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P38074

- HMT1_YEAST

UniProt

P38074 - HMT1_YEAST

Protein

HNRNP arginine N-methyltransferase

Gene

HMT1

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 131 (01 Oct 2014)
      Sequence version 1 (01 Oct 1994)
      Previous versions | rss
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    Functioni

    Methylates arginines in a variety of RNA-binding proteins. Methylates NOP3. Can catalyze both the mono- and asymmetric dimethylation.1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei33 – 331S-adenosyl-L-methionineBy similarity
    Binding sitei42 – 421S-adenosyl-L-methionineBy similarity
    Binding sitei66 – 661S-adenosyl-L-methionine; via carbonyl oxygenBy similarity
    Binding sitei88 – 881S-adenosyl-L-methionineBy similarity
    Binding sitei117 – 1171S-adenosyl-L-methionineBy similarity

    GO - Molecular functioni

    1. identical protein binding Source: IntAct
    2. protein-arginine omega-N asymmetric methyltransferase activity Source: SGD
    3. protein-arginine omega-N monomethyltransferase activity Source: SGD
    4. protein binding Source: IntAct

    GO - Biological processi

    1. mRNA export from nucleus Source: SGD
    2. negative regulation of DNA-templated transcription, termination Source: SGD
    3. peptidyl-arginine methylation Source: SGD
    4. peptidyl-arginine methylation, to asymmetrical-dimethyl arginine Source: GOC
    5. peptidyl-arginine omega-N-methylation Source: GOC
    6. positive regulation of transcription elongation from RNA polymerase II promoter Source: SGD

    Keywords - Molecular functioni

    Methyltransferase, Transferase

    Keywords - Ligandi

    S-adenosyl-L-methionine

    Enzyme and pathway databases

    BioCyciYEAST:G3O-29011-MONOMER.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    HNRNP arginine N-methyltransferase (EC:2.1.1.-)
    Alternative name(s):
    Protein ODP1
    Gene namesi
    Name:HMT1
    Synonyms:ODP1, RMT1
    Ordered Locus Names:YBR034C
    ORF Names:YBR0320
    OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
    Taxonomic identifieri559292 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
    ProteomesiUP000002311: Chromosome II

    Organism-specific databases

    CYGDiYBR034c.
    SGDiS000000238. HMT1.

    Subcellular locationi

    GO - Cellular componenti

    1. nucleus Source: SGD

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 348348HNRNP arginine N-methyltransferasePRO_0000212341Add
    BLAST

    Proteomic databases

    MaxQBiP38074.
    PaxDbiP38074.
    PeptideAtlasiP38074.

    Expressioni

    Gene expression databases

    GenevestigatoriP38074.

    Interactioni

    Subunit structurei

    Homodimer. The dimers can then associate to form a ring-shaped homohexamer. Interacts with NOP3/NPL3.1 Publication

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    itself4EBI-8394,EBI-8394
    BRE5P537412EBI-8394,EBI-28528
    DBF2P222044EBI-8394,EBI-5569
    MTR4P470472EBI-8394,EBI-11592
    NAB2P325052EBI-8394,EBI-11770
    NPL3Q015609EBI-8394,EBI-12114
    PPH22P235953EBI-8394,EBI-12752
    SNF2P220823EBI-8394,EBI-17526
    SSD1P242762EBI-8394,EBI-18153
    SUM1P466762EBI-8394,EBI-18547

    Protein-protein interaction databases

    BioGridi32735. 300 interactions.
    DIPiDIP-2608N.
    IntActiP38074. 265 interactions.
    MINTiMINT-423994.
    STRINGi4932.YBR034C.

    Structurei

    Secondary structure

    1
    348
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi30 – 378
    Helixi40 – 5718
    Beta strandi61 – 655
    Helixi71 – 788
    Beta strandi82 – 909
    Helixi92 – 10211
    Turni106 – 1083
    Beta strandi109 – 1146
    Turni116 – 1183
    Beta strandi122 – 1243
    Beta strandi126 – 1316
    Helixi144 – 15411
    Beta strandi155 – 1639
    Beta strandi165 – 1739
    Helixi176 – 18510
    Helixi197 – 2015
    Beta strandi206 – 2083
    Helixi212 – 2143
    Beta strandi220 – 2267
    Turni227 – 2293
    Helixi232 – 2354
    Beta strandi236 – 24510
    Beta strandi250 – 26112
    Beta strandi272 – 2743
    Beta strandi286 – 29611
    Beta strandi302 – 31211
    Beta strandi315 – 32814
    Helixi334 – 3374
    Beta strandi339 – 3479

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1G6QX-ray2.901/2/3/4/5/621-348[»]
    ProteinModelPortaliP38074.
    SMRiP38074. Positions 28-348.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP38074.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini20 – 322303SAM-dependent MTase PRMT-typePROSITE-ProRule annotationAdd
    BLAST

    Sequence similaritiesi

    Belongs to the class I-like SAM-binding methyltransferase superfamily. Protein arginine N-methyltransferase family.PROSITE-ProRule annotation
    Contains 1 SAM-dependent MTase PRMT-type domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiCOG0500.
    GeneTreeiENSGT00550000074406.
    HOGENOMiHOG000198521.
    KOiK11434.
    OMAiDIDFTAC.
    OrthoDBiEOG7WDNBC.

