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Conserved domains on  [gi|1732634125|ref|NP_001359312|]
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methenyltetrahydrofolate synthase domain-containing protein isoform 3 [Mus musculus]

Protein Classification

methenyltetrahydrofolate synthase domain-containing protein( domain architecture ID 110533)

methenyltetrahydrofolate synthase domain-containing protein (MTHFSD) is a novel RNA-binding protein abnormally regulated in amyotrophic lateral sclerosis

Gene Symbol:  mthfsd
Gene Ontology:  GO:0003723
PubMed:  26525917

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 ...
 9-206 2.73e-22

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: 92.76  E-value: 2.73e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732634125   9 KQSIRERI---WDYMESHDIADFPRPVHHRIPNFKGSylagQSIRDLEVFagtqeVKVDPDKPLEGVRFLALQSKKTLLV 85
Cdd:pfam01812   1 KQELRKQLlarRRALSEEERAAQSEALHQRLISLPEY----QKAKRVAAY-----VSVGGEIDTRELIDLLLEEGKRVLL 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732634125  86 PTPRLRTGLFN--KITPPPGATKDILRKCATSQGVRNFSVPVGLDSSVLVDLVVVgsvAVSEKGWRIGKGEGYADLEYAM 163
Cdd:pfam01812  72 PVPRPGSGHLDmvRFTPYYPEDSLPRGAWGLKEPVEEELRELALGQLDLVLVPGV---AFDRQGYRLGRGGGYYDRYLAR 148

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1732634125 164 MVSMGAvhKGTPVVTIVHDCQVVDIPealVEDHDLTVDYILTP 206
Cdd:pfam01812 149 LQGHGA--KPYTVGLAFDEQLVERLP---VEPHDVPVDEVVTE 186
RRM_SF super family cl17169
RNA recognition motif (RRM) superfamily; RRM, also known as RBD (RNA binding domain) or RNP ...
 297-366 4.23e-18

RNA recognition motif (RRM) superfamily; RRM, also known as RBD (RNA binding domain) or RNP (ribonucleoprotein domain), is a highly abundant domain in eukaryotes found in proteins involved in post-transcriptional gene expression processes including mRNA and rRNA processing, RNA export, and RNA stability. This domain is 90 amino acids in length and consists of a four-stranded beta-sheet packed against two alpha-helices. RRM usually interacts with ssRNA, but is also known to interact with ssDNA as well as proteins. RRM binds a variable number of nucleotides, ranging from two to eight. The active site includes three aromatic side-chains located within the conserved RNP1 and RNP2 motifs of the domain. The RRM domain is found in a variety heterogeneous nuclear ribonucleoproteins (hnRNPs), proteins implicated in regulation of alternative splicing, and protein components of small nuclear ribonucleoproteins (snRNPs).


The actual alignment was detected with superfamily member cd12270:

Pssm-ID: 473069 [Multi-domain]  Cd Length: 72  Bit Score: 77.75  E-value: 4.23e-18
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732634125 297 TVCVGNLPFTTRVRELKRVLQELGVVPLRLTWQGPQHRAVLHYTDSAAAQQAASLLQGLRLGANALRVSL 366
Cdd:cd12270     1 TVYVGNIPRSVRVSDLKSALRERGINPLRITWQGARGKAFLHYSDMADADSAVSSLQGLRIGGNTLTVEL 70
 
Name Accession Description Interval E-value
5-FTHF_cyc-lig pfam01812
5-formyltetrahydrofolate cyclo-ligase family; 5-formyltetrahydrofolate cyclo-ligase or ...
 9-206 2.73e-22

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: 92.76  E-value: 2.73e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732634125   9 KQSIRERI---WDYMESHDIADFPRPVHHRIPNFKGSylagQSIRDLEVFagtqeVKVDPDKPLEGVRFLALQSKKTLLV 85
Cdd:pfam01812   1 KQELRKQLlarRRALSEEERAAQSEALHQRLISLPEY----QKAKRVAAY-----VSVGGEIDTRELIDLLLEEGKRVLL 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732634125  86 PTPRLRTGLFN--KITPPPGATKDILRKCATSQGVRNFSVPVGLDSSVLVDLVVVgsvAVSEKGWRIGKGEGYADLEYAM 163
Cdd:pfam01812  72 PVPRPGSGHLDmvRFTPYYPEDSLPRGAWGLKEPVEEELRELALGQLDLVLVPGV---AFDRQGYRLGRGGGYYDRYLAR 148

