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Conserved domains on  [gi|1929648531|ref|XP_037146827|]
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uncharacterized protein HG535_0H04290 [Zygotorulaspora mrakii]

Protein Classification

5-formyltetrahydrofolate cyclo-ligase( domain architecture ID 10000709)

5-formyltetrahydrofolate cyclo-ligase catalyzes the irreversible conversion of 5-formyltetrahydrofolate (5-FTHF) to 5,10-methenyltetrahydrofolate, part of the folate metabolism

CATH:  3.40.50.10420
EC:  6.3.3.2
Gene Ontology:  GO:0005524|GO:0030272
PubMed:  8034591

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
FAU1 COG0212
5-formyltetrahydrofolate cyclo-ligase [Coenzyme transport and metabolism];
1-207 4.78e-39

5-formyltetrahydrofolate cyclo-ligase [Coenzyme transport and metabolism];


:

Pssm-ID: 439982 [Multi-domain]  Cd Length: 186  Bit Score: 132.59  E-value: 4.78e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929648531   1 MTDKRLLRKKIGLILRNVSSQEIERQSRNITNSVI--PLLRTCRSVACYMSMeSGEVATQYLLKHLFDEGKTVYLPRCts 78
Cdd:COG0212     2 AMDKKALRKELLARRRALSPEERAEASAAIAERLLalLEFRRAKTIALYLPI-RGEVDTRPLIEALLARGKRVALPVV-- 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929648531  79 teetghvvlrEPKRNypHLTFHKmqsWQQIQELKPqGKYRLREPAREHPDPLPAQLDVVLVPGVAFSLKnggrlghgggY 158
Cdd:COG0212    79 ----------VPDGR--PLEFRR---WTPGDPLEP-GRFGIPEPVGDAPEVAPEEIDLVLVPLLAFDRRgyrlg-ygggY 141
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1929648531 159 YDDFFRRYKlqhngGKPLLIGLSLNEQIVEGIDLEIHDQKMDCIVTGDG 207
Cdd:COG0212   142 YDRTLARLR-----PRPLTIGLAFDCQLVDELPVEPHDVPLDAIVTEKG 185
 
Name Accession Description Interval E-value
FAU1 COG0212
5-formyltetrahydrofolate cyclo-ligase [Coenzyme transport and metabolism];
1-207 4.78e-39

5-formyltetrahydrofolate cyclo-ligase [Coenzyme transport and metabolism];


Pssm-ID: 439982 [Multi-domain]  Cd Length: 186  Bit Score: 132.59  E-value: 4.78e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929648531   1 MTDKRLLRKKIGLILRNVSSQEIERQSRNITNSVI--PLLRTCRSVACYMSMeSGEVATQYLLKHLFDEGKTVYLPRCts 78
Cdd:COG0212     2 AMDKKALRKELLARRRALSPEERAEASAAIAERLLalLEFRRAKTIALYLPI-RGEVDTRPLIEALLARGKRVALPVV-- 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929648531  79 teetghvvlrEPKRNypHLTFHKmqsWQQIQELKPqGKYRLREPAREHPDPLPAQLDVVLVPGVAFSLKnggrlghgggY 158
Cdd:COG0212    79 ----------VPDGR--PLEFRR---WTPGDPLEP-GRFGIPEPVGDAPEVAPEEIDLVLVPLLAFDRRgyrlg-ygggY 141
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1929648531 159 YDDFFRRYKlqhngGKPLLIGLSLNEQIVEGIDLEIHDQKMDCIVTGDG 207
Cdd:COG0212   142 YDRTLARLR-----PRPLTIGLAFDCQLVDELPVEPHDVPLDAIVTEKG 185
5-FTHF_cyc-lig pfam01812
5-formyltetrahydrofolate cyclo-ligase family; 5-formyltetrahydrofolate cyclo-ligase or ...
4-205 3.71e-30

5-formyltetrahydrofolate cyclo-ligase family; 5-formyltetrahydrofolate cyclo-ligase or methenyl-THF synthetase EC:6.3.3.2 catalyzes the interchange of 5-formyltetrahydrofolate (5-FTHF) to 5-10-methenyltetrahydrofolate, this requires ATP and Mg2+. 5-FTHF is used in chemotherapy where it is clinically known as Leucovorin.