    Family and domain databases

    Gene3Di3.40.50.150. 1 hit.
    InterProiIPR025799. Arg_MeTrfase.
    IPR025714. Methyltranfer_dom.
    IPR029063. SAM-dependent_MTases-like.
    [Graphical view]
    PANTHERiPTHR11006. PTHR11006. 1 hit.
    PfamiPF13847. Methyltransf_31. 1 hit.
    [Graphical view]
    SUPFAMiSSF53335. SSF53335. 1 hit.
    PROSITEiPS51678. SAM_MT_PRMT. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P38074-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSKTAVKDSA TEKTKLSESE QHYFNSYDHY GIHEEMLQDT VRTLSYRNAI    50
    IQNKDLFKDK IVLDVGCGTG ILSMFAAKHG AKHVIGVDMS SIIEMAKELV 100
    ELNGFSDKIT LLRGKLEDVH LPFPKVDIII SEWMGYFLLY ESMMDTVLYA 150
    RDHYLVEGGL IFPDKCSIHL AGLEDSQYKD EKLNYWQDVY GFDYSPFVPL 200
    VLHEPIVDTV ERNNVNTTSD KLIEFDLNTV KISDLAFKSN FKLTAKRQDM 250
    INGIVTWFDI VFPAPKGKRP VEFSTGPHAP YTHWKQTIFY FPDDLDAETG 300
    DTIEGELVCS PNEKNNRDLN IKISYKFESN GIDGNSRSRK NEGSYLMH 348
    Length:348
    Mass (Da):39,786
    Last modified:October 1, 1994 - v1
    Checksum:i383AF61033FB4AC2
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X76078 Genomic DNA. Translation: CAA53689.1.
    Z35903 Genomic DNA. Translation: CAA84976.1.
    X76992 Genomic DNA. Translation: CAA54296.1.
    AY557869 Genomic DNA. Translation: AAS56195.1.
    BK006936 Genomic DNA. Translation: DAA07154.1.
    PIRiS45890.
    RefSeqiNP_009590.1. NM_001178382.1.

    Genome annotation databases

    EnsemblFungiiYBR034C; YBR034C; YBR034C.
    GeneIDi852322.
    KEGGisce:YBR034C.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X76078 Genomic DNA. Translation: CAA53689.1 .
    Z35903 Genomic DNA. Translation: CAA84976.1 .
    X76992 Genomic DNA. Translation: CAA54296.1 .
    AY557869 Genomic DNA. Translation: AAS56195.1 .
    BK006936 Genomic DNA. Translation: DAA07154.1 .
    PIRi S45890.
    RefSeqi NP_009590.1. NM_001178382.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1G6Q X-ray 2.90 1/2/3/4/5/6 21-348 [» ]
    ProteinModelPortali P38074.
    SMRi P38074. Positions 28-348.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 32735. 300 interactions.
    DIPi DIP-2608N.
    IntActi P38074. 265 interactions.
    MINTi MINT-423994.
    STRINGi 4932.YBR034C.

    Proteomic databases

    MaxQBi P38074.
    PaxDbi P38074.
    PeptideAtlasi P38074.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblFungii YBR034C ; YBR034C ; YBR034C .
    GeneIDi 852322.
    KEGGi sce:YBR034C.

    Organism-specific databases

    CYGDi YBR034c.
    SGDi S000000238. HMT1.

    Phylogenomic databases

    eggNOGi COG0500.
    GeneTreei ENSGT00550000074406.
    HOGENOMi HOG000198521.
    KOi K11434.
    OMAi DIDFTAC.
    OrthoDBi EOG7WDNBC.

    Enzyme and pathway databases

    BioCyci YEAST:G3O-29011-MONOMER.

    Miscellaneous databases

    EvolutionaryTracei P38074.
    NextBioi 971020.

    Gene expression databases

    Genevestigatori P38074.

