(data stored in SCRATCH zone)

SWISSPROT: Q750C1_ASHGO

ID   Q750C1_ASHGO            Unreviewed;       306 AA.
AC   Q750C1;
DT   05-JUL-2004, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2004, sequence version 1.
DT   11-DEC-2019, entry version 102.
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   ORFNames=AGOS_AGR036W {ECO:0000313|EMBL:AAS54525.1};
OS   Ashbya gossypii (strain ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056)
OS   (Yeast) (Eremothecium gossypii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Eremothecium.
OX   NCBI_TaxID=284811 {ECO:0000313|EMBL:AAS54525.1, ECO:0000313|Proteomes:UP000000591};
RN   [1] {ECO:0000313|EMBL:AAS54525.1, ECO:0000313|Proteomes:UP000000591}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056
RC   {ECO:0000313|Proteomes:UP000000591};
RX   PubMed=15001715; DOI=10.1126/science.1095781;
RA   Dietrich F.S., Voegeli S., Brachat S., Lerch A., Gates K., Steiner S.,
RA   Mohr C., Pohlmann R., Luedi P., Choi S., Wing R.A., Flavier A.,
RA   Gaffney T.D., Philippsen P.;
RT   "The Ashbya gossypii genome as a tool for mapping the ancient Saccharomyces
RT   cerevisiae genome.";
RL   Science 304:304-307(2004).
RN   [2] {ECO:0000313|Proteomes:UP000000591}
RP   GENOME REANNOTATION.
RC   STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056
RC   {ECO:0000313|Proteomes:UP000000591};
RX   PubMed=23749448; DOI=10.1534/g3.112.002881;
RA   Dietrich F.S., Voegeli S., Kuo S., Philippsen P.;
RT   "Genomes of Ashbya fungi isolated from insects reveal four mating-type
RT   loci, numerous translocations, lack of transposons, and distinct gene
RT   duplications.";
RL   G3 (Bethesda) 3:1225-1239(2013).
CC   -!- FUNCTION: Methylates the 2'-O-ribose of nucleotides at positions 32 and
CC       34 of the tRNA anticodon loop of substrate tRNAs. {ECO:0000256|HAMAP-
CC       Rule:MF_03162}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=cytidine(32)/guanosine(34) in tRNA + 2 S-adenosyl-L-methionine
CC         = 2'-O-methylcytidine(32)/2'-O-methylguanosine(34) in tRNA + 2 H(+) +
CC         2 S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:42396, Rhea:RHEA-
CC         COMP:10246, Rhea:RHEA-COMP:10247, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:74269,
CC         ChEBI:CHEBI:74445, ChEBI:CHEBI:74495, ChEBI:CHEBI:82748;
CC         EC=2.1.1.205; 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 methyltransferase
CC       superfamily. RNA methyltransferase RlmE family. TRM7 subfamily.
CC       {ECO:0000256|HAMAP-Rule:MF_03162}.
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DR   EMBL; AE016820; AAS54525.1; -; Genomic_DNA.
DR   RefSeq; NP_986701.1; NM_211763.1.
DR   STRING; 33169.AAS54525; -.
DR   EnsemblFungi; AAS54525; AAS54525; AGOS_AGR036W.
DR   GeneID; 4623001; -.
DR   KEGG; ago:AGOS_AGR036W; -.
DR   HOGENOM; HOG000162368; -.
DR   InParanoid; Q750C1; -.
DR   KO; K14864; -.
DR   OMA; AFIVCLN; -.
DR   Proteomes; UP000000591; Chromosome VII.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0052666; F:tRNA (cytosine-2'-O-)-methyltransferase activity; IEA:EnsemblFungi.
DR   GO; GO:0009020; F:tRNA (guanosine-2'-O-)-methyltransferase activity; IEA:EnsemblFungi.
DR   GO; GO:0008175; F:tRNA methyltransferase activity; IBA:GO_Central.
DR   GO; GO:0002181; P:cytoplasmic translation; IBA:GO_Central.
DR   GO; GO:0030488; P:tRNA methylation; IBA:GO_Central.
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; Q750C1.
DR   SWISS-2DPAGE; Q750C1.
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_03162};
KW   Methyltransferase {ECO:0000256|HAMAP-Rule:MF_03162};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000591};
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
FT                   /note="FtsJ"
FT                   /evidence="ECO:0000259|Pfam:PF01728"
FT   REGION          277..306
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        159
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03162"
FT   BINDING         53
FT                   /note="S-adenosyl-L-methionine; via amide nitrogen"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03162"
FT   BINDING         55
FT                   /note="S-adenosyl-L-methionine; via amide nitrogen"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03162"
FT   BINDING         78
FT                   /note="S-adenosyl-L-methionine"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03162"
FT   BINDING         94
FT                   /note="S-adenosyl-L-methionine"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03162"
FT   BINDING         119
FT                   /note="S-adenosyl-L-methionine"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03162"
SQ   SEQUENCE   306 AA;  34188 MW;  C72643B14199EEE8 CRC64;
     MGKSSKDKRD LYYRKAKEQG FRARSAFKLL QLNDEFHFLD GVQRVVDLCA APGSWSQVLS
     RELFPDGKNT KKRIVAVDLQ PMSRIEHVTT LQADITHPRT LTKIIELFKG EKADFVCSDG
     APDVTGLHDL DEYVQQQLIL SALKLTVSLL APGGCFVAKI FRGRDIDMLY SQLGLLFDKV
     TCAKPRSSRG TSLESFIVCQ GYTPPLSWAP NIEKNVSVEE FFEEFFQNWS IQQPLTPGRP
     LPMYSEGHRG IAPFISCGGL DSFDSDATYH DLPKSATALD PVQSPTNPPY KRALELKRSG
     KLGRSV
//

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