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 03-AUG-2022, entry version 113.
DE RecName: Full=CCR4-Not complex 3'-5'-exoribonuclease subunit Ccr4 {ECO:0000305};
DE EC=3.1.13.4;
DE AltName: Full=Carbon catabolite repressor protein 4;
DE AltName: Full=Cytoplasmic deadenylase;
DE AltName: Full=Glucose-repressible alcohol dehydrogenase transcriptional effector;
GN Name=CCR4; OrderedLocusNames=DEHA2F04136g;
OS Debaryomyces hansenii (strain ATCC 36239 / CBS 767 / BCRC 21394 / JCM 1990
OS / NBRC 0083 / IGC 2968) (Yeast) (Torulaspora hansenii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Debaryomyces.
OX NCBI_TaxID=284592;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 36239 / CBS 767 / BCRC 21394 / JCM 1990 / NBRC 0083 / IGC 2968;
RX PubMed=15229592; DOI=10.1038/nature02579;
RA Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA Weissenbach J., 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 complex,
CC which in the nucleus seems to be a general transcription factor, and in
CC the cytoplasm the major mRNA deadenylase involved in mRNA turnover (By
CC similarity). Ccr4 has 3'-5' RNase activity with a strong preference for
CC polyadenylated substrates and also low exonuclease activity towards
CC single-stranded DNA (By similarity). {ECO:0000250|UniProtKB:P31384}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Exonucleolytic cleavage of poly(A) to 5'-AMP.; 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 {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the CCR4/nocturin family. {ECO:0000305}.
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DR EMBL; CR382138; CAG88862.2; -; Genomic_DNA.
DR RefSeq; XP_460546.2; XM_460546.1.
DR AlphaFoldDB; Q6BMM5; -.
DR SMR; Q6BMM5; -.
DR STRING; 4959.XP_460546.2; -.
DR PRIDE; Q6BMM5; -.
DR EnsemblFungi; CAG88862; CAG88862; DEHA2F04136g.
DR GeneID; 2903197; -.
DR KEGG; dha:DEHA2F04136g; -.
DR VEuPathDB; FungiDB:DEHA2F04136g; -.
DR eggNOG; KOG0620; Eukaryota.
DR HOGENOM; CLU_016428_4_1_1; -.
DR InParanoid; Q6BMM5; -.
DR OMA; LWHAIDF; -.
DR OrthoDB; 724242at2759; -.
DR Proteomes; UP000000599; Chromosome F.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
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 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;
KW Cytoplasm; Exonuclease; Hydrolase; Leucine-rich repeat; Magnesium;
KW Metal-binding; Nuclease; Nucleus; Reference proteome; Repeat; RNA-binding;
KW Transcription; Transcription regulation.
FT CHAIN 1..831
FT /note="CCR4-Not complex 3'-5'-exoribonuclease subunit Ccr4"
FT /id="PRO_0000290611"
FT REPEAT 311..333
FT /note="LRR 1"
FT REPEAT 335..356
FT /note="LRR 2"
FT REPEAT 358..379
FT /note="LRR 3"
FT REPEAT 381..402
FT /note="LRR 4"
FT REPEAT 404..426
FT /note="LRR 5"
FT REGION 29..50
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 142..163
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 806..831
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 807..831
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 533
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:O95551"
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