    Family and domain databases

    Gene3Di 3.40.50.150. 1 hit.
    InterProi IPR025799. Arg_MeTrfase.
    IPR025714. Methyltranfer_dom.
    IPR029063. SAM-dependent_MTases-like.
    [Graphical view ]
    PANTHERi PTHR11006. PTHR11006. 1 hit.
    Pfami PF13847. Methyltransf_31. 1 hit.
    [Graphical view ]
    SUPFAMi SSF53335. SSF53335. 1 hit.
    PROSITEi PS51678. SAM_MT_PRMT. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "The complete sequence of a 33 kb fragment on the right arm of chromosome II from Saccharomyces cerevisiae reveals 16 open reading frames, including ten new open reading frames, five previously identified genes and a homologue of the SCO1 gene."
      Smits P.H.M., de Haan M., Maat C., Grivell L.A.
      Yeast 10:S75-S80(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: ATCC 204508 / S288c.
    2. "Complete DNA sequence of yeast chromosome II."
      Feldmann H., Aigle M., Aljinovic G., Andre B., Baclet M.C., Barthe C., Baur A., Becam A.-M., Biteau N., Boles E., Brandt T., Brendel M., Brueckner M., Bussereau F., Christiansen C., Contreras R., Crouzet M., Cziepluch C.
      , Demolis N., Delaveau T., Doignon F., Domdey H., Duesterhus S., Dubois E., Dujon B., El Bakkoury M., Entian K.-D., Feuermann M., Fiers W., Fobo G.M., Fritz C., Gassenhuber J., Glansdorff N., Goffeau A., Grivell L.A., de Haan M., Hein C., Herbert C.J., Hollenberg C.P., Holmstroem K., Jacq C., Jacquet M., Jauniaux J.-C., Jonniaux J.-L., Kallesoee T., Kiesau P., Kirchrath L., Koetter P., Korol S., Liebl S., Logghe M., Lohan A.J.E., Louis E.J., Li Z.Y., Maat M.J., Mallet L., Mannhaupt G., Messenguy F., Miosga T., Molemans F., Mueller S., Nasr F., Obermaier B., Perea J., Pierard A., Piravandi E., Pohl F.M., Pohl T.M., Potier S., Proft M., Purnelle B., Ramezani Rad M., Rieger M., Rose M., Schaaff-Gerstenschlaeger I., Scherens B., Schwarzlose C., Skala J., Slonimski P.P., Smits P.H.M., Souciet J.-L., Steensma H.Y., Stucka R., Urrestarazu L.A., van der Aart Q.J.M., Van Dyck L., Vassarotti A., Vetter I., Vierendeels F., Vissers S., Wagner G., de Wergifosse P., Wolfe K.H., Zagulski M., Zimmermann F.K., Mewes H.-W., Kleine K.
      EMBO J. 13:5795-5809(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 204508 / S288c.
    3. Cited for: GENOME REANNOTATION.
      Strain: ATCC 204508 / S288c.
    4. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: ATCC 204508 / S288c.
    5. "Sterol uptake induced by an impairment of pyridoxal phosphate synthesis in Saccharomyces cerevisiae: cloning and sequencing of the PDX3 gene encoding pyridoxine (pyridoxamine) phosphate oxidase."
      Loubbardi A., Karst F., Guilloton M., Marcireau C.
      J. Bacteriol. 177:1817-1823(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-55.
    6. Henry M.F., Silver P.A.
      Unpublished observations (MAR-1996)
      Cited for: CHARACTERIZATION.
    7. "The predominant protein-arginine methyltransferase from Saccharomyces cerevisiae."
      Gary J.D., Lin W.-J., Yang M.C., Herschmann H.R., Clarke S.
      J. Biol. Chem. 271:12585-12594(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: CHARACTERIZATION.
    8. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
    9. "The structure and oligomerization of the yeast arginine methyltransferase, Hmt1."
      Weiss V.H., McBride A.E., Soriano M.A., Filman D.J., Silver P.A., Hogle J.M.
      Nat. Struct. Biol. 7:1165-1171(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF 24-348, FUNCTION, INTERACTION WITH NOP3/NPL3, SUBUNIT.

    Entry informationi

    Entry nameiHMT1_YEAST
    AccessioniPrimary (citable) accession number: P38074
    Secondary accession number(s): D6VQ34
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1994
    Last sequence update: October 1, 1994
    Last modified: October 1, 2014
    This is version 131 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programFungal Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    Present with 37600 molecules/cell in log phase SD medium.1 Publication

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    2. SIMILARITY comments
      Index of protein domains and families
    3. Yeast
      Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
    4. Yeast chromosome II
      Yeast (Saccharomyces cerevisiae) chromosome II: entries and gene names

    External Data

    Dasty 3