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Conserved domains on  [gi|491102488|ref|WP_004964088|]
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MULTISPECIES: GTP cyclohydrolase MptA [Haloarcula]

Protein Classification

GTP cyclohydrolase IV( domain architecture ID 10014325)

GTP cyclohydrolase IV converts GTP to 7,8-dihydro-D-neopterin 2',3'-cyclic phosphate, the first intermediate in the biosynthesis of coenzyme methanopterin

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PRK13675 PRK13675
GTP cyclohydrolase; Provisional
2-308 0e+00

GTP cyclohydrolase; Provisional


:

Pssm-ID: 184232  Cd Length: 308  Bit Score: 512.94  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491102488   2 SQQLPDVQASSPDVTVGLNRVGVTGVEKLVKLGRRDRDPIVLMAEFEVFVDLPSWRKGADMSRNMEVIDETLETAVSEEA 81
Cdd:PRK13675   1 MMQLPDVQASEPDIKIGLTRVGVTNVKKLVKIKRKGKRPIVLIPTFEVFVDLPSDRKGIHMSRNVEVIDEVLEEAVEEEV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491102488  82 YRVEDVCGDAAELLLEKHDYTTKAEVRMEAEYVTHESTPASEMATQSTADIIASATATEDG-TSEEIGARVTGMTVCPCS 160
Cdd:PRK13675  81 YEIEDLCGDIAKRLLEKHEYATRAEVRMRSEYMMRRETPVSKKKSQEVVDIIAGAIATRDGnVRKEIGAEVVGMTACPCA 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491102488 161 QGMSASRARETLKQLNVEDDVIEEFLETNPQAGHSQRGHATLTVQSDGAPEVDLNELIEVARDSMSARIYNLAKRPDEDH 240
Cdd:PRK13675 161 QEMMKERARKKLAELGVDEETIEKFLDNVPMATHNQRGRGTLTIEVPGDEDVSLEDIIDIIESSMSSPIYELLKRPDENA 240
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 491102488 241 MTYEAHKDAKFVEDCVRALAEGVVNTFPDLPDDAVVTMKQSNDESIHQHNAHAERVAQLDDLRQEVSE 308
Cdd:PRK13675 241 VVYEAHKNPKFVEDCVREMAKKVVEEFPHLPDDAVVTVRQINEESIHRHNAFAERVATMGELRKELNA 308
 
Name Accession Description Interval E-value
PRK13675 PRK13675
GTP cyclohydrolase; Provisional
2-308 0e+00

GTP cyclohydrolase; Provisional


Pssm-ID: 184232  Cd Length: 308  Bit Score: 512.94  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491102488   2 SQQLPDVQASSPDVTVGLNRVGVTGVEKLVKLGRRDRDPIVLMAEFEVFVDLPSWRKGADMSRNMEVIDETLETAVSEEA 81
Cdd:PRK13675   1 MMQLPDVQASEPDIKIGLTRVGVTNVKKLVKIKRKGKRPIVLIPTFEVFVDLPSDRKGIHMSRNVEVIDEVLEEAVEEEV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491102488  82 YRVEDVCGDAAELLLEKHDYTTKAEVRMEAEYVTHESTPASEMATQSTADIIASATATEDG-TSEEIGARVTGMTVCPCS 160
Cdd:PRK13675  81 YEIEDLCGDIAKRLLEKHEYATRAEVRMRSEYMMRRETPVSKKKSQEVVDIIAGAIATRDGnVRKEIGAEVVGMTACPCA 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491102488 161 QGMSASRARETLKQLNVEDDVIEEFLETNPQAGHSQRGHATLTVQSDGAPEVDLNELIEVARDSMSARIYNLAKRPDEDH 240
Cdd:PRK13675 161 QEMMKERARKKLAELGVDEETIEKFLDNVPMATHNQRGRGTLTIEVPGDEDVSLEDIIDIIESSMSSPIYELLKRPDENA 240
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 491102488 241 MTYEAHKDAKFVEDCVRALAEGVVNTFPDLPDDAVVTMKQSNDESIHQHNAHAERVAQLDDLRQEVSE 308
Cdd:PRK13675 241 VVYEAHKNPKFVEDCVREMAKKVVEEFPHLPDDAVVTVRQINEESIHRHNAFAERVATMGELRKELNA 308
FolE2 COG1469
GTP cyclohydrolase FolE2 [Coenzyme transport and metabolism]; GTP cyclohydrolase FolE2 is part ...
4-296 6.14e-111

