TRM13_DEBHA
ID TRM13_DEBHA Reviewed; 457 AA.
AC Q6BP10;
DT 10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT 16-DEC-2008, sequence version 2.
DT 03-AUG-2022, entry version 78.
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=DEHA2E17446g;
OS Debaryomyces hansenii (strain ATCC 36239 / CBS 767 / BCRC 21394 / JCM 1990
OS / NBRC 0083 / IGC 2968) (Yeast) (Torulaspora hansenii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Debaryomyces.
OX NCBI_TaxID=284592;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 36239 / CBS 767 / BCRC 21394 / JCM 1990 / NBRC 0083 / IGC 2968;
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; CR382137; CAG88318.2; -; Genomic_DNA.
DR RefSeq; XP_460060.2; XM_460060.1.
DR AlphaFoldDB; Q6BP10; -.
DR STRING; 4959.XP_460060.2; -.
DR PRIDE; Q6BP10; -.
DR EnsemblFungi; CAG88318; CAG88318; DEHA2E17446g.
DR GeneID; 2902249; -.
DR KEGG; dha:DEHA2E17446g; -.
DR VEuPathDB; FungiDB:DEHA2E17446g; -.
DR eggNOG; KOG2811; Eukaryota.
DR HOGENOM; CLU_027610_1_0_1; -.
DR InParanoid; Q6BP10; -.
DR OMA; HRCSWRS; -.
DR OrthoDB; 713196at2759; -.
DR Proteomes; UP000000599; 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:InterPro.
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..457
FT /note="tRNA:m(4)X modification enzyme TRM13"
FT /id="PRO_0000339422"
FT ZN_FING 75..102
FT /note="CHHC U11-48K-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01141"
FT REGION 1..29
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 78
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01141"
FT BINDING 84
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01141"
FT BINDING 94
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01141"
FT BINDING 98
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01141"
SQ SEQUENCE 457 AA; 52466 MW; 58D9B58C93F4318E CRC64;
MANIDKEVLA SQPDEISKDQ KRRKLNKHEK KERTHLQCEY FIAKKNRRCC MQRKADRKYC
SEHLVDNNEP DKGERVPCPL DNNHSVWSKN LTNHLKKCNA KPKENEEIWY EKDLNTKLGV
DITEDSFKND GNDNDNEDDD LNEKELYEKY IPILRNIKDH FEPLGFSISK HSGLKNRLSE
VSNQKHAIQQ SSLIGNMKKR GLLDINKFYL EFGCGKGELS RFVNLSVLED LQVKDLAGKS
KYGYGFIDRG VNRMKMDSKI VKDAKENTIE VNITTKRSKI DIKDLHVDKF LKDIDPEHVV
VISKHLCGAA TDLTFKSLLN SSLLQGNSDK FGGLLIAMCC RHVCAYDQLL PESRAFLQSK
GFRSLSSFNI LKKIVSWAVC GKRDGTNEES TGEHISGLTF KEREELGLVA RRLIDESRVF
AMNLLVNPLG FHTEMFWYVE KEITLENVCL CIIPDSN
