDRNIPLDRVGVKGVRKPVRVKDKDGRpQHLVATFDLFVDLPA-DRKGIHMSRFVEALD--EHEEVLSEESL 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 590120203   85 QRVLRAMVDSHRDcdTRSARVRLHFDLLARRTALVTdGLSGWKAYPVRVDATL-AGDAFALRAQVTVVYSSTCPCSAALS 163
Cdd:pfam02649  77 EDILEELLERHEY--AERAEVEMRFPYFIEKKAPVS-GVKGLEDYDVTLEAELdRGGGVRKELGVEVPVTTLCPCSKEIS 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 590120203  164 RHWIeqafltafgredrvdpaavaawlKQHATAATPHSQRSEAVVSVALPaDGATLGLIGLVDRVEQALGTPVQTAVKRA 243
Cdd:pfam02649 154 RQLI-----------------------QLDGIPYGAHNQRSHATITVELK-DGKFVWIEDLIDIAESSASSPVYTLLKRP 209
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|...
gi 590120203  244 DEQAFAVLNGGNLMFVEDAARRVQAALEGHH--AGPRVRVRHLESLHPHDAVA 294
Cdd:pfam02649 210 DEKAVTERAYENPKFVEDVVRDVAARLNADPrvEAFRVEVENFESIHNHNAYA 262
TIGR00294 TIGR00294
GTP cyclohydrolase, MptA/FolE2 family; This family includes type I GTP cyclohydrolases ...
20-294 3.24e-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: 62.96  E-value: 3.24e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 590120203   20 LEWVGMQGIDLPVVVAEPGCRRDVHARA-DVQVDLPAPQvKGIHMSRLYWLLD-WLADGEALSPAGLQRVLRAMVDS--- 94
Cdd:TIGR00294  13 LTRVGVTGIKKLVPVEREGKRPIILISTfDVFVDLPSHQ-KGVHMSRNPEVITsVLEEAEETTAANFEMLCNEIVNQllk 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 590120203   95 -HRDcdTRSARVRLHFDLLARRTALVTDGLSGwKAYPVRVDATLA--GDAFALRAQV--TVVYSSTCPCSAALSRHwIEQ 169
Cdd:TIGR00294  92 kHRY--ATLAEVYMNSDFILSKRSPKTGQFTQ-ELAKIMGTASGTrdDDFIFERKMVgaEVVGITACPCAQELVKE-KSQ 167
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 590120203  170 AFLTAFGREDRVDPAavaawLKQHATAATpHSQRSEAVVSVALPaDGATLGLIGLVDRVEQALGTPVQTAVKRADEQAFA 249
Cdd:TIGR00294 168 PFLQEAGFSDETIPK-----ILDIVEFAT-HNQRGRGRIFTEVP-SLPSIVIADLIDIAESSMSAELHEILKRPDEKAVV 240
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 590120203  250 VLNGGNLMFVEDAARRVQAAL-EGHHAGPR-----VRVRHLESLHPHDAVA 294
Cdd:TIGR00294 241 ETAHENPRFVEDCVRLMAARLvELFPHLPDdteveCRQINEESIHRHNAFA 291
 
Name Accession Description Interval E-value
PRK13674 PRK13674
GTP cyclohydrolase I FolE2;
1-304 5.89e-127

GTP cyclohydrolase I FolE2;