Pssm-ID: 396398 [Multi-domain]  Cd Length: 186  Bit Score: 110.09  E-value: 3.71e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929648531   4 KRLLRKKIGLILRNVSSQEIERQSRNITNSVIPLL--RTCRSVACYMSMeSGEVATQYLLKHLFDEGKTVYLPRCT-STE 80
Cdd:pfam01812   1 KQELRKQLLARRRALSEEERAAQSEALHQRLISLPeyQKAKRVAAYVSV-GGEIDTRELIDLLLEEGKRVLLPVPRpGSG 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929648531  81 ETGHVVLREPKRNYPhltfhkmqswqqiqelKPQGKYRLREPAREHPDPLP-AQLDVVLVPGVAFSlKNGGRLGHGGGYY 159
Cdd:pfam01812  80 HLDMVRFTPYYPEDS----------------LPRGAWGLKEPVEEELRELAlGQLDLVLVPGVAFD-RQGYRLGRGGGYY 142
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1929648531 160 DDFFRRYKLQhnGGKPLLIGLSLNEQIVEGIDLEIHDQKMDCIVTG 205
Cdd:pfam01812 143 DRYLARLQGH--GAKPYTVGLAFDEQLVERLPVEPHDVPVDEVVTE 186
MTHFS_bact TIGR02727
5,10-methenyltetrahydrofolate synthetase; This enzyme, 5,10-methenyltetrahydrofolate ...
4-204 1.85e-26

5,10-methenyltetrahydrofolate synthetase; This enzyme, 5,10-methenyltetrahydrofolate synthetase, is also called 5-formyltetrahydrofolate cycloligase. Function of bacterial proteins in this family was inferred originally from the known activity of eukaryotic homologs. Recently, activity was shown explicitly for the member from Mycoplasma pneumonia. Members of this family from alpha- and gamma-proteobacteria, designated ygfA, are often found in an operon with 6S structural RNA, and show a similar pattern of high expression during stationary phase. The function may be to deplete folate to slow 1-carbon biosynthetic metabolism. [Central intermediary metabolism, One-carbon metabolism]


Pssm-ID: 274270 [Multi-domain]  Cd Length: 179  Bit Score: 100.04  E-value: 1.85e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929648531   4 KRLLRKKIGLILRNVSSQEIERQSRNITNSVI--PLLRTCRSVACYMSMEsGEVATQYLLKHLFDEGKTVYLPRCTSTEE 81
Cdd:TIGR02727   1 KKELRKKLLEARKALSSEERKAASSAIAKRLLalIEWKNAKTIALYLPLR-GEVDTRPLIEQLLKEGKRVALPKVDPDGK 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929648531  82 TGHVVLRepkrnyphltfhkmqsWQQIQELKPqGKYRLREPAREHPDPL-PAQLDVVLVPGVAFSlKNGGRLGHGGGYYD 160
Cdd:TIGR02727  80 EMLFFRI----------------WSPEQLLTK-GPFGILEPVGDLEEPVpPDEIDLIIVPGVAFD-RRGYRLGYGGGYYD 141
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1929648531 161 DFFRRYklqhnggKPLLIGLSLNEQIVEGIDLEIHDQKMDCIVT 204
Cdd:TIGR02727 142 RFLARL-------KGITIGLAFDFQLVDELPREPHDVPVDAIIT 178
PLN02812 PLN02812
5-formyltetrahydrofolate cyclo-ligase
4-209 8.70e-21

5-formyltetrahydrofolate cyclo-ligase


Pssm-ID: 178408  Cd Length: 211  Bit Score: 86.24  E-value: 8.70e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929648531   4 KRLLRKKIGLILRNVSSQEIERQSRNITNSVI--PLLRTCRSVACYMSMES-GEVATQYLLKHLFDEG-KTVYLPRCTst 79
Cdd:PLN02812    7 KKALRKEVRRALKALSPEQRAQEDAAIQSRLLelPWFKSSKRLCAYVSCAKlREVDTSKILSEILQNPdKRLYVPRVE-- 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929648531  80 EETGHVVLREPKRNYPHLTFHKMqSWQQIQELKPQGKyrLREPAREHPDPLpaqlDVVLVPGVAFSLKNGGRLGHgGGYY 159
Cdd:PLN02812   85 DKNSNMRMLHITDMADDLVANSM-NILEPTPVDADGN--PREDVLQAPEPL----DLLLLPGLAFDRSGRRLGRG-GGYY 156
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1929648531 160 DDFFRRY-KLQHNGG--KPLLIGLSLNEQIVEG--IDLEIHDQKMDCIVTGDGDI 209
Cdd:PLN02812  157 DTFLSKYqELAKEKGwkQPLLVALSYSPQILDEgsVPVDETDVLVDALVTPSGVI 211
 
