(data stored in SCRATCH zone)

SWISSPROT: Q6FJE5_CANGA

ID   Q6FJE5_CANGA            Unreviewed;       492 AA.
AC   Q6FJE5;
DT   19-JUL-2004, integrated into UniProtKB/TrEMBL.
DT   19-JUL-2004, sequence version 1.
DT   30-AUG-2017, entry version 70.
DE   SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:CAG62625.1};
GN   OrderedLocusNames=CAGL0M06941g {ECO:0000313|CGD:CAL0137081,
GN   ECO:0000313|EMBL:CAG62625.1};
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:CAG62625.1, 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   -!- SIMILARITY: Belongs to the class I-like SAM-binding
CC       methyltransferase superfamily. RsmB/NOP family.
CC       {ECO:0000256|PROSITE-ProRule:PRU01023}.
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DR   EMBL; CR380959; CAG62625.1; -; Genomic_DNA.
DR   RefSeq; XP_449649.1; XM_449649.1.
DR   ProteinModelPortal; Q6FJE5; -.
DR   STRING; 284593.XP_449649.1; -.
DR   EnsemblFungi; CAG62625; CAG62625; CAGL0M06941g.
DR   KEGG; cgr:CAGL0M06941g; -.
DR   CGD; CAL0137081; CAGL0M06941g.
DR   EuPathDB; FungiDB:CAGL0M06941g; -.
DR   eggNOG; KOG2360; Eukaryota.
DR   eggNOG; COG0144; LUCA.
DR   HOGENOM; HOG000203203; -.
DR   InParanoid; Q6FJE5; -.
DR   KO; K15264; -.
DR   OMA; LVCETQR; -.
DR   OrthoDB; EOG092C2T4H; -.
DR   Proteomes; UP000002428; Chromosome M.
DR   GO; GO:0005730; C:nucleolus; IEA:EnsemblFungi.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0009383; F:rRNA (cytosine-C5-)-methyltransferase activity; IEA:EnsemblFungi.
DR   GO; GO:0070475; P:rRNA base methylation; IEA:EnsemblFungi.
DR   InterPro; IPR001678; MeTrfase_RsmB/NOP2.
DR   InterPro; IPR023267; RCMT.
DR   InterPro; IPR029063; SAM-dependent_MTases.
DR   Pfam; PF01189; Methyltr_RsmB-F; 1.
DR   PRINTS; PR02008; RCMTFAMILY.
DR   SUPFAM; SSF53335; SSF53335; 1.
DR   PROSITE; PS51686; SAM_MT_RSMB_NOP; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q6FJE5.
DR   SWISS-2DPAGE; Q6FJE5.
KW   Complete proteome {ECO:0000313|Proteomes:UP000002428};
KW   Methyltransferase {ECO:0000256|PROSITE-ProRule:PRU01023};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002428};
KW   RNA-binding {ECO:0000256|PROSITE-ProRule:PRU01023};
KW   S-adenosyl-L-methionine {ECO:0000256|PROSITE-ProRule:PRU01023};
KW   Transferase {ECO:0000256|PROSITE-ProRule:PRU01023}.
FT   DOMAIN      145    492       SAM_MT_RSMB_NOP. {ECO:0000259|PROSITE:
FT                                PS51686}.
FT   ACT_SITE    406    406       Nucleophile. {ECO:0000256|PROSITE-
FT                                ProRule:PRU01023}.
FT   BINDING     282    282       S-adenosyl-L-methionine.
FT                                {ECO:0000256|PROSITE-ProRule:PRU01023}.
FT   BINDING     310    310       S-adenosyl-L-methionine.
FT                                {ECO:0000256|PROSITE-ProRule:PRU01023}.
FT   BINDING     329    329       S-adenosyl-L-methionine.
FT                                {ECO:0000256|PROSITE-ProRule:PRU01023}.
SQ   SEQUENCE   492 AA;  56164 MW;  3D560ECEFB29F824 CRC64;
     MEFYRDSTWV LEYLEGQIEK TGRVSGSLQT IVLRCCKQYR IKTNPKHIYA IVSSCWKYKP
     YLDKIMKKSG LLDAIPRKKG KPAFSKLTLL LLCHDLLLSK AKRIQMGKHP IKNYVLKYKN
     ALNAEFVKLK IKLKITDLSQ VVDKDDAADD MTPVRWIRIN PLRISNHDTD QVLNELKKKF
     PTRVNTWKDI IPGSIYYDEF IPNLYGIHIS DKITSHELYK QGKIIIQDRA SCFPAHILNP
     SADDVVIDAC SAPGNKTTHV AAHIFGDPEN PRNDNVQIYA FEKDPERAQI LQKMIKTAGC
     HKNIDVNVGD FTQIATPSKY SDVTGFILDP SCSGSGIFGR KSVDILNNHG KKSNDEVPDE
     NDAEETTDSK NEQLKERLSK LASFQFQIVR HAMSFPNAKK IVYSTCSIHA EENERVVIDL
     LLDKKVQSWG WRVAKKELVL PTWYRRGFKE EFQEVFTDKT EQECQELADG CVRALPKEDG
     GIGFFAVCFV RD
//

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