(data stored in ACNUC6288 zone)

SWISSPROT: CCR4_DEBHA

ID   CCR4_DEBHA              Reviewed;         831 AA.
AC   Q6BMM5;
DT   12-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT   16-DEC-2008, sequence version 2.
DT   08-MAY-2019, entry version 100.
DE   RecName: Full=Glucose-repressible alcohol dehydrogenase transcriptional effector;
DE            EC=3.1.13.4;
DE   AltName: Full=Carbon catabolite repressor protein 4;
DE   AltName: Full=Cytoplasmic deadenylase;
GN   Name=CCR4; OrderedLocusNames=DEHA2F04136g;
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;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 36239 / CBS 767 / JCM 1990 / NBRC 0083 / IGC 2968;
RX   PubMed=15229592; DOI=10.1038/nature02579;
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   Swennen D., Tekaia F., Wesolowski-Louvel M., Westhof E., Wirth B.,
RA   Zeniou-Meyer M., Zivanovic Y., 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: Acts as catalytic component of the CCR4-NOT core
CC       complex, which in the nucleus seems to be a general transcription
CC       factor, and in the cytoplasm the major mRNA deadenylase involved
CC       in mRNA turnover. Ccr4 has 3'-5' RNase activity with a strong
CC       preference for polyadenylated substrates and also low exonuclease
CC       activity towards single-stranded DNA. Discovered because of its
CC       role in the control of ADH2 gene expression. It is required for
CC       the expression of genes involved in non-fermentative growth (By
CC       similarity). {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Exonucleolytic cleavage of poly(A) to 5'-AMP.;
CC         EC=3.1.13.4;
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus
CC       {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the CCR4/nocturin family. {ECO:0000305}.
DR   EMBL; CR382138; CAG88862.2; -; Genomic_DNA.
DR   RefSeq; XP_460546.2; XM_460546.1.
DR   SMR; Q6BMM5; -.
DR   STRING; 4959.XP_460546.2; -.
DR   EnsemblFungi; CAG88862; CAG88862; DEHA2F04136g.
DR   GeneID; 2903197; -.
DR   KEGG; dha:DEHA2F04136g; -.
DR   HOGENOM; HOG000294222; -.
DR   InParanoid; Q6BMM5; -.
DR   KO; K12603; -.
DR   OMA; HFPADHI; -.
DR   OrthoDB; 724242at2759; -.
DR   Proteomes; UP000000599; Chromosome F.
DR   GO; GO:0030015; C:CCR4-NOT core complex; IEA:EnsemblFungi.
DR   GO; GO:0016593; C:Cdc73/Paf1 complex; IEA:EnsemblFungi.
DR   GO; GO:0000932; C:P-body; IEA:EnsemblFungi.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004535; F:poly(A)-specific ribonuclease activity; IEA:UniProtKB-EC.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0000076; P:DNA replication checkpoint; IEA:EnsemblFungi.
DR   GO; GO:0000289; P:nuclear-transcribed mRNA poly(A) tail shortening; IEA:EnsemblFungi.
DR   GO; GO:0032968; P:positive regulation of transcription elongation from RNA polymerase II promoter; IEA:EnsemblFungi.
DR   GO; GO:0048478; P:replication fork protection; IEA:EnsemblFungi.
DR   GO; GO:0006368; P:transcription elongation from RNA polymerase II promoter; IEA:EnsemblFungi.
DR   GO; GO:0007089; P:traversing start control point of mitotic cell cycle; IEA:EnsemblFungi.
DR   Gene3D; 3.60.10.10; -; 1.
DR   Gene3D; 3.80.10.10; -; 1.
DR   InterPro; IPR036691; Endo/exonu/phosph_ase_sf.
DR   InterPro; IPR005135; Endo/exonuclease/phosphatase.
DR   InterPro; IPR001611; Leu-rich_rpt.
DR   InterPro; IPR025875; Leu-rich_rpt_4.
DR   InterPro; IPR003591; Leu-rich_rpt_typical-subtyp.
DR   InterPro; IPR032675; LRR_dom_sf.
DR   Pfam; PF03372; Exo_endo_phos; 1.
DR   Pfam; PF12799; LRR_4; 1.
DR   SMART; SM00369; LRR_TYP; 3.
DR   SUPFAM; SSF56219; SSF56219; 1.
DR   PROSITE; PS51450; LRR; 4.
PE   3: Inferred from homology;
DR   PRODOM; Q6BMM5.
DR   SWISS-2DPAGE; Q6BMM5.
KW   Complete proteome; Cytoplasm; Exonuclease; Hydrolase;
KW   Leucine-rich repeat; Magnesium; Metal-binding; Nuclease; Nucleus;
KW   Reference proteome; Repeat; RNA-binding; Transcription;
KW   Transcription regulation.
FT   CHAIN         1    831       Glucose-repressible alcohol dehydrogenase
FT                                transcriptional effector.
FT                                /FTId=PRO_0000290611.
FT   REPEAT      311    333       LRR 1.
FT   REPEAT      335    356       LRR 2.
FT   REPEAT      358    379       LRR 3.
FT   REPEAT      381    402       LRR 4.
FT   REPEAT      404    426       LRR 5.
FT   COMPBIAS      7    219       Gln-rich.
FT   METAL       563    563       Magnesium. {ECO:0000250}.
SQ   SEQUENCE   831 AA;  96108 MW;  E97A1B330DA94BC3 CRC64;
     MNIPKYQQAQ VQGQQPNLQA QQILLQQLQQ GQSQQSQPSI GGSGSAGQFS QQDIYNDNIA
     QQGLYQNSYQ RPVQAQQPPQ LQNIHQQQQF FPQQFSSQQQ NQPQASSLQQ YQQQQQQQQQ
     QQQQQQQQQQ QQQQQQQQQQ PQIHLPQQYQ QSQGQQVPHQ PPHIQQQQFF NQQAAALQQQ
     QQQQQQQQQQ QQQPAQKLNS INIENPNSIY WQHQQQLCQL SRNANIPHYY ARQYAANSRK
     NKNPYSDVKT VSLIDATRSI VSALNEQENS KSNPGSATNS ALLQNKKLAQ DLDDDHLQEE
     QRMRQKTQGR QLWCQLDLSG QGLVNLSPKL FQYDFLESLY LNNNKLTSVP PIVNKLRSLR
     TLDLSHNRIN EVPSELGMCF NLRYLYLFDN NIKTLPNEFG NLIELLFLGI EGNPIDLKIA
     NLVAEKGTKE LIAYLRDLKP SFSKPPPRQW LLLEDDGEII DPINNPDAYT NDNNNSDTND
     TFTMMSYNTL CQHYATTKMY KYTPSWALEW GFRRAALQEE VLHFKSDLVC MQEVETRTFH
     EFWVPVMQGF GYKGVFFNKT RSKTMSESDS KKVDGCATFY KTDKFELLHK QNFEYNSVCM
     GSDKYKKTKD LFNRFMNKDN IALITYFNHI QTGEKILFVN THLHWDPAFN DVKTLQVGIL
     LEELRTIMKK YHHTNSIDEI KNASMVICGD FNSTKENAVY QLFSTGAVSN HEDLEGRDYG
     KFTDEGFRHS FKLKSAYDHV GELPFTTISP AFTDAIDYIW YSTPTLQVKG LLGKIDEEYS
     SHCIGFPNAH FPSDHIPLVT KFQIKKSGGN KKPDFKPDFK PDFKSGSSRK T
//

If you have problems or comments...

PBIL Back to PBIL home page