Name Accession Description Interval E-value
FAU1 COG0212
5-formyltetrahydrofolate cyclo-ligase [Coenzyme transport and metabolism];
1-207 4.78e-39

5-formyltetrahydrofolate cyclo-ligase [Coenzyme transport and metabolism];


Pssm-ID: 439982 [Multi-domain]  Cd Length: 186  Bit Score: 132.59  E-value: 4.78e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929648531   1 MTDKRLLRKKIGLILRNVSSQEIERQSRNITNSVI--PLLRTCRSVACYMSMeSGEVATQYLLKHLFDEGKTVYLPRCts 78
Cdd:COG0212     2 AMDKKALRKELLARRRALSPEERAEASAAIAERLLalLEFRRAKTIALYLPI-RGEVDTRPLIEALLARGKRVALPVV-- 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929648531  79 teetghvvlrEPKRNypHLTFHKmqsWQQIQELKPqGKYRLREPAREHPDPLPAQLDVVLVPGVAFSLKnggrlghgggY 158
Cdd:COG0212    79 ----------VPDGR--PLEFRR---WTPGDPLEP-GRFGIPEPVGDAPEVAPEEIDLVLVPLLAFDRRgyrlg-ygggY 141
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1929648531 159 YDDFFRRYKlqhngGKPLLIGLSLNEQIVEGIDLEIHDQKMDCIVTGDG 207
Cdd:COG0212   142 YDRTLARLR-----PRPLTIGLAFDCQLVDELPVEPHDVPLDAIVTEKG 185
5-FTHF_cyc-lig pfam01812
5-formyltetrahydrofolate cyclo-ligase family; 5-formyltetrahydrofolate cyclo-ligase or ...
4-205 3.71e-30

5-formyltetrahydrofolate cyclo-ligase family; 5-formyltetrahydrofolate cyclo-ligase or methenyl-THF synthetase EC:6.3.3.2 catalyzes the interchange of 5-formyltetrahydrofolate (5-FTHF) to 5-10-methenyltetrahydrofolate, this requires ATP and Mg2+. 5-FTHF is used in chemotherapy where it is clinically known as Leucovorin.


Pssm-ID: 396398 [Multi-domain]  Cd Length: 186  Bit Score: 110.09  E-value: 3.71e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929648531   4 KRLLRKKIGLILRNVSSQEIERQSRNITNSVIPLL--RTCRSVACYMSMeSGEVATQYLLKHLFDEGKTVYLPRCT-STE 80
Cdd:pfam01812   1 KQELRKQLLARRRALSEEERAAQSEALHQRLISLPeyQKAKRVAAYVSV-GGEIDTRELIDLLLEEGKRVLLPVPRpGSG 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929648531  81 ETGHVVLREPKRNYPhltfhkmqswqqiqelKPQGKYRLREPAREHPDPLP-AQLDVVLVPGVAFSlKNGGRLGHGGGYY 159
Cdd:pfam01812  80 HLDMVRFTPYYPEDS----------------LPRGAWGLKEPVEEELRELAlGQLDLVLVPGVAFD-RQGYRLGRGGGYY 142
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1929648531 160 DDFFRRYKLQhnGGKPLLIGLSLNEQIVEGIDLEIHDQKMDCIVTG 205
Cdd:pfam01812 143 DRYLARLQGH--GAKPYTVGLAFDEQLVERLPVEPHDVPVDEVVTE 186
MTHFS_bact TIGR02727
5,10-methenyltetrahydrofolate synthetase; This enzyme, 5,10-methenyltetrahydrofolate ...
4-204 1.85e-26

5,10-methenyltetrahydrofolate synthetase; This enzyme, 5,10-methenyltetrahydrofolate synthetase, is also called 5-formyltetrahydrofolate cycloligase. Function of bacterial proteins in this family was inferred originally from the known activity of eukaryotic homologs. Recently, activity was shown explicitly for the member from Mycoplasma pneumonia. Members of this family from alpha- and gamma-proteobacteria, designated ygfA, are often found in an operon with 6S structural RNA, and show a similar pattern of high expression during stationary phase. The function may be to deplete folate to slow 1-carbon biosynthetic metabolism. [Central intermediary metabolism, One-carbon metabolism]


