(data stored in SCRATCH zone)

SWISSPROT: Q6FJQ8_CANGA

ID   Q6FJQ8_CANGA            Unreviewed;       320 AA.
AC   Q6FJQ8;
DT   19-JUL-2004, integrated into UniProtKB/TrEMBL.
DT   19-JUL-2004, sequence version 1.
DT   30-AUG-2017, entry version 59.
DE   RecName: Full=U6 snRNA phosphodiesterase {ECO:0000256|HAMAP-Rule:MF_03040};
DE            EC=3.1.4.- {ECO:0000256|HAMAP-Rule:MF_03040};
GN   Name=USB1 {ECO:0000256|HAMAP-Rule:MF_03040};
GN   OrderedLocusNames=CAGL0M04345g {ECO:0000313|CGD:CAL0137285,
GN   ECO:0000313|EMBL:CAG62512.1};
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:CAG62512.1, 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: Phosphodiesterase responsible for the U6 snRNA 3' end
CC       processing. Acts as an exoribonuclease (RNase) responsible for
CC       trimming the poly(U) tract of the last nucleotides in the pre-U6
CC       snRNA molecule, leading to the formation of mature U6 snRNA.
CC       {ECO:0000256|HAMAP-Rule:MF_03040}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|HAMAP-Rule:MF_03040}.
CC   -!- SIMILARITY: Belongs to the 2H phosphoesterase superfamily. USB1
CC       family. {ECO:0000256|HAMAP-Rule:MF_03040}.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; CR380959; CAG62512.1; -; Genomic_DNA.
DR   RefSeq; XP_449536.1; XM_449536.1.
DR   STRING; 284593.XP_449536.1; -.
DR   EnsemblFungi; CAG62512; CAG62512; CAGL0M04345g.
DR   KEGG; cgr:CAGL0M04345g; -.
DR   CGD; CAL0137285; CAGL0M04345g.
DR   EuPathDB; FungiDB:CAGL0M04345g; -.
DR   eggNOG; ENOG410J1N5; Eukaryota.
DR   eggNOG; ENOG410ZPI4; LUCA.
DR   InParanoid; Q6FJQ8; -.
DR   OMA; YISERAN; -.
DR   OrthoDB; EOG092C5VMW; -.
DR   Proteomes; UP000002428; Chromosome M.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0004518; F:nuclease activity; IEA:UniProtKB-KW.
DR   GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR   GO; GO:0008380; P:RNA splicing; IEA:UniProtKB-HAMAP.
DR   GO; GO:0034477; P:U6 snRNA 3'-end processing; IEA:UniProtKB-HAMAP.
DR   HAMAP; MF_03040; USB1; 1.
DR   InterPro; IPR027521; Usb1.
DR   PANTHER; PTHR13522; PTHR13522; 1.
DR   Pfam; PF09749; HVSL; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q6FJQ8.
DR   SWISS-2DPAGE; Q6FJQ8.
KW   Complete proteome {ECO:0000313|Proteomes:UP000002428};
KW   Hydrolase {ECO:0000256|HAMAP-Rule:MF_03040};
KW   mRNA processing {ECO:0000256|HAMAP-Rule:MF_03040};
KW   mRNA splicing {ECO:0000256|HAMAP-Rule:MF_03040};
KW   Nuclease {ECO:0000256|HAMAP-Rule:MF_03040};
KW   Nucleus {ECO:0000256|HAMAP-Rule:MF_03040};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002428}.
FT   ACT_SITE    160    160       Proton donor/acceptor.
FT                                {ECO:0000256|HAMAP-Rule:MF_03040}.
FT   ACT_SITE    256    256       Proton donor/acceptor.
FT                                {ECO:0000256|HAMAP-Rule:MF_03040}.
SQ   SEQUENCE   320 AA;  36610 MW;  A6510C088C1E8F12 CRC64;
     MNILAEYSSE SEFESEENLK SQNSEEVIPP IENWEKSGEV SNLEEWQRTH RDDIDTVIKL
     PPIPSSVYDK YQIPPNTDKY IERTDNGMSL GAIKGSDVFK RNIGKWSCFL YIEYRPSSTE
     REMISKTLSQ FNQSWQKKFP GTDIFEPLHY TTLGVPVPLH ISLTKNIPFD SETQRDRFYN
     ILVPKVAQLR QHLVQFEDTL RFYGSPQTTS VFLGYNVAQS VKDNIIKDIT DNIESALIDS
     GLSESDKMVT VPSFSHMSIA KLSNAPKDIL DKVGYADSNQ MAKQIQDYVE ISPNQQPVFY
     VSSIKMNKNR ELLTIPFATP
//

If you have problems or comments...

PBIL Back to PBIL home page