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Conserved domains on  [gi|21355167|ref|NP_649466|]
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lost [Drosophila melanogaster]

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
RRM_SF super family cl17169
RNA recognition motif (RRM) superfamily; RRM, also known as RBD (RNA binding domain) or RNP ...
 384-455 5.28e-27

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: 103.94  E-value: 5.28e-27
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 21355167 384 CIKLTNLSRDIRVKDLKSELRKRECTPMSISWKGHFGKCFLHFGNrkgvpstQDDMDKVLKSLNDLSLTITT 455
Cdd:cd12270   1 TVYVGNIPRSVRVSDLKSALRERGINPLRITWQGARGKAFLHYSD-------MADADSAVSSLQGLRIGGNT 65
5-FTHF_cyc-lig super family cl00360
5-formyltetrahydrofolate cyclo-ligase family; 5-formyltetrahydrofolate cyclo-ligase or ...
 34-232 8.15e-10

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: 58.47  E-value: 8.15e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355167    34 KRSLRVQT---WKKIQEGKVGIGFNNIFNRIPSFVGADKAAALFAneeefkkaqHIKVNIDRVLHEFKELALLADKSVYL 110
Cdd:pfam01812   1 KQELRKQLlarRRALSEEERAAQSEALHQRLISLPEYQKAKRVAA---------YVSVGGEIDTRELIDLLLEEGKRVLL 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355167   111 PSTRESSaLCLKVDVLADATEEQKKEALRVQDIQKFRSEIGLDSGLKLDIVVIGSVVVSREGYRIGRGNGFADLDIGLLI 190
Cdd:pfam01812  72 PVPRPGS-GHLDMVRFTPYYPEDSLPRGAWGLKEPVEEELRELALGQLDLVLVPGVAFDRQGYRLGRGGGYYDRYLARLQ 150

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 21355167   191 ELGAITPKtiIVTIVHDmQVVDSLPPNlfqKYDTPVDIIATP 232
Cdd:pfam01812 151 GHGAKPYT--VGLAFDE-QLVERLPVE---PHDVPVDEVVTE 186
 
Name Accession Description Interval E-value
RRM_MTHFSD cd12270
RNA recognition motif (RRM) found in vertebrate methenyltetrahydrofolate synthetase ...
 384-455 5.28e-27

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: 103.94  E-value: 5.28e-27
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 21355167 384 CIKLTNLSRDIRVKDLKSELRKRECTPMSISWKGHFGKCFLHFGNrkgvpstQDDMDKVLKSLNDLSLTITT 455
Cdd:cd12270   1 TVYVGNIPRSVRVSDLKSALRERGINPLRITWQGARGKAFLHYSD-------MADADSAVSSLQGLRIGGNT 65
5-FTHF_cyc-lig pfam01812
5-formyltetrahydrofolate cyclo-ligase family; 5-formyltetrahydrofolate cyclo-ligase or ...
 34-232 8.15e-10

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: 58.47  E-value: 8.15e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355167    34 KRSLRVQT---WKKIQEGKVGIGFNNIFNRIPSFVGADKAAALFAneeefkkaqHIKVNIDRVLHEFKELALLADKSVYL 110
Cdd:pfam01812   1 KQELRKQLlarRRALSEEERAAQSEALHQRLISLPEYQKAKRVAA---------YVSVGGEIDTRELIDLLLEEGKRVLL 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355167   111 PSTRESSaLCLKVDVLADATEEQKKEALRVQDIQKFRSEIGLDSGLKLDIVVIGSVVVSREGYRIGRGNGFADLDIGLLI 190
Cdd:pfam01812  72 PVPRPGS-GHLDMVRFTPYYPEDSLPRGAWGLKEPVEEELRELALGQLDLVLVPGVAFDRQGYRLGRGGGYYDRYLARLQ 150

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 21355167   191 ELGAITPKtiIVTIVHDmQVVDSLPPNlfqKYDTPVDIIATP 232
Cdd:pfam01812 151 GHGAKPYT--VGLAFDE-QLVERLPVE---PHDVPVDEVVTE 186
FAU1 COG0212
5-formyltetrahydrofolate cyclo-ligase [Coenzyme transport and metabolism];
170-235 4.13e-09

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


Pssm-ID: 439982 [Multi-domain]  Cd Length: 186  Bit Score: 56.32  E-value: 4.13e-09
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 21355167 170 REGYRIGRGNGFAD-LdigllieLGAITPKTIIVTIVHDMQVVDSLPPnlfQKYDTPVDIIATPTEI 235
Cdd:COG0212 130 RRGYRLGYGGGYYDrT-------LARLRPRPLTIGLAFDCQLVDELPV---EPHDVPLDAIVTEKGV 186
 
Name Accession Description Interval E-value
RRM_MTHFSD cd12270
RNA recognition motif (RRM) found in vertebrate methenyltetrahydrofolate synthetase ...
 384-455 5.28e-27

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: 103.94  E-value: 5.28e-27
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 21355167 384 CIKLTNLSRDIRVKDLKSELRKRECTPMSISWKGHFGKCFLHFGNrkgvpstQDDMDKVLKSLNDLSLTITT 455
Cdd:cd12270   1 TVYVGNIPRSVRVSDLKSALRERGINPLRITWQGARGKAFLHYSD-------MADADSAVSSLQGLRIGGNT 65
5-FTHF_cyc-lig pfam01812
5-formyltetrahydrofolate cyclo-ligase family; 5-formyltetrahydrofolate cyclo-ligase or ...
 34-232 8.15e-10

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: 58.47  E-value: 8.15e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355167    34 KRSLRVQT---WKKIQEGKVGIGFNNIFNRIPSFVGADKAAALFAneeefkkaqHIKVNIDRVLHEFKELALLADKSVYL 110
Cdd:pfam01812   1 KQELRKQLlarRRALSEEERAAQSEALHQRLISLPEYQKAKRVAA---------YVSVGGEIDTRELIDLLLEEGKRVLL 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355167   111 PSTRESSaLCLKVDVLADATEEQKKEALRVQDIQKFRSEIGLDSGLKLDIVVIGSVVVSREGYRIGRGNGFADLDIGLLI 190
Cdd:pfam01812  72 PVPRPGS-GHLDMVRFTPYYPEDSLPRGAWGLKEPVEEELRELALGQLDLVLVPGVAFDRQGYRLGRGGGYYDRYLARLQ 150

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 21355167   191 ELGAITPKtiIVTIVHDmQVVDSLPPNlfqKYDTPVDIIATP 232
Cdd:pfam01812 151 GHGAKPYT--VGLAFDE-QLVERLPVE---PHDVPVDEVVTE 186
FAU1 COG0212
5-formyltetrahydrofolate cyclo-ligase [Coenzyme transport and metabolism];
170-235 4.13e-09

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


Pssm-ID: 439982 [Multi-domain]  Cd Length: 186  Bit Score: 56.32  E-value: 4.13e-09
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 21355167 170 REGYRIGRGNGFAD-LdigllieLGAITPKTIIVTIVHDMQVVDSLPPnlfQKYDTPVDIIATPTEI 235
Cdd:COG0212 130 RRGYRLGYGGGYYDrT-------LARLRPRPLTIGLAFDCQLVDELPV---EPHDVPLDAIVTEKGV 186
 
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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