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TRM13_SCHPO
ID   TRM13_SCHPO             Reviewed;         368 AA.
AC   Q9UTH1;
DT   10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT   13-JUN-2012, sequence version 2.
DT   03-AUG-2022, entry version 115.
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=SPAC1805.03c;
OS   Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC   Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC   Schizosaccharomyces.
OX   NCBI_TaxID=284812;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=972 / ATCC 24843;
RX   PubMed=11859360; DOI=10.1038/nature724;
RA   Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA   Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA   Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA   Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA   Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA   Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA   Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA   Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA   O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA   Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA   Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA   Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA   Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA   Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA   Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA   Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA   Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA   Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA   Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA   Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA   del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA   Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA   Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA   Nurse P.;
RT   "The genome sequence of Schizosaccharomyces pombe.";
RL   Nature 415:871-880(2002).
RN   [2]
RP   REVISION OF GENE MODEL.
RX   PubMed=21511999; DOI=10.1126/science.1203357;
RA   Rhind N., Chen Z., Yassour M., Thompson D.A., Haas B.J., Habib N.,
RA   Wapinski I., Roy S., Lin M.F., Heiman D.I., Young S.K., Furuya K., Guo Y.,
RA   Pidoux A., Chen H.M., Robbertse B., Goldberg J.M., Aoki K., Bayne E.H.,
RA   Berlin A.M., Desjardins C.A., Dobbs E., Dukaj L., Fan L., FitzGerald M.G.,
RA   French C., Gujja S., Hansen K., Keifenheim D., Levin J.Z., Mosher R.A.,
RA   Mueller C.A., Pfiffner J., Priest M., Russ C., Smialowska A., Swoboda P.,
RA   Sykes S.M., Vaughn M., Vengrova S., Yoder R., Zeng Q., Allshire R.,
RA   Baulcombe D., Birren B.W., Brown W., Ekwall K., Kellis M., Leatherwood J.,
RA   Levin H., Margalit H., Martienssen R., Nieduszynski C.A., Spatafora J.W.,
RA   Friedman N., Dalgaard J.Z., Baumann P., Niki H., Regev A., Nusbaum C.;
RT   "Comparative functional genomics of the fission yeasts.";
RL   Science 332:930-936(2011).
RN   [3]
RP   SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX   PubMed=16823372; DOI=10.1038/nbt1222;
RA   Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S.,
RA   Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S.,
RA   Yoshida M.;
RT   "ORFeome cloning and global analysis of protein localization in the fission
RT   yeast Schizosaccharomyces pombe.";
RL   Nat. Biotechnol. 24:841-847(2006).
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:0000269|PubMed:16823372}. Nucleus,
CC       nucleolus {ECO:0000269|PubMed:16823372}.
CC   -!- SIMILARITY: Belongs to the methyltransferase TRM13 family.
CC       {ECO:0000305}.
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DR   EMBL; CU329670; CAB55844.2; -; Genomic_DNA.
DR   PIR; T37888; T37888.
DR   RefSeq; NP_593914.2; NM_001019343.2.
DR   AlphaFoldDB; Q9UTH1; -.
DR   BioGRID; 278862; 42.
DR   STRING; 4896.SPAC1805.03c.1; -.
DR   MaxQB; Q9UTH1; -.
DR   PaxDb; Q9UTH1; -.
DR   PRIDE; Q9UTH1; -.
DR   EnsemblFungi; SPAC1805.03c.1; SPAC1805.03c.1:pep; SPAC1805.03c.
DR   GeneID; 2542398; -.
DR   KEGG; spo:SPAC1805.03c; -.
DR   PomBase; SPAC1805.03c; trm13.
DR   VEuPathDB; FungiDB:SPAC1805.03c; -.
DR   eggNOG; KOG2811; Eukaryota.
DR   HOGENOM; CLU_027610_0_0_1; -.
DR   InParanoid; Q9UTH1; -.
DR   OMA; HRCSWRS; -.
DR   PRO; PR:Q9UTH1; -.
DR   Proteomes; UP000002485; Chromosome I.
DR   GO; GO:0005829; C:cytosol; HDA:PomBase.
DR   GO; GO:0005730; C:nucleolus; HDA:PomBase.
DR   GO; GO:0005634; C:nucleus; HDA:PomBase.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0106050; F:tRNA 2'-O-methyltransferase activity; ISO:PomBase.
DR   GO; GO:0008175; F:tRNA methyltransferase activity; IBA:GO_Central.
DR   GO; GO:0030488; P:tRNA methylation; ISO:PomBase.
DR   InterPro; IPR007871; Methyltransferase_TRM13.
DR   InterPro; IPR039044; Trm13.
DR   InterPro; IPR022776; TRM13/UPF0224_CHHC_Znf_dom.
DR   InterPro; IPR036236; Znf_C2H2_sf.
DR   PANTHER; PTHR12998; PTHR12998; 1.
DR   Pfam; PF05206; TRM13; 1.
DR   Pfam; PF05253; zf-U11-48K; 1.
DR   SUPFAM; SSF57667; SSF57667; 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..368
FT                   /note="tRNA:m(4)X modification enzyme TRM13"
FT                   /id="PRO_0000339427"
FT   ZN_FING         15..42
FT                   /note="CHHC U11-48K-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01141"
FT   BINDING         18
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01141"
FT   BINDING         24
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01141"
FT   BINDING         34
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01141"
FT   BINDING         38
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01141"
SQ   SEQUENCE   368 AA;  42666 MW;  6440DAEE8FA9B4E6 CRC64;
     MARIKKIFTQ EELKQIPCPY DHKHTIVRHR LEYHLKRCNA RPVERTDPYY KKDINISTST
     DASESSSFEI VDLSKEELSK WICLFNRISD SLPTPQKKVL FHPAMNARLE EGTKKKHAIQ
     QASLLGHMEK LHYFDNQGSI YYEFGAGRAE LSRYVQHCSQ QENVYILIDR DSNRTKHDSR
     ILKDSIKNNW PEPKIIRCKI DIKDLKLDFF ASEFRNSGKP VFAYSKHLCG AATDLTLNCL
     KSSPPNALVI ALCCHHHCRW RTLSTFAREQ LSHWGISNPQ EFQILRQMTG WAVNSLREHM
     HASGGADSHI SGLSHEERVK IGLKCKHIIN YMRKLECEKM GYESSLVYYV GEETTLENVA
     LIAYKRIN
 
 
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