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: 322.48  E-value: 6.14e-111
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491102488   4 QLPDVQASSPDVTVGLNRVGVTGVEKLVKLGRRDRDPIVLMAEFEVFVDLPSWRKGADMSRNMEVIDETLETAVSeeAYR 83
Cdd:COG1469    1 TLPDVQSSPDDRNIPLDRVGIKGVRLPVRIADKDGGPQHTVATFDMYVDLPADQKGTHMSRFVEVLDEHLEEALS--VES 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491102488  84 VEDVCGDAAELLlekhdYTTKAEVRMEAEYVTHESTPASEMATQSTADIIASATATEDG-TSEEIGARVTGMTVCPCSQG 162
Cdd:COG1469   79 LEALLEEMAERL-----YAERAEVEMRFPYFIRKKAPVSGLSGLEDYDVTLEAELDRDGeFRKTLGVEVPVTSLCPCSKE 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491102488 163 MSASRAREtlkqlnveddvieeflETNPQAGHSQRGHATLTVQSDGAPEVDLNELIEVARDSMSARIYNLAKRPDEDHMT 242
Cdd:COG1469  154 ISRQLAQE----------------RGIPYGAHNQRSHATISVELDEDEDVWIEDLIDLAESAASTPVYTLLKRPDEKAVT 217
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....
gi 491102488 243 YEAHKDAKFVEDCVRALAEGVVntfpDLPDDAVVTMKQSNDESIHQHNAHAERV 296
Cdd:COG1469  218 ELAYENPKFVEDAVRDVAAALV----EDPRIADFRVEVENFESIHNHDAYAEIE 267
GCHY-1 pfam02649
Type I GTP cyclohydrolase folE2; This is a family of prokaryotic proteins with type I GTP ...
6-293 1.83e-101

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: 297.87  E-value: 1.83e-101
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491102488    6 PDVQASSPDVTVGLNRVGVTGVEKLVKLGRRDRDPIVLMAEFEVFVDLPSWRKGADMSRNMEVIDETLETAvseEAYRVE 85
Cdd:pfam02649   1 PDVQSEPPDRNIPLDRVGVKGVRKPVRVKDKDGRPQHLVATFDLFVDLPADRKGIHMSRFVEALDEHEEVL---SEESLE 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491102488   86 DVcgdaAELLLEKHDYTTKAEVRMEAEYVTHESTPASEMATQSTADIIASATATEDGTSE-EIGARVTGMTVCPCSQGMS 164
Cdd:pfam02649  78 DI----LEELLERHEYAERAEVEMRFPYFIEKKAPVSGVKGLEDYDVTLEAELDRGGGVRkELGVEVPVTTLCPCSKEIS 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491102488  165 ASRARetlkqlnveddvieefLETNPQAGHSQRGHATLTVQSDGAPEVDLNELIEVARDSMSARIYNLAKRPDEDHMTYE 244
Cdd:pfam02649 154 RQLIQ----------------LDGIPYGAHNQRSHATITVELKDGKFVWIEDLIDIAESSASSPVYTLLKRPDEKAVTER 217
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 491102488  245 AHKDAKFVEDCVRALAEGVvntfpdLPDDAVV--TMKQSNDESIHQHNAHA 293
Cdd:pfam02649 218 AYENPKFVEDVVRDVAARL------NADPRVEafRVEVENFESIHNHNAYA 262
TIGR00294 TIGR00294
GTP cyclohydrolase, MptA/FolE2 family; This family includes type I GTP cyclohydrolases ...
7-308 8.47e-92

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: 275.20  E-value: 8.47e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491102488    7 DVQASSPDVTVGLNRVGVTGVEKLVKLGRRDRDPIVLMAEFEVFVDLPSWRKGADMSRNMEVIDETLETAVSEEAYRVED 86
Cdd:TIGR00294   1 DVQTLLPKVPIRLTRVGVTGIKKLVPVEREGKRPIILISTFDVFVDLPSHQKGVHMSRNPEVITSVLEEAEETTAANFEM 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491102488   87 VCGDAAELLLEKHDYTTKAEVRMEAEYVTHESTPASEMATQSTADIIASATATEDGTSEE----IGARVTGMTVCPCSQG 162
Cdd:TIGR00294  81 LCNEIVNQLLKKHRYATLAEVYMNSDFILSKRSPKTGQFTQELAKIMGTASGTRDDDFIFerkmVGAEVVGITACPCAQE 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491102488  163 MSASRARETLKQLNVEDDVIEEFLETNPQAGHSQRGHATLTVQSDGAPEVDLNELIEVARDSMSARIYNLAKRPDEDHMT 242
Cdd:TIGR00294 161 LVKEKSQPFLQEAGFSDETIPKILDIVEFATHNQRGRGRIFTEVPSLPSIVIADLIDIAESSMSAELHEILKRPDEKAVV 240
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 491102488  243 YEAHKDAKFVEDCVRALAEGVVNTFPDLPDDAVVTMKQSNDESIHQHNAHAERVAQLDDLRQEVSE 308
Cdd:TIGR00294 241 ETAHENPRFVEDCVRLMAARLVELFPHLPDDTEVECRQINEESIHRHNAFAEKVATFGELRDEIGS 306
 
