ID H0GXR1_SACCK Unreviewed; 518 AA.
AC H0GXR1;
DT 22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT 22-FEB-2012, sequence version 1.
DT 27-MAR-2024, entry version 39.
DE SubName: Full=Trm2p {ECO:0000313|EMBL:EHN01405.1};
GN ORFNames=VIN7_8455 {ECO:0000313|EMBL:EHN01405.1};
OS Saccharomyces cerevisiae x Saccharomyces kudriavzevii (strain VIN7)
OS (Yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=1095631 {ECO:0000313|EMBL:EHN01405.1, ECO:0000313|Proteomes:UP000009009};
RN [1] {ECO:0000313|EMBL:EHN01405.1, ECO:0000313|Proteomes:UP000009009}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VIN7 {ECO:0000313|EMBL:EHN01405.1,
RC ECO:0000313|Proteomes:UP000009009};
RX PubMed=22136070; DOI=10.1111/j.1567-1364.2011.00773.x;
RA Borneman A.R., Desany B.A., Riches D., Affourtit J.P., Forgan A.H.,
RA Pretorius I.S., Egholm M., Chambers P.J.;
RT "The genome sequence of the wine yeast VIN7 reveals an allotriploid hybrid
RT genome with Saccharomyces cerevisiae and Saccharomyces kudriavzevii
RT origins.";
RL FEMS Yeast Res. 12:88-96(2012).
CC -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC superfamily. RNA M5U methyltransferase family. {ECO:0000256|PROSITE-
CC ProRule:PRU01024}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EHN01405.1}.
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DR EMBL; AGVY01000295; EHN01405.1; -; Genomic_DNA.
DR AlphaFoldDB; H0GXR1; -.
DR HOGENOM; CLU_014689_3_1_1; -.
DR PhylomeDB; H0GXR1; -.
DR Proteomes; UP000009009; Unassembled WGS sequence.
DR GO; GO:0030697; F:tRNA (uracil(54)-C5)-methyltransferase activity, S-adenosyl methionine-dependent; IEA:InterPro.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR GO; GO:0009451; P:RNA modification; IEA:UniProt.
DR GO; GO:0008033; P:tRNA processing; IEA:InterPro.
DR CDD; cd02440; AdoMet_MTases; 1.
DR Gene3D; 2.40.50.1070; -; 1.
DR Gene3D; 2.40.50.140; Nucleic acid-binding proteins; 1.
DR Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR InterPro; IPR030390; MeTrfase_TrmA_AS.
DR InterPro; IPR030391; MeTrfase_TrmA_CS.
DR InterPro; IPR012340; NA-bd_OB-fold.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR InterPro; IPR002792; TRAM_dom.
DR InterPro; IPR025795; tRNA_(uracil-5-)_MeTrfase.
DR InterPro; IPR010280; U5_MeTrfase_fam.
DR PANTHER; PTHR11061; RNA M5U METHYLTRANSFERASE; 1.
DR PANTHER; PTHR11061:SF30; TRNA (URACIL(54)-C(5))-METHYLTRANSFERASE; 1.
DR Pfam; PF01938; TRAM; 1.
DR Pfam; PF05958; tRNA_U5-meth_tr; 1.
DR SUPFAM; SSF50249; Nucleic acid-binding proteins; 1.
DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR PROSITE; PS51687; SAM_MT_RNA_M5U; 1.
DR PROSITE; PS51622; SAM_MT_RNA_M5U_2; 1.
DR PROSITE; PS50926; TRAM; 1.
DR PROSITE; PS01230; TRMA_1; 1.
DR PROSITE; PS01231; TRMA_2; 1.
PE 3: Inferred from homology;
KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603, ECO:0000256|PROSITE-
KW ProRule:PRU01024};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691,
KW ECO:0000256|PROSITE-ProRule:PRU01024};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PROSITE-
KW ProRule:PRU01024}.
FT DOMAIN 42..107
FT /note="TRAM"
FT /evidence="ECO:0000259|PROSITE:PS50926"
FT ACT_SITE 470
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10015"
FT ACT_SITE 470
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT BINDING 340
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT BINDING 375
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT BINDING 396
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT BINDING 443
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
SQ SEQUENCE 518 AA; 58594 MW; BAD4C3FE98D19271 CRC64;
MGVLEFEVND LLKSQDLSRE QVLNDVTAIL NDKSRVDGPI VLQYHREVKN VKVLEITSNG
NGLALIDNPV EPGKKQVVII PFGLPGDMVN IKVFKTHPYY VESDLLDVIE KSPMRRDDLI
RDKYFGKFSG SQLEFLTYDD QLKLKRKTIM NAYKFFAPRL VAENLLPQFG TTVASPLQFG
YRTKITPHFD MPRIKEKKLT ERPPLGFGQK GRPQWRKDTL HIGGHASILD IDECVLATEV
LNIGLTNERR KFEEEFKNYK KGATILLREN TIVLDPSKPT PEQLTEEGSR DENGNISYVE
VEDEEHNVKL AKTCVTNSRQ IVTEYVDGYT FNFSAGEFFQ NNNAILPVIT KYVRDNLQNS
TKDGENEPRF LVDAYCGSGL FSICSSKGVD KVIGVEISAD SVSFAEKNAK ANGVENCRFI
VGKAEKLFES IDTASDRTSV ILDPPRKGCD ELFLKQLAAY NPAKIVYISC NVHSQARDVE
YFLKETENGS AYQIESIRGF DFFPQTHHVE SVCIMKRV
//
