ID   TRM13_VANPO             Reviewed;         430 AA.
AC   A7TSF4;
DT   10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT   02-OCT-2007, sequence version 1.
DT   03-AUG-2022, entry version 63.
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; ORFNames=Kpol_1076p3;
OS   Vanderwaltozyma polyspora (strain ATCC 22028 / DSM 70294 / BCRC 21397 / CBS
OS   2163 / NBRC 10782 / NRRL Y-8283 / UCD 57-17) (Kluyveromyces polysporus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Vanderwaltozyma.
OX   NCBI_TaxID=436907;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 22028 / DSM 70294 / BCRC 21397 / CBS 2163 / NBRC 10782 / NRRL
RC   Y-8283 / UCD 57-17;
RX   PubMed=17494770; DOI=10.1073/pnas.0608218104;
RA   Scannell D.R., Frank A.C., Conant G.C., Byrne K.P., Woolfit M., Wolfe K.H.;
RT   "Independent sorting-out of thousands of duplicated gene pairs in two yeast
RT   species descended from a whole-genome duplication.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:8397-8402(2007).
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; DS480508; EDO14797.1; -; Genomic_DNA.
DR   RefSeq; XP_001642655.1; XM_001642605.1.
DR   AlphaFoldDB; A7TSF4; -.
DR   STRING; 436907.A7TSF4; -.
DR   EnsemblFungi; EDO14797; EDO14797; Kpol_1076p3.
DR   GeneID; 5542827; -.
DR   KEGG; vpo:Kpol_1076p3; -.
DR   eggNOG; KOG2811; Eukaryota.
DR   HOGENOM; CLU_027610_0_0_1; -.
DR   InParanoid; A7TSF4; -.
DR   OMA; HRCSWRS; -.
DR   OrthoDB; 713196at2759; -.
DR   PhylomeDB; A7TSF4; -.
DR   Proteomes; UP000000267; Unassembled WGS sequence.
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..430
FT                   /note="tRNA:m(4)X modification enzyme TRM13"
FT                   /id="PRO_0000339428"
FT   ZN_FING         46..73
FT                   /note="CHHC U11-48K-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01141"
FT   BINDING         49
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01141"
FT   BINDING         55
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01141"
FT   BINDING         65
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01141"
FT   BINDING         69
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01141"
SQ   SEQUENCE   430 AA;  50213 MW;  D95FADAE36453EB1 CRC64;
     MQPESKKQRL QCEFYMEKKK RRCGMSRNLS SKYCSEHQIL NENTKRIPCP LDPNHTVWES
     DLDSHLKKCN KLKLIHQHDN KPYFLKDCNA ITTEDSNTTV ITKDSLQNWI MKTIPVLKNF
     FKDDEKNYLS NVPLDIRKNH TMEDKRFPQL NENDNIGKKY HAIQQSSLIQ NMIDRNILQF
     KENSLANFIE FGCGRAELSR YVNQVVIKNS EEKIYNPHFI LIDRSTNRMK FDTKMKKDAL
     EFNQNLNPPT ITRIRIDIKD LKIDPLLQKD SKYIAISKHL CGVATDLTLR SLTYNPDDND
     FLQGVCIAMC CRHVCNSNNY VNPDFVKSII GNTNTEEQLP YDQFFHALTK IAAWATSGDR
     PTSSDENNTH FTNLPYTERQ ELGLMARRVI DQGRCDWLQQ KLGESFKVEL IRYVEPSISL
     ENVALLAYRK