ID I2H3W1_TETBL Unreviewed; 607 AA.
AC I2H3W1;
DT 11-JUL-2012, integrated into UniProtKB/TrEMBL.
DT 11-JUL-2012, sequence version 1.
DT 27-MAR-2024, entry version 48.
DE RecName: Full=TRAM domain-containing protein {ECO:0000259|PROSITE:PS50926};
GN Name=TBLA0D05720 {ECO:0000313|EMBL:CCH61063.1};
GN ORFNames=TBLA_0D05720 {ECO:0000313|EMBL:CCH61063.1};
OS Tetrapisispora blattae (strain ATCC 34711 / CBS 6284 / DSM 70876 / NBRC
OS 10599 / NRRL Y-10934 / UCD 77-7) (Yeast) (Kluyveromyces blattae).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Tetrapisispora.
OX NCBI_TaxID=1071380 {ECO:0000313|EMBL:CCH61063.1, ECO:0000313|Proteomes:UP000002866};
RN [1] {ECO:0000313|EMBL:CCH61063.1, ECO:0000313|Proteomes:UP000002866}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 34711 / CBS 6284 / DSM 70876 / NBRC 10599 / NRRL Y-10934 /
RC UCD 77-7 {ECO:0000313|Proteomes:UP000002866};
RX PubMed=22123960; DOI=10.1073/pnas.1112808108;
RA Gordon J.L., Armisen D., Proux-Wera E., OhEigeartaigh S.S., Byrne K.P.,
RA Wolfe K.H.;
RT "Evolutionary erosion of yeast sex chromosomes by mating-type switching
RT accidents.";
RL Proc. Natl. Acad. Sci. U.S.A. 108:20024-20029(2011).
CC -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC superfamily. RNA M5U methyltransferase family. {ECO:0000256|PROSITE-
CC ProRule:PRU01024}.
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DR EMBL; HE806319; CCH61063.1; -; Genomic_DNA.
DR RefSeq; XP_004180582.1; XM_004180534.1.
DR AlphaFoldDB; I2H3W1; -.
DR STRING; 1071380.I2H3W1; -.
DR GeneID; 14496099; -.
DR KEGG; tbl:TBLA_0D05720; -.
DR eggNOG; KOG2187; Eukaryota.
DR HOGENOM; CLU_014689_3_1_1; -.
DR InParanoid; I2H3W1; -.
DR OMA; GGCKWQH; -.
DR OrthoDB; 52228at2759; -.
DR Proteomes; UP000002866; Chromosome 4.
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; 2.40.50.140; Nucleic acid-binding proteins; 1.
DR Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 2.
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}; Reference proteome {ECO:0000313|Proteomes:UP000002866};
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 129..194
FT /note="TRAM"
FT /evidence="ECO:0000259|PROSITE:PS50926"
FT REGION 290..310
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 559
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10015"
FT ACT_SITE 559
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT BINDING 433
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT BINDING 464
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT BINDING 485
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT BINDING 532
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
SQ SEQUENCE 607 AA; 68966 MW; 253D13C7DDB0768B CRC64;
MLTFSHGLTR FINHNIVYRP SISRLLKLKF KRQIFVLSKM SVTNKNAEIA KRPLPTETNP
VVETPITKKA KKIKTKKYKA KKVDPTSPLG VFQFEIAELL KEQGIKEADT INDITAILND
ASSDGQVKEA YHRKVNDVKV LKLTSSGDGL AIIDNPVESD KKQVVIIPFG LPGDIVHIRV
FKTHPNYVES DLLDVNAKSD IRRDDLINCK YFGKCSGSQY QNLTYETQLK LKQDTVSNAY
KFFAPRLIEK KILPEVGTTI GSPLQYEYRT KLTPHFDIPR RIKKAGELKE RPPLGFGQKG
RPTWRKETLH EGGNASTLDI EEYTIGTSII NKGLKNERRK FEKEFNTYKK GATILLRENT
IVMDKDSTEE QIKERLKNEE GSRDKDGNIS YEVHMSNDGD KKLIKTCVTQ PRQIVNEYVN
GYSFQFSAGE FFQNNNSILP IVTKYVRDNL QLPEGEHNYL VDAYCGSGLF SICSSEGVDK
VVGVEISADS VKFARINSEL NKIANCKFIV GKAEKLFEEI DLPNDRTSVI LDPPRKGCDE
LFLKQLSEFN PAKIVYISCN VHSQARDLEY FLLNTLNGKN YKIESLRGFD FFPQTHHVES
VCVLSRV
//