Pssm-ID: 274270 [Multi-domain]  Cd Length: 179  Bit Score: 100.04  E-value: 1.85e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929648531   4 KRLLRKKIGLILRNVSSQEIERQSRNITNSVI--PLLRTCRSVACYMSMEsGEVATQYLLKHLFDEGKTVYLPRCTSTEE 81
Cdd:TIGR02727   1 KKELRKKLLEARKALSSEERKAASSAIAKRLLalIEWKNAKTIALYLPLR-GEVDTRPLIEQLLKEGKRVALPKVDPDGK 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929648531  82 TGHVVLRepkrnyphltfhkmqsWQQIQELKPqGKYRLREPAREHPDPL-PAQLDVVLVPGVAFSlKNGGRLGHGGGYYD 160
Cdd:TIGR02727  80 EMLFFRI----------------WSPEQLLTK-GPFGILEPVGDLEEPVpPDEIDLIIVPGVAFD-RRGYRLGYGGGYYD 141
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1929648531 161 DFFRRYklqhnggKPLLIGLSLNEQIVEGIDLEIHDQKMDCIVT 204
Cdd:TIGR02727 142 RFLARL-------KGITIGLAFDFQLVDELPREPHDVPVDAIIT 178
PLN02812 PLN02812
5-formyltetrahydrofolate cyclo-ligase
4-209 8.70e-21

5-formyltetrahydrofolate cyclo-ligase


Pssm-ID: 178408  Cd Length: 211  Bit Score: 86.24  E-value: 8.70e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929648531   4 KRLLRKKIGLILRNVSSQEIERQSRNITNSVI--PLLRTCRSVACYMSMES-GEVATQYLLKHLFDEG-KTVYLPRCTst 79
Cdd:PLN02812    7 KKALRKEVRRALKALSPEQRAQEDAAIQSRLLelPWFKSSKRLCAYVSCAKlREVDTSKILSEILQNPdKRLYVPRVE-- 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929648531  80 EETGHVVLREPKRNYPHLTFHKMqSWQQIQELKPQGKyrLREPAREHPDPLpaqlDVVLVPGVAFSLKNGGRLGHgGGYY 159
Cdd:PLN02812   85 DKNSNMRMLHITDMADDLVANSM-NILEPTPVDADGN--PREDVLQAPEPL----DLLLLPGLAFDRSGRRLGRG-GGYY 156
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1929648531 160 DDFFRRY-KLQHNGG--KPLLIGLSLNEQIVEG--IDLEIHDQKMDCIVTGDGDI 209
Cdd:PLN02812  157 DTFLSKYqELAKEKGwkQPLLVALSYSPQILDEgsVPVDETDVLVDALVTPSGVI 211
PRK10333 PRK10333
5-formyltetrahydrofolate cyclo-ligase family protein; Provisional
43-204 4.38e-06

5-formyltetrahydrofolate cyclo-ligase family protein; Provisional


Pssm-ID: 182385  Cd Length: 182  Bit Score: 45.31  E-value: 4.38e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929648531  43 SVACYMSMEsGEVATQYLLKHLFDEGKTVYLPrctsteetghVVLREPKRNYPHLTFHKmQSWQQIQELKpqgkyrLREP 122
Cdd:PRK10333   36 TVAVFLSFD-GELDTQPLIEQLWRAGKRVYLP----------VLHPFSAGNLLFLNYHP-QSELVMNRLK------IHEP 97
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929648531 123 AREHPDPLP-AQLDVVLVPGVAFSlKNGGRLGHGGGYYDDFFRRYklQHNGGKPllIGLSLNEQIVEGIDLEIHDQKMDC 201
Cdd:PRK10333   98 KLDVRDVLPlSRLDVLITPLVAFD-EYGQRLGMGGGFYDRTLQNW--QHYKTQP--VGYAHDCQLVEKLPVEEWDIPLPA 172

                  ...
gi 1929648531 202 IVT 204
Cdd:PRK10333  173 VVT 175
IKBKB_SDD pfam18397
IQBAL scaffold dimerization domain; This is the C-terminal scaffold dimerization domain (SDD) ...
64-112 3.39e-03

IQBAL scaffold dimerization domain; This is the C-terminal scaffold dimerization domain (SDD) found in inhibitor of nuclear factor kappa-B kinase subunit beta IKBKB (EC:2.7.11.10). IKK2 also known as IKBKB is one of the core component of IKB kinases (IKK). IKB kinase (IKK) is an enzyme that quickly becomes active in response to diverse stresses on a cell. The SDD consists primarily of two long alpha-helices.


Pssm-ID: 465745  Cd Length: 275  Bit Score: 37.39  E-value: 3.39e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1929648531  64 LFDEGKTVYLPRCTSTEETGHV--VLREPKRNYPHLTFHKM--QSWQQIQELK 112
Cdd:pfam18397   1 LFDKSKTVYEGQFAPRPLPESVnyIVRDPKRQLPYSPLRKVwgQAWHYIRGLK 53
 
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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