Name Accession Description Interval E-value
PRK13675 PRK13675
GTP cyclohydrolase; Provisional
2-308 0e+00

GTP cyclohydrolase; Provisional


Pssm-ID: 184232  Cd Length: 308  Bit Score: 512.94  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491102488   2 SQQLPDVQASSPDVTVGLNRVGVTGVEKLVKLGRRDRDPIVLMAEFEVFVDLPSWRKGADMSRNMEVIDETLETAVSEEA 81
Cdd:PRK13675   1 MMQLPDVQASEPDIKIGLTRVGVTNVKKLVKIKRKGKRPIVLIPTFEVFVDLPSDRKGIHMSRNVEVIDEVLEEAVEEEV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491102488  82 YRVEDVCGDAAELLLEKHDYTTKAEVRMEAEYVTHESTPASEMATQSTADIIASATATEDG-TSEEIGARVTGMTVCPCS 160
Cdd:PRK13675  81 YEIEDLCGDIAKRLLEKHEYATRAEVRMRSEYMMRRETPVSKKKSQEVVDIIAGAIATRDGnVRKEIGAEVVGMTACPCA 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491102488 161 QGMSASRARETLKQLNVEDDVIEEFLETNPQAGHSQRGHATLTVQSDGAPEVDLNELIEVARDSMSARIYNLAKRPDEDH 240
Cdd:PRK13675 161 QEMMKERARKKLAELGVDEETIEKFLDNVPMATHNQRGRGTLTIEVPGDEDVSLEDIIDIIESSMSSPIYELLKRPDENA 240
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 491102488 241 MTYEAHKDAKFVEDCVRALAEGVVNTFPDLPDDAVVTMKQSNDESIHQHNAHAERVAQLDDLRQEVSE 308
Cdd:PRK13675 241 VVYEAHKNPKFVEDCVREMAKKVVEEFPHLPDDAVVTVRQINEESIHRHNAFAERVATMGELRKELNA 308
FolE2 COG1469
GTP cyclohydrolase FolE2 [Coenzyme transport and metabolism]; GTP cyclohydrolase FolE2 is part ...
4-296 6.14e-111

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: 322.48  E-value: 6.14e-111
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491102488   4 QLPDVQASSPDVTVGLNRVGVTGVEKLVKLGRRDRDPIVLMAEFEVFVDLPSWRKGADMSRNMEVIDETLETAVSeeAYR 83
Cdd:COG1469    1 TLPDVQSSPDDRNIPLDRVGIKGVRLPVRIADKDGGPQHTVATFDMYVDLPADQKGTHMSRFVEVLDEHLEEALS--VES 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491102488  84 VEDVCGDAAELLlekhdYTTKAEVRMEAEYVTHESTPASEMATQSTADIIASATATEDG-TSEEIGARVTGMTVCPCSQG 162
Cdd:COG1469   79 LEALLEEMAERL-----YAERAEVEMRFPYFIRKKAPVSGLSGLEDYDVTLEAELDRDGeFRKTLGVEVPVTSLCPCSKE 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491102488 163 MSASRAREtlkqlnveddvieeflETNPQAGHSQRGHATLTVQSDGAPEVDLNELIEVARDSMSARIYNLAKRPDEDHMT 242
Cdd:COG1469  154 ISRQLAQE----------------RGIPYGAHNQRSHATISVELDEDEDVWIEDLIDLAESAASTPVYTLLKRPDEKAVT 217
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....
gi 491102488 243 YEAHKDAKFVEDCVRALAEGVVntfpDLPDDAVVTMKQSNDESIHQHNAHAERV 296
Cdd:COG1469  218 ELAYENPKFVEDAVRDVAAALV----EDPRIADFRVEVENFESIHNHDAYAEIE 267
GCHY-1 pfam02649
Type I GTP cyclohydrolase folE2; This is a family of prokaryotic proteins with type I GTP ...
6-293 1.83e-101

