(data stored in ACNUC6288 zone)

SWISSPROT: Q6BMB4_DEBHA

ID   Q6BMB4_DEBHA            Unreviewed;       301 AA.
AC   Q6BMB4;
DT   16-AUG-2004, integrated into UniProtKB/TrEMBL.
DT   16-AUG-2004, sequence version 1.
DT   08-MAY-2019, entry version 90.
DE   RecName: Full=Putative tRNA (cytidine(32)/guanosine(34)-2'-O)-methyltransferase {ECO:0000256|HAMAP-Rule:MF_03162};
DE            EC=2.1.1.205 {ECO:0000256|HAMAP-Rule:MF_03162};
DE   AltName: Full=2'-O-ribose RNA methyltransferase TRM7 homolog {ECO:0000256|HAMAP-Rule:MF_03162};
GN   Name=TRM7 {ECO:0000256|HAMAP-Rule:MF_03162};
GN   OrderedLocusNames=DEHA2F06842g {ECO:0000313|EMBL:CAG88989.1};
OS   Debaryomyces hansenii (strain ATCC 36239 / CBS 767 / JCM 1990 / NBRC
OS   0083 / IGC 2968) (Yeast) (Torulaspora hansenii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
OC   Saccharomycetes; Saccharomycetales; Debaryomycetaceae; Debaryomyces.
OX   NCBI_TaxID=284592 {ECO:0000313|EMBL:CAG88989.1, ECO:0000313|Proteomes:UP000000599};
RN   [1] {ECO:0000313|EMBL:CAG88989.1, ECO:0000313|Proteomes:UP000000599}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 36239 / CBS 767 / JCM 1990 / NBRC 0083 / IGC 2968
RC   {ECO:0000313|Proteomes:UP000000599};
RX   PubMed=15229592; DOI=10.1038/nature02579;
RG   Genolevures;
RA   Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S.,
RA   Lafontaine I., de Montigny J., Marck C., Neuveglise C., Talla E.,
RA   Goffard N., Frangeul L., Aigle M., Anthouard V., Babour A., Barbe V.,
RA   Barnay S., Blanchin S., Beckerich J.M., Beyne E., Bleykasten C.,
RA   Boisrame A., Boyer J., Cattolico L., Confanioleri F., de Daruvar A.,
RA   Despons L., Fabre E., Fairhead C., Ferry-Dumazet H., Groppi A.,
RA   Hantraye F., Hennequin C., Jauniaux N., Joyet P., Kachouri R.,
RA   Kerrest A., Koszul R., Lemaire M., Lesur I., Ma L., Muller H.,
RA   Nicaud J.M., Nikolski M., Oztas S., Ozier-Kalogeropoulos O.,
RA   Pellenz S., Potier S., Richard G.F., Straub M.L., Suleau A.,
RA   Swennene D., Tekaia F., Wesolowski-Louvel M., Westhof E., Wirth B.,
RA   Zeniou-Meyer M., Zivanovic I., Bolotin-Fukuhara M., Thierry A.,
RA   Bouchier C., Caudron B., Scarpelli C., Gaillardin C., Weissenbach J.,
RA   Wincker P., Souciet J.L.;
RT   "Genome evolution in yeasts.";
RL   Nature 430:35-44(2004).
CC   -!- FUNCTION: Methylates the 2'-O-ribose of nucleotides at positions
CC       32 and 34 of the tRNA anticodon loop of substrate tRNAs.
CC       {ECO:0000256|HAMAP-Rule:MF_03162}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=cytidine(32)/guanosine(34) in tRNA + 2 S-adenosyl-L-
CC         methionine = 2'-O-methylcytidine(32)/2'-O-methylguanosine(34) in
CC         tRNA + 2 H(+) + 2 S-adenosyl-L-homocysteine;
CC         Xref=Rhea:RHEA:42396, Rhea:RHEA-COMP:10246, Rhea:RHEA-
CC         COMP:10247, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856,
CC         ChEBI:CHEBI:59789, ChEBI:CHEBI:74269, ChEBI:CHEBI:74445,
CC         ChEBI:CHEBI:74495, ChEBI:CHEBI:82748; EC=2.1.1.205;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_03162};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_03162}.
CC   -!- SIMILARITY: Belongs to the class I-like SAM-binding