Pssm-ID: 237466  Cd Length: 271  Bit Score: 362.97  E-value: 5.89e-127
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 590120203   1 MNAALPDISLTDvAPGHRPLEWVGMQGIDLPVVVAEP-GCRRDVHARADVQVDLPApQVKGIHMSRLYWLLDWLADGEaL 79
Cdd:PRK13674   5 MKATMPDVQSTP-DTRLIPIDWVGIKNIRLPVRVDTRdGGTQTTVARVDLTVSLPA-DFKGIHMSRLYELLEEHAEQE-L 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 590120203  80 SPAGLQRVLRAMVDSHrdcDTRSARVRLHFDLLARRTALVTdGLSGWKAYPVRVDATLAGDAFALRAQVTVVYSSTCPCS 159
Cdd:PRK13674  82 SPASLEQLLRDMLESL---ESRAARIEVSFPYFLRKPAPVS-GLSGWKDYPVTLEAELRDGVFRLELKVEVPVSSLCPCS 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 590120203 160 AALSRHwieqafltafgredrvdpaavaawlkqhataaTPHSQRSEAVVSVALPADgATLGLIGLVDRVEQALGTPVQTA 239
Cdd:PRK13674 158 KAISRY--------------------------------TAHSQRSVATVKVRLAAD-AQLWIEDLIDLAEAAASTPLQTL 204
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 590120203 240 VKRADEQAFAVLNGGNLMFVEDAARRVQAALEGH--HAGPRVRVRHLESLHPHDAVAWAAPLREGGD 304
Cdd:PRK13674 205 LKRPDEKAVTELAYENPMFVEDAARRVAAALEADprISAFRVEVEHFESIHNHDAVAVIEKDKRGAA 271
FolE2 COG1469
GTP cyclohydrolase FolE2 [Coenzyme transport and metabolism]; GTP cyclohydrolase FolE2 is part ...
4-295 3.85e-98

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: 289.74  E-value: 3.85e-98
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 590120203   4 ALPDISLTDvAPGHRPLEWVGMQGIDLPVVVAEPGCR-RDVHARADVQVDLPApQVKGIHMSRLYWLLDWLADgEALSPA 82
Cdd:COG1469    1 TLPDVQSSP-DDRNIPLDRVGIKGVRLPVRIADKDGGpQHTVATFDMYVDLPA-DQKGTHMSRFVEVLDEHLE-EALSVE 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 590120203  83 GLQRVLRAMVDSHrdcDTRSARVRLHFDLLARRTALVTdGLSGWKAYPVRVDATL-AGDAFALRAQVTVVYSSTCPCSAA 161
Cdd:COG1469   78 SLEALLEEMAERL---YAERAEVEMRFPYFIRKKAPVS-GLSGLEDYDVTLEAELdRDGEFRKTLGVEVPVTSLCPCSKE 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 590120203 162 LSRHWIeqafltafgredrvdpaavaawlKQHATAATPHSQRSEAVVSVALPaDGATLGLIGLVDRVEQALGTPVQTAVK 241
Cdd:COG1469  154 ISRQLA-----------------------QERGIPYGAHNQRSHATISVELD-EDEDVWIEDLIDLAESAASTPVYTLLK 209
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 590120203 242 RADEQAFAVLNGGNLMFVEDAARRVQAALEGHH--AGPRVRVRHLESLHPHDAVAW 295
Cdd:COG1469  210 RPDEKAVTELAYENPKFVEDAVRDVAAALVEDPriADFRVEVENFESIHNHDAYAE 265
GCHY-1 pfam02649
Type I GTP cyclohydrolase folE2; This is a family of prokaryotic proteins with type I GTP ...
6-294 1.17e-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: 270.53  E-value: 1.17e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 590120203    6 PDISLTDvAPGHRPLEWVGMQGIDLPVVVAEPGCR-RDVHARADVQVDLPApQVKGIHMSRLYWLLDwlADGEALSPAGL 84
Cdd:pfam02649   1 PDVQSEP-PDRNIPLDRVGVKGVRKPVRVKDKDGRpQHLVATFDLFVDLPA-DRKGIHMSRFVEALD--EHEEVLSEESL 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 590120203   85 QRVLRAMVDSHRDcdTRSARVRLHFDLLARRTALVTdGLSGWKAYPVRVDATL-AGDAFALRAQVTVVYSSTCPCSAALS 163
Cdd:pfam02649  77 EDILEELLERHEY--AERAEVEMRFPYFIEKKAPVS-GVKGLEDYDVTLEAELdRGGGVRKELGVEVPVTTLCPCSKEIS 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 590120203  164 RHWIeqafltafgredrvdpaavaawlKQHATAATPHSQRSEAVVSVALPaDGATLGLIGLVDRVEQALGTPVQTAVKRA 243
Cdd:pfam02649 154 RQLI-----------------------QLDGIPYGAHNQRSHATITVELK-DGKFVWIEDLIDIAESSASSPVYTLLKRP 209
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|...
gi 590120203  244 DEQAFAVLNGGNLMFVEDAARRVQAALEGHH--AGPRVRVRHLESLHPHDAVA 294
Cdd:pfam02649 210 DEKAVTERAYENPKFVEDVVRDVAARLNADPrvEAFRVEVENFESIHNHNAYA 262
PRK13675 PRK13675
GTP cyclohydrolase; Provisional
3-301 1.54e-16