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: 297.87  E-value: 1.83e-101
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491102488    6 PDVQASSPDVTVGLNRVGVTGVEKLVKLGRRDRDPIVLMAEFEVFVDLPSWRKGADMSRNMEVIDETLETAvseEAYRVE 85
Cdd:pfam02649   1 PDVQSEPPDRNIPLDRVGVKGVRKPVRVKDKDGRPQHLVATFDLFVDLPADRKGIHMSRFVEALDEHEEVL---SEESLE 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491102488   86 DVcgdaAELLLEKHDYTTKAEVRMEAEYVTHESTPASEMATQSTADIIASATATEDGTSE-EIGARVTGMTVCPCSQGMS 164
Cdd:pfam02649  78 DI----LEELLERHEYAERAEVEMRFPYFIEKKAPVSGVKGLEDYDVTLEAELDRGGGVRkELGVEVPVTTLCPCSKEIS 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491102488  165 ASRARetlkqlnveddvieefLETNPQAGHSQRGHATLTVQSDGAPEVDLNELIEVARDSMSARIYNLAKRPDEDHMTYE 244
Cdd:pfam02649 154 RQLIQ----------------LDGIPYGAHNQRSHATITVELKDGKFVWIEDLIDIAESSASSPVYTLLKRPDEKAVTER 217
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 491102488  245 AHKDAKFVEDCVRALAEGVvntfpdLPDDAVV--TMKQSNDESIHQHNAHA 293
Cdd:pfam02649 218 AYENPKFVEDVVRDVAARL------NADPRVEafRVEVENFESIHNHNAYA 262
TIGR00294 TIGR00294
GTP cyclohydrolase, MptA/FolE2 family; This family includes type I GTP cyclohydrolases ...
7-308 8.47e-92

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: 275.20  E-value: 8.47e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491102488    7 DVQASSPDVTVGLNRVGVTGVEKLVKLGRRDRDPIVLMAEFEVFVDLPSWRKGADMSRNMEVIDETLETAVSEEAYRVED 86
Cdd:TIGR00294   1 DVQTLLPKVPIRLTRVGVTGIKKLVPVEREGKRPIILISTFDVFVDLPSHQKGVHMSRNPEVITSVLEEAEETTAANFEM 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491102488   87 VCGDAAELLLEKHDYTTKAEVRMEAEYVTHESTPASEMATQSTADIIASATATEDGTSEE----IGARVTGMTVCPCSQG 162
Cdd:TIGR00294  81 LCNEIVNQLLKKHRYATLAEVYMNSDFILSKRSPKTGQFTQELAKIMGTASGTRDDDFIFerkmVGAEVVGITACPCAQE 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491102488  163 MSASRARETLKQLNVEDDVIEEFLETNPQAGHSQRGHATLTVQSDGAPEVDLNELIEVARDSMSARIYNLAKRPDEDHMT 242
Cdd:TIGR00294 161 LVKEKSQPFLQEAGFSDETIPKILDIVEFATHNQRGRGRIFTEVPSLPSIVIADLIDIAESSMSAELHEILKRPDEKAVV 240
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 491102488  243 YEAHKDAKFVEDCVRALAEGVVNTFPDLPDDAVVTMKQSNDESIHQHNAHAERVAQLDDLRQEVSE 308
Cdd:TIGR00294 241 ETAHENPRFVEDCVRLMAARLVELFPHLPDDTEVECRQINEESIHRHNAFAEKVATFGELRDEIGS 306
PRK13674 PRK13674
GTP cyclohydrolase I FolE2;
1-294 3.25e-40

GTP cyclohydrolase I FolE2;


Pssm-ID: 237466  Cd Length: 271  Bit Score: 141.48  E-value: 3.25e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491102488   1 MSQQLPDVQASSPDVTVGLNRVGVTGVEKLVKLGRRDRDPIVLMAEFEVFVDLPSWRKGADMSRNMEVIDETLETAVSEE 80
Cdd:PRK13674   5 MKATMPDVQSTPDTRLIPIDWVGIKNIRLPVRVDTRDGGTQTTVARVDLTVSLPADFKGIHMSRLYELLEEHAEQELSPA 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491102488  81 ayrvedVCGDAAELLLEKHDyTTKAEVRMEAEYVTHESTPASEMATQSTADIIASATATEDGTSEEIGARVTGMTVCPCS 160
Cdd:PRK13674  85 ------SLEQLLRDMLESLE-SRAARIEVSFPYFLRKPAPVSGLSGWKDYPVTLEAELRDGVFRLELKVEVPVSSLCPCS 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491102488 161 qgmsASRARETlkqlnveddvieefletnpqaGHSQRGHATLTVQSDGAPEVDLNELIEVARDSMSARIYNLAKRPDEDH 240
Cdd:PRK13674 158 ----KAISRYT---------------------AHSQRSVATVKVRLAADAQLWIEDLIDLAEAAASTPLQTLLKRPDEKA 212
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 491102488 241 MTYEAHKDAKFVEDCVRALAEgvvntfpDLPDDAVVT---MKQSNDESIHQHNAHAE 294
Cdd:PRK13674 213 VTELAYENPMFVEDAARRVAA-------ALEADPRISafrVEVEHFESIHNHDAVAV 262
 
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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