CC       methyltransferase superfamily. RNA methyltransferase RlmE family.
CC       TRM7 subfamily. {ECO:0000256|HAMAP-Rule:MF_03162}.
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DR   EMBL; CR382138; CAG88989.1; -; Genomic_DNA.
DR   RefSeq; XP_460657.1; XM_460657.1.
DR   STRING; 4959.XP_460657.1; -.
DR   EnsemblFungi; CAG88989; CAG88989; DEHA2F06842g.
DR   GeneID; 2904129; -.
DR   KEGG; dha:DEHA2F06842g; -.
DR   HOGENOM; HOG000162368; -.
DR   InParanoid; Q6BMB4; -.
DR   KO; K14864; -.
DR   OMA; YDVDFNQ; -.
DR   OrthoDB; 1362679at2759; -.
DR   Proteomes; UP000000599; Chromosome F.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0008175; F:tRNA methyltransferase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0002181; P:cytoplasmic translation; IEA:UniProtKB-UniRule.
DR   GO; GO:0002128; P:tRNA nucleoside ribose methylation; IEA:UniProtKB-UniRule.
DR   HAMAP; MF_01547; RNA_methyltr_E; 1.
DR   HAMAP; MF_03162; RNA_methyltr_E_TRM7; 1.
DR   InterPro; IPR028590; RNA_methyltr_E_Trm7.
DR   InterPro; IPR015507; rRNA-MeTfrase_E.
DR   InterPro; IPR002877; rRNA_MeTrfase_FtsJ_dom.
DR   InterPro; IPR029063; SAM-dependent_MTases.
DR   PANTHER; PTHR10920:SF12; PTHR10920:SF12; 1.
DR   Pfam; PF01728; FtsJ; 1.
DR   SUPFAM; SSF53335; SSF53335; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q6BMB4.
DR   SWISS-2DPAGE; Q6BMB4.
KW   Complete proteome {ECO:0000313|Proteomes:UP000000599};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_03162};
KW   Methyltransferase {ECO:0000256|HAMAP-Rule:MF_03162};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000599};
KW   S-adenosyl-L-methionine {ECO:0000256|HAMAP-Rule:MF_03162};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_03162};
KW   tRNA processing {ECO:0000256|HAMAP-Rule:MF_03162}.
FT   DOMAIN       21    202       FtsJ. {ECO:0000259|Pfam:PF01728}.
FT   ACT_SITE    159    159       Proton acceptor. {ECO:0000256|HAMAP-Rule:
FT                                MF_03162}.
FT   BINDING      53     53       S-adenosyl-L-methionine; via amide
FT                                nitrogen. {ECO:0000256|HAMAP-Rule:
FT                                MF_03162}.
FT   BINDING      55     55       S-adenosyl-L-methionine; via amide
FT                                nitrogen. {ECO:0000256|HAMAP-Rule:
FT                                MF_03162}.
FT   BINDING      78     78       S-adenosyl-L-methionine.
FT                                {ECO:0000256|HAMAP-Rule:MF_03162}.
FT   BINDING      94     94       S-adenosyl-L-methionine.
FT                                {ECO:0000256|HAMAP-Rule:MF_03162}.
FT   BINDING     119    119       S-adenosyl-L-methionine.
FT                                {ECO:0000256|HAMAP-Rule:MF_03162}.
SQ   SEQUENCE   301 AA;  33865 MW;  7F2FA77F70C5E3E4 CRC64;
     MGKSSKDKRD LYYRRAKEEG WRARSAFKLL QLNEQFQLFK GVKRVVDLCA APGSWSQVLS
     RELFENQKQA DAKIVSVDLQ PMTPIEGVTT LQADITHPKT LQKILEIFGG EPADFVCSDG
     APDVTGLHDL DEYIQAQLIL SALQLTTCIL KPGGAFVAKI FRGRDIDLLY SQLSYLFERV
     ICAKPRSSRG TSLEAFIVCL GYKPREGWNP ILDLTKSTEE FFEGANIGRS DNLEHLDLPE
     DEERLIAKFV ACGDLNDVDS DATYTLDTNF KKLALDPVQM PTAPPYKKAL EMKRRGDLVR
     R
//

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