GTP cyclohydrolase; Provisional


Pssm-ID: 184232  Cd Length: 308  Bit Score: 78.44  E-value: 1.54e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 590120203   3 AALPDISLtdvapghrPLEWVGMQGIDLPVVVAEPGCRRDVH-ARADVQVDLPAPQvKGIHMSRLYWLLDwladgEALSP 81
Cdd:PRK13675   9 ASEPDIKI--------GLTRVGVTNVKKLVKIKRKGKRPIVLiPTFEVFVDLPSDR-KGIHMSRNVEVID-----EVLEE 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 590120203  82 A------GLQ----RVLRAMVDSHRdcDTRSARVRLHFDLLARRTALVTDGLSGwKAYPVRVDATlAGDAFALRAQVTV- 150
Cdd:PRK13675  75 AveeevyEIEdlcgDIAKRLLEKHE--YATRAEVRMRSEYMMRRETPVSKKKSQ-EVVDIIAGAI-ATRDGNVRKEIGAe 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 590120203 151 VYSST-CPCSAALSRHWIEQAfLTAFGREDRVDPAAVAAwlkqhATAATpHSQRSEAVVSVALPaDGATLGLIGLVDRVE 229
Cdd:PRK13675 151 VVGMTaCPCAQEMMKERARKK-LAELGVDEETIEKFLDN-----VPMAT-HNQRGRGTLTIEVP-GDEDVSLEDIIDIIE 222
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 590120203 230 QALGTPVQTAVKRADEqAFAVLNG-GNLMFVEDAARRV-QAALEGHHAGP---RVRVRHL--ESLHPHDAVA--WA--AP 298
Cdd:PRK13675 223 SSMSSPIYELLKRPDE-NAVVYEAhKNPKFVEDCVREMaKKVVEEFPHLPddaVVTVRQIneESIHRHNAFAerVAtmGE 301

                 ...
gi 590120203 299 LRE 301
Cdd:PRK13675 302 LRK 304
TIGR00294 TIGR00294
GTP cyclohydrolase, MptA/FolE2 family; This family includes type I GTP cyclohydrolases ...
20-294 3.24e-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: 62.96  E-value: 3.24e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 590120203   20 LEWVGMQGIDLPVVVAEPGCRRDVHARA-DVQVDLPAPQvKGIHMSRLYWLLD-WLADGEALSPAGLQRVLRAMVDS--- 94
Cdd:TIGR00294  13 LTRVGVTGIKKLVPVEREGKRPIILISTfDVFVDLPSHQ-KGVHMSRNPEVITsVLEEAEETTAANFEMLCNEIVNQllk 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 590120203   95 -HRDcdTRSARVRLHFDLLARRTALVTDGLSGwKAYPVRVDATLA--GDAFALRAQV--TVVYSSTCPCSAALSRHwIEQ 169
Cdd:TIGR00294  92 kHRY--ATLAEVYMNSDFILSKRSPKTGQFTQ-ELAKIMGTASGTrdDDFIFERKMVgaEVVGITACPCAQELVKE-KSQ 167
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 590120203  170 AFLTAFGREDRVDPAavaawLKQHATAATpHSQRSEAVVSVALPaDGATLGLIGLVDRVEQALGTPVQTAVKRADEQAFA 249
Cdd:TIGR00294 168 PFLQEAGFSDETIPK-----ILDIVEFAT-HNQRGRGRIFTEVP-SLPSIVIADLIDIAESSMSAELHEILKRPDEKAVV 240
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 590120203  250 VLNGGNLMFVEDAARRVQAAL-EGHHAGPR-----VRVRHLESLHPHDAVA 294
Cdd:TIGR00294 241 ETAHENPRFVEDCVRLMAARLvELFPHLPDdteveCRQINEESIHRHNAFA 291
 
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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