(data stored in SCRATCH zone)

SWISSPROT: Q6FJF1_CANGA

ID   Q6FJF1_CANGA            Unreviewed;       415 AA.
AC   Q6FJF1;
DT   19-JUL-2004, integrated into UniProtKB/TrEMBL.
DT   19-JUL-2004, sequence version 1.
DT   30-AUG-2017, entry version 78.
DE   RecName: Full=tRNA wybutosine-synthesizing protein 2 {ECO:0000256|PIRNR:PIRNR038972};
DE            Short=tRNA-yW-synthesizing protein 2 {ECO:0000256|PIRNR:PIRNR038972};
DE   AltName: Full=tRNA(Phe) (4-demethylwyosine(37)-C(7)) aminocarboxypropyltransferase {ECO:0000256|PIRNR:PIRNR038972};
GN   OrderedLocusNames=CAGL0M06809g {ECO:0000313|CGD:CAL0136561,
GN   ECO:0000313|EMBL:CAG62619.1};
OS   Candida glabrata (strain ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 /
OS   NRRL Y-65) (Yeast) (Torulopsis glabrata).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
OC   Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Nakaseomyces;
OC   Nakaseomyces/Candida clade.
OX   NCBI_TaxID=284593 {ECO:0000313|Proteomes:UP000002428};
RN   [1] {ECO:0000313|EMBL:CAG62619.1, ECO:0000313|Proteomes:UP000002428}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL Y-65
RC   {ECO:0000313|Proteomes:UP000002428};
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: S-adenosyl-L-methionine-dependent transferase that acts
CC       as a component of the wybutosine biosynthesis pathway. Wybutosine
CC       is a hyper modified guanosine with a tricyclic base found at the
CC       3'-position adjacent to the anticodon of eukaryotic phenylalanine
CC       tRNA. Catalyzes the transfer of the alpha-amino-alpha-
CC       carboxypropyl (acp) group from S-adenosyl-L-methionine to the C-7
CC       position of 4-demethylwyosine (imG-14) to produce wybutosine-86.
CC       {ECO:0000256|PIRNR:PIRNR038972}.
CC   -!- PATHWAY: tRNA modification; wybutosine-tRNA(Phe) biosynthesis.
CC       {ECO:0000256|PIRNR:PIRNR038972}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|PIRNR:PIRNR038972}.
CC   -!- SIMILARITY: Belongs to the class I-like SAM-binding
CC       methyltransferase superfamily. TRM5/TYW2 family.
CC       {ECO:0000256|PIRNR:PIRNR038972}.
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DR   EMBL; CR380959; CAG62619.1; -; Genomic_DNA.
DR   RefSeq; XP_449643.1; XM_449643.1.
DR   ProteinModelPortal; Q6FJF1; -.
DR   STRING; 284593.XP_449643.1; -.
DR   EnsemblFungi; CAG62619; CAG62619; CAGL0M06809g.
DR   KEGG; cgr:CAGL0M06809g; -.
DR   CGD; CAL0136561; CAGL0M06809g.
DR   EuPathDB; FungiDB:CAGL0M06809g; -.
DR   eggNOG; KOG1227; Eukaryota.
DR   eggNOG; COG2520; LUCA.
DR   HOGENOM; HOG000000750; -.
DR   InParanoid; Q6FJF1; -.
DR   KO; K07055; -.
DR   OMA; RFTIYEP; -.
DR   OrthoDB; EOG092C29GN; -.
DR   UniPathway; UPA00375; -.
DR   Proteomes; UP000002428; Chromosome M.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0008757; F:S-adenosylmethionine-dependent methyltransferase activity; IEA:EnsemblFungi.
DR   GO; GO:0016765; F:transferase activity, transferring alkyl or aryl (other than methyl) groups; IEA:EnsemblFungi.
DR   GO; GO:0030488; P:tRNA methylation; IEA:EnsemblFungi.
DR   GO; GO:0031591; P:wybutosine biosynthetic process; IEA:EnsemblFungi.
DR   InterPro; IPR030382; MeTrfase_TRM5/TYW2.
DR   InterPro; IPR029063; SAM-dependent_MTases.
DR   InterPro; IPR026274; tRNA_wybutosine_synth_prot_2.
DR   Pfam; PF02475; Met_10; 1.
DR   PIRSF; PIRSF038972; Trm12; 1.
DR   SUPFAM; SSF53335; SSF53335; 1.
DR   PROSITE; PS51684; SAM_MT_TRM5_TYW2; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q6FJF1.
DR   SWISS-2DPAGE; Q6FJF1.
KW   Complete proteome {ECO:0000313|Proteomes:UP000002428};
KW   Cytoplasm {ECO:0000256|PIRNR:PIRNR038972};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002428};
KW   S-adenosyl-L-methionine {ECO:0000256|PIRNR:PIRNR038972,
KW   ECO:0000256|SAAS:SAAS00415313};
KW   Transferase {ECO:0000256|PIRNR:PIRNR038972,
KW   ECO:0000256|SAAS:SAAS00415325};
KW   tRNA processing {ECO:0000256|PIRNR:PIRNR038972,
KW   ECO:0000256|SAAS:SAAS00629554}.
FT   DOMAIN      147    415       SAM_MT_TRM5_TYW2. {ECO:0000259|PROSITE:
FT                                PS51684}.
SQ   SEQUENCE   415 AA;  47993 MW;  5B57A3FAE223BB34 CRC64;
     MVLELVVRDL KLLKPIKTIL ENEGLFVKPI YSEGEDKIIR TRISDSNHQL LESLGTGVLI
     REIDGPVIQS HTKNDITEFT RHFFEGKLEN ATVIKLLEVL PVKYTVFPPL LLFNYSKQRS
     FLNELWQQTV PSELMDQFYQ AMLSAPFLAN KKVSHIATNM PIIESDVMRR PFNIVPLYGF
     KNSIPNEDKI WDSPSAQDFQ DALWCQVNQN GIEQVWAPQF TMFSRGNIKE KKRILDTFTD
     IEGNDVVDMY SGIGYFTLSY LTRNARTVFA FELNPWSVEG LKRGLKANRI DQNRCHIFNE
     SNANCLTRIK EYASIHGPPH IRHINLGLLP SSRDGWPLAV QLYRYQLQFS TDRITIHIHE
     NVHIDHIRDN SFIANTVAQL QEIDSELTYT PTHLEQIKTF APDVWHICLD VDIDH
//

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