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Conserved domains on  [gi|1039789792|ref|XP_017168242|]
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methenyltetrahydrofolate synthase domain-containing protein isoform X6 [Mus musculus]

Protein Classification

5-formyltetrahydrofolate cyclo-ligase family protein( domain architecture ID 951)

5-formyltetrahydrofolate cyclo-ligase family protein similar to Mus musculus methenyltetrahydrofolate synthase domain-containing protein (MTHFSD), a novel RNA-binding protein abnormally regulated in amyotrophic lateral sclerosis

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
5-FTHF_cyc-lig super family cl00360
5-formyltetrahydrofolate cyclo-ligase family; 5-formyltetrahydrofolate cyclo-ligase or ...
 81-223 2.09e-05

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.


The actual alignment was detected with superfamily member pfam01812:

Pssm-ID: 444864 [Multi-domain]  Cd Length: 186  Bit Score: 43.84  E-value: 2.09e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039789792  81 KQSIRERI---WDYMESHDIADFPRPVHHRIPNFKGSylagQSIRDLEVFagtqeVKVDPDKPLEGVRFLALQSKKTLLV 157
Cdd:pfam01812   1 KQELRKQLlarRRALSEEERAAQSEALHQRLISLPEY----QKAKRVAAY-----VSVGGEIDTRELIDLLLEEGKRVLL 71

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1039789792 158 PTPRLRTGLFN--KITPPPGATKDILRKCATSQGVRNFSVPVGLDSSVLVDLvvvGSVAVSEKGAQAG 223
Cdd:pfam01812  72 PVPRPGSGHLDmvRFTPYYPEDSLPRGAWGLKEPVEEELRELALGQLDLVLV---PGVAFDRQGYRLG 136
 
Name Accession Description Interval E-value
5-FTHF_cyc-lig pfam01812
5-formyltetrahydrofolate cyclo-ligase family; 5-formyltetrahydrofolate cyclo-ligase or ...
 81-223 2.09e-05

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: 43.84  E-value: 2.09e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039789792  81 KQSIRERI---WDYMESHDIADFPRPVHHRIPNFKGSylagQSIRDLEVFagtqeVKVDPDKPLEGVRFLALQSKKTLLV 157
Cdd:pfam01812   1 KQELRKQLlarRRALSEEERAAQSEALHQRLISLPEY----QKAKRVAAY-----VSVGGEIDTRELIDLLLEEGKRVLL 71

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1039789792 158 PTPRLRTGLFN--KITPPPGATKDILRKCATSQGVRNFSVPVGLDSSVLVDLvvvGSVAVSEKGAQAG 223
Cdd:pfam01812  72 PVPRPGSGHLDmvRFTPYYPEDSLPRGAWGLKEPVEEELRELALGQLDLVLV---PGVAFDRQGYRLG 136
 
Name Accession Description Interval E-value
5-FTHF_cyc-lig pfam01812
5-formyltetrahydrofolate cyclo-ligase family; 5-formyltetrahydrofolate cyclo-ligase or ...
 81-223 2.09e-05

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: 43.84  E-value: 2.09e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039789792  81 KQSIRERI---WDYMESHDIADFPRPVHHRIPNFKGSylagQSIRDLEVFagtqeVKVDPDKPLEGVRFLALQSKKTLLV 157
Cdd:pfam01812   1 KQELRKQLlarRRALSEEERAAQSEALHQRLISLPEY----QKAKRVAAY-----VSVGGEIDTRELIDLLLEEGKRVLL 71

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1039789792 158 PTPRLRTGLFN--KITPPPGATKDILRKCATSQGVRNFSVPVGLDSSVLVDLvvvGSVAVSEKGAQAG 223
Cdd:pfam01812  72 PVPRPGSGHLDmvRFTPYYPEDSLPRGAWGLKEPVEEELRELALGQLDLVLV---PGVAFDRQGYRLG 136
 
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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