TRM13_YARLI
ID TRM13_YARLI Reviewed; 464 AA.
AC Q6C4F8;
DT 10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 1.
DT 03-AUG-2022, entry version 82.
DE RecName: Full=tRNA:m(4)X modification enzyme TRM13;
DE EC=2.1.1.225;
DE AltName: Full=tRNA methylase 13;
GN Name=TRM13; OrderedLocusNames=YALI0E27137g;
OS Yarrowia lipolytica (strain CLIB 122 / E 150) (Yeast) (Candida lipolytica).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Dipodascaceae; Yarrowia.
OX NCBI_TaxID=284591;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CLIB 122 / E 150;
RX PubMed=15229592; DOI=10.1038/nature02579;
RA Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA Weissenbach J., Wincker P., Souciet J.-L.;
RT "Genome evolution in yeasts.";
RL Nature 430:35-44(2004).
CC -!- FUNCTION: tRNA methylase which 2'-O-methylates cytidine(4) in tRNA(Pro)
CC and tRNA(Gly)(GCC), and adenosine(4) in tRNA(His).
CC {ECO:0000250|UniProtKB:Q12383}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=cytidine(4) in tRNA(Pro) + S-adenosyl-L-methionine = 2'-O-
CC methylcytidine(4) in tRNA(Pro) + H(+) + S-adenosyl-L-homocysteine;
CC Xref=Rhea:RHEA:32767, Rhea:RHEA-COMP:10397, Rhea:RHEA-COMP:10398,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC ChEBI:CHEBI:74495, ChEBI:CHEBI:82748; EC=2.1.1.225;
CC Evidence={ECO:0000250|UniProtKB:Q12383};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=cytidine(4) in tRNA(Gly)(GCC) + S-adenosyl-L-methionine = 2'-
CC O-methylcytidine(4) in tRNA(Gly)(GCC) + H(+) + S-adenosyl-L-
CC homocysteine; Xref=Rhea:RHEA:43192, Rhea:RHEA-COMP:10399, Rhea:RHEA-
CC COMP:10400, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC ChEBI:CHEBI:74495, ChEBI:CHEBI:82748; EC=2.1.1.225;
CC Evidence={ECO:0000250|UniProtKB:Q12383};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=adenosine(4) in tRNA(His) + S-adenosyl-L-methionine = 2'-O-
CC methyladenosine(4) in tRNA(His) + H(+) + S-adenosyl-L-homocysteine;
CC Xref=Rhea:RHEA:43196, Rhea:RHEA-COMP:10401, Rhea:RHEA-COMP:10402,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC ChEBI:CHEBI:74411, ChEBI:CHEBI:74477; EC=2.1.1.225;
CC Evidence={ECO:0000250|UniProtKB:Q12383};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus, nucleolus
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the methyltransferase TRM13 family.
CC {ECO:0000305}.
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DR EMBL; CR382131; CAG80055.1; -; Genomic_DNA.
DR RefSeq; XP_504454.1; XM_504454.1.
DR AlphaFoldDB; Q6C4F8; -.
DR STRING; 4952.CAG80055; -.
DR PRIDE; Q6C4F8; -.
DR EnsemblFungi; CAG80055; CAG80055; YALI0_E27137g.
DR GeneID; 2912777; -.
DR KEGG; yli:YALI0E27137g; -.
DR VEuPathDB; FungiDB:YALI0_E27137g; -.
DR HOGENOM; CLU_027610_1_0_1; -.
DR InParanoid; Q6C4F8; -.
DR OMA; HRCSWRS; -.
DR Proteomes; UP000001300; Chromosome E.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0106050; F:tRNA 2'-O-methyltransferase activity; IEA:EnsemblFungi.
DR GO; GO:0008175; F:tRNA methyltransferase activity; IBA:GO_Central.
DR GO; GO:0030488; P:tRNA methylation; IBA:GO_Central.
DR GO; GO:0002128; P:tRNA nucleoside ribose methylation; IEA:EnsemblFungi.
DR InterPro; IPR007871; Methyltransferase_TRM13.
DR InterPro; IPR039044; Trm13.
DR InterPro; IPR022776; TRM13/UPF0224_CHHC_Znf_dom.
DR InterPro; IPR021721; Znf_CCCH-type_TRM13.
DR PANTHER; PTHR12998; PTHR12998; 1.
DR Pfam; PF05206; TRM13; 1.
DR Pfam; PF11722; zf-TRM13_CCCH; 1.
DR Pfam; PF05253; zf-U11-48K; 1.
DR PROSITE; PS51800; ZF_CHHC_U11_48K; 1.
PE 3: Inferred from homology;
KW Cytoplasm; Metal-binding; Methyltransferase; Nucleus; Reference proteome;
KW S-adenosyl-L-methionine; Transferase; tRNA processing; Zinc; Zinc-finger.
FT CHAIN 1..464
FT /note="tRNA:m(4)X modification enzyme TRM13"
FT /id="PRO_0000339429"
FT ZN_FING 88..115
FT /note="CHHC U11-48K-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01141"
FT REGION 1..40
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 385..412
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 91
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01141"
FT BINDING 97
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01141"
FT BINDING 107
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01141"
FT BINDING 111
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01141"
SQ SEQUENCE 464 AA; 52624 MW; 2E5AD85BC0661516 CRC64;
MTTETGIPEV VKASSETMSA DGKPEKPNPS MFPKRQKRDT PKEYSYLRCE YKLPHKNHRQ
CHMQRKAEEK FCAQHVLLQK DSYAGRERVV CPVDPGHTVW ADELQQHMYK CNKVKERMQK
EREGWHRDDM NISNPEAKPC VGKKSDITVD YAKWIPVVEA AFKDVEEVPV EILNHEKGLA
KRMTEVQNKK HALQQASLIA HMEKTGLLKS SSRILEFGAG RAELSRYINY AICAERQQDD
KTAANYLFID RAMPRMKMDG KLVKDTKDDF PEQPLPLIKR LKMDIKDLML DGVPVEGPYD
ANLIVSKHLC GCATDLTLQC LLNSAVFTKE ARPAALVIAL CCRQICNVQM FPKAGIEWLQ
ERGFDDDGFA ALTRMTSWVL CGERPKKEPV EGEQTEAADN ETPAPVGHPS GLPAEARKVI
GLKCRRLLDQ GRLHALRKEG LDARLVQYTE MDISPENVCL IVNK