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1732634125 164 MVSMGAvhKGTPVVTIVHDCQVVDIPealVEDHDLTVDYILTP 206
Cdd:pfam01812 149 LQGHGA--KPYTVGLAFDEQLVERLP---VEPHDVPVDEVVTE 186
RRM_MTHFSD cd12270
RNA recognition motif (RRM) found in vertebrate methenyltetrahydrofolate synthetase ...
 297-366 4.23e-18

RNA recognition motif (RRM) found in vertebrate methenyltetrahydrofolate synthetase domain-containing proteins; This subfamily corresponds to methenyltetrahydrofolate synthetase domain (MTHFSD), a putative RNA-binding protein found in various vertebrate species. It contains an N-terminal 5-formyltetrahydrofolate cyclo-ligase domain and a C-terminal RNA recognition motif (RRM), also termed RBD (RNA binding domain) or RNP (ribonucleoprotein domain). The biological role of MTHFSD remains unclear.


Pssm-ID: 409713 [Multi-domain]  Cd Length: 72  Bit Score: 77.75  E-value: 4.23e-18
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732634125 297 TVCVGNLPFTTRVRELKRVLQELGVVPLRLTWQGPQHRAVLHYTDSAAAQQAASLLQGLRLGANALRVSL 366
Cdd:cd12270     1 TVYVGNIPRSVRVSDLKSALRERGINPLRITWQGARGKAFLHYSDMADADSAVSSLQGLRIGGNTLTVEL 70
FAU1 COG0212
5-formyltetrahydrofolate cyclo-ligase [Coenzyme transport and metabolism];
142-209 1.74e-09

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


Pssm-ID: 439982 [Multi-domain]  Cd Length: 186  Bit Score: 56.70  E-value: 1.74e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1732634125 142 AVSEKGWRIGKGEGYAD--LEyammvsmgAVHKGTPVVTIVHDCQVVD-IPealVEDHDLTVDYILTPTRV 209
Cdd:COG0212   127 AFDRRGYRLGYGGGYYDrtLA--------RLRPRPLTIGLAFDCQLVDeLP---VEPHDVPLDAIVTEKGV 186
MTHFS_bact TIGR02727
5,10-methenyltetrahydrofolate synthetase; This enzyme, 5,10-methenyltetrahydrofolate ...
 142-206 1.87e-05

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: 44.57  E-value: 1.87e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1732634125 142 AVSEKGWRIGKGEGYADLEYAMMVsmgavhkgTPVVTIVHDCQVVD-IPealVEDHDLTVDYILTP 206
Cdd:TIGR02727 125 AFDRRGYRLGYGGGYYDRFLARLK--------GITIGLAFDFQLVDeLP---REPHDVPVDAIITE 179
PLN02812 PLN02812
5-formyltetrahydrofolate cyclo-ligase
 142-210 2.41e-03

5-formyltetrahydrofolate cyclo-ligase


Pssm-ID: 178408  Cd Length: 211  Bit Score: 38.86  E-value: 2.41e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1732634125 142 AVSEKGWRIGKGEGYADLEYAMMVSMgAVHKG---TPVVTIVHDCQVVDIPEALVEDHDLTVDYILTPTRVI 210
Cdd:PLN02812  141 AFDRSGRRLGRGGGYYDTFLSKYQEL-AKEKGwkqPLLVALSYSPQILDEGSVPVDETDVLVDALVTPSGVI 211
 
Name Accession Description Interval E-value
5-FTHF_cyc-lig pfam01812
5-formyltetrahydrofolate cyclo-ligase family; 5-formyltetrahydrofolate cyclo-ligase or ...
 9-206 2.73e-22

