CCR4_CANGA
ID CCR4_CANGA Reviewed; 873 AA.
AC Q6FRT2;
DT 12-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2004, sequence version 1.
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=CAGL0H06149g;
OS Candida glabrata (strain ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL
OS Y-65) (Yeast) (Torulopsis glabrata).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Nakaseomyces;
OC Nakaseomyces/Candida clade.
OX NCBI_TaxID=284593;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL Y-65;
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; CR380954; CAG59995.1; -; Genomic_DNA.
DR RefSeq; XP_447062.1; XM_447062.1.
DR AlphaFoldDB; Q6FRT2; -.
DR SMR; Q6FRT2; -.
DR STRING; 5478.XP_447062.1; -.
DR PRIDE; Q6FRT2; -.
DR EnsemblFungi; CAG59995; CAG59995; CAGL0H06149g.
DR GeneID; 2888713; -.
DR KEGG; cgr:CAGL0H06149g; -.
DR CGD; CAL0131866; CAGL0H06149g.
DR VEuPathDB; FungiDB:CAGL0H06149g; -.
DR eggNOG; KOG0620; Eukaryota.
DR HOGENOM; CLU_016428_4_1_1; -.
DR InParanoid; Q6FRT2; -.
DR OMA; LWHAIDF; -.
DR Proteomes; UP000002428; Chromosome H.
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 signaling; 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; -; 2.
DR InterPro; IPR036691; Endo/exonu/phosph_ase_sf.
DR InterPro; IPR005135; Endo/exonuclease/phosphatase.
DR InterPro; IPR001611; Leu-rich_rpt.
DR InterPro; IPR003591; Leu-rich_rpt_typical-subtyp.
DR InterPro; IPR032675; LRR_dom_sf.
DR Pfam; PF03372; Exo_endo_phos; 1.
DR Pfam; PF13855; LRR_8; 1.
DR SMART; SM00369; LRR_TYP; 2.
DR SUPFAM; SSF56219; SSF56219; 1.
DR PROSITE; PS51450; LRR; 3.
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..873
FT /note="CCR4-Not complex 3'-5'-exoribonuclease subunit Ccr4"
FT /id="PRO_0000290608"
FT REPEAT 391..412
FT /note="LRR 1"
FT REPEAT 414..435
FT /note="LRR 2"
FT REPEAT 437..459
FT /note="LRR 3"
FT REPEAT 460..480
FT /note="LRR 4"
FT REGION 1..29
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 292..332
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 9..29
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 298..332
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 589
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:O95551"
SQ SEQUENCE 873 AA; 98578 MW; 796DB965C95E673D CRC64;
MNDISMMGYP GMGQQQPQPQ QAQQPQQQPI SMQPHTMMNM MNTNLPPPGM MMGGAGSNTG
NENMINHGLM SGNPVSGIPN NNSHQLLDQL INKNPNNMGI PQQQQDSLAA QMQLPMGGMP
MGNGSAHNGN VGMNNNNTGG NNNIPMGNAN VLRNNNIIGN LGGSSLAGGN MNSGMPGIST
FGNTPGQLAA PPIQPNANAN NPMYHPHLED PSLMNNPIWK LQLQLATVSA QSVGQPNIYA
RQNAMKKYLA TQVPPQNQTQ QQAQAQSQIA ETSKSLVDCT KQALMDIMAP DDSKLKGMSA
PNTASTTTNS TISTPTTSKI DMNNSREQPS TPSLLLQHKK LSQYSIDEDD EVENRMVAPK
DTKYNDQIWH AIDLSNLQIF NISPNLMKYD FLTRLYLNGN GLESIPSSIR NLKNLRVLDL
SHNKLKELPK EIGNCYQLKY LYFFDNQITT LPWELGNLCN IQFLGCEGNP LDKELLKILT
EKSFTGLIFY LRDNRPEVPY PHDRKFIEIN ADGEPEKEYD TVQEAERNLS SDMQKKSFTM
LSYNTLCQHY ATPKMYRYTP SWALSWDYRR EKLKEQILNF NTDIICLQEV EAKTFEDFWQ
PLLEKHGYTG LFHAKTRAKT MQSKDSKKVD GCCAFYKTSK FKMLFKECVD FSGLWMKHKK
FQRTEDYLNR AMNKDNVAIV MKLQHIQSGE IMWLVTTHLH WDPKFNDVKT FQVGVLLDHM
ETLLKEQNPK QDVKKYPLVI CGDLNSYLSS SVYELFSTGR VQHHHDGKDR DFGYFSEDNF
SHNLALKSSY NCIGELAFTN FTPSFTDVID YIWFSSQALR VRGLLGEVDS EYVSNFIGFP
NDKFPSDHIP LLGRYEFLKS NNTQNSNSGS RKV
