CCR4_KLULA
ID CCR4_KLULA Reviewed; 790 AA.
AC Q6CJU4;
DT 12-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 1.
DT 03-AUG-2022, entry version 116.
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=KLLA0F15884g;
OS Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 /
OS NRRL Y-1140 / WM37) (Yeast) (Candida sphaerica).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Kluyveromyces.
OX NCBI_TaxID=284590;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37;
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; CR382126; CAG98503.1; -; Genomic_DNA.
DR RefSeq; XP_455795.1; XM_455795.1.
DR AlphaFoldDB; Q6CJU4; -.
DR SMR; Q6CJU4; -.
DR STRING; 28985.XP_455795.1; -.
DR EnsemblFungi; CAG98503; CAG98503; KLLA0_F15884g.
DR GeneID; 2895850; -.
DR KEGG; kla:KLLA0_F15884g; -.
DR eggNOG; KOG0620; Eukaryota.
DR HOGENOM; CLU_016428_4_1_1; -.
DR InParanoid; Q6CJU4; -.
DR OMA; YHFPSDH; -.
DR Proteomes; UP000000598; 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 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; 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..790
FT /note="CCR4-Not complex 3'-5'-exoribonuclease subunit Ccr4"
FT /id="PRO_0000290613"
FT REPEAT 251..272
FT /note="LRR 1"
FT REPEAT 283..305
FT /note="LRR 2"
FT REPEAT 307..328
FT /note="LRR 3"
FT REPEAT 330..351
FT /note="LRR 4"
FT REPEAT 353..374
FT /note="LRR 5"
FT REPEAT 376..398
FT /note="LRR 6"
FT REGION 156..193
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 505
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:O95551"
SQ SEQUENCE 790 AA; 89628 MW; D42349B56