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: 92.76  E-value: 2.73e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732634125   9 KQSIRERI---WDYMESHDIADFPRPVHHRIPNFKGSylagQSIRDLEVFagtqeVKVDPDKPLEGVRFLALQSKKTLLV 85
Cdd:pfam01812   1 KQELRKQLlarRRALSEEERAAQSEALHQRLISLPEY----QKAKRVAAY-----VSVGGEIDTRELIDLLLEEGKRVLL 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732634125  86 PTPRLRTGLFN--KITPPPGATKDILRKCATSQGVRNFSVPVGLDSSVLVDLVVVgsvAVSEKGWRIGKGEGYADLEYAM 163
Cdd:pfam01812  72 PVPRPGSGHLDmvRFTPYYPEDSLPRGAWGLKEPVEEELRELALGQLDLVLVPGV---AFDRQGYRLGRGGGYYDRYLAR 148

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1732634125 164 MVSMGAvhKGTPVVTIVHDCQVVDIPealVEDHDLTVDYILTP 206
Cdd:pfam01812 149 LQGHGA--KPYTVGLAFDEQLVERLP---VEPHDVPVDEVVTE 186
RRM_MTHFSD cd12270
RNA recognition motif (RRM) found in vertebrate methenyltetrahydrofolate synthetase ...
 297-366 4.23e-18

RNA recognition motif (RRM) found in vertebrate methenyltetrahydrofolate synthetase domain-containing proteins; This subfamily corresponds to methenyltetrahydrofolate synthetase domain (MTHFSD), a putative RNA-binding protein found in various vertebrate species. It contains an N-terminal 5-formyltetrahydrofolate cyclo-ligase domain and a C-terminal RNA recognition motif (RRM), also termed RBD (RNA binding domain) or RNP (ribonucleoprotein domain). The biological role of MTHFSD remains unclear.


Pssm-ID: 409713 [Multi-domain]  Cd Length: 72  Bit Score: 77.75  E-value: 4.23e-18
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732634125 297 TVCVGNLPFTTRVRELKRVLQELGVVPLRLTWQGPQHRAVLHYTDSAAAQQAASLLQGLRLGANALRVSL 366
Cdd:cd12270     1 TVYVGNIPRSVRVSDLKSALRERGINPLRITWQGARGKAFLHYSDMADADSAVSSLQGLRIGGNTLTVEL 70
FAU1 COG0212
5-formyltetrahydrofolate cyclo-ligase [Coenzyme transport and metabolism];
142-209 1.74e-09

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


Pssm-ID: 439982 [Multi-domain]  Cd Length: 186  Bit Score: 56.70  E-value: 1.74e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1732634125 142 AVSEKGWRIGKGEGYAD--LEyammvsmgAVHKGTPVVTIVHDCQVVD-IPealVEDHDLTVDYILTPTRV 209
Cdd:COG0212   127 AFDRRGYRLGYGGGYYDrtLA--------RLRPRPLTIGLAFDCQLVDeLP---VEPHDVPLDAIVTEKGV 186
MTHFS_bact TIGR02727
5,10-methenyltetrahydrofolate synthetase; This enzyme, 5,10-methenyltetrahydrofolate ...
 142-206 1.87e-05

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: 44.57  E-value: 1.87e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1732634125 142 AVSEKGWRIGKGEGYADLEYAMMVsmgavhkgTPVVTIVHDCQVVD-IPealVEDHDLTVDYILTP 206
Cdd:TIGR02727 125 AFDRRGYRLGYGGGYYDRFLARLK--------GITIGLAFDFQLVDeLP---REPHDVPVDAIITE 179
PLN02812 PLN02812
5-formyltetrahydrofolate cyclo-ligase
 142-210 2.41e-03

5-formyltetrahydrofolate cyclo-ligase


Pssm-ID: 178408  Cd Length: 211  Bit Score: 38.86  E-value: 2.41e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1732634125 142 AVSEKGWRIGKGEGYADLEYAMMVSMgAVHKG---TPVVTIVHDCQVVDIPEALVEDHDLTVDYILTPTRVI 210
Cdd:PLN02812  141 AFDRSGRRLGRGGGYYDTFLSKYQEL-AKEKGwkqPLLVALSYSPQILDEGSVPVDETDVLVDALVTPSGVI 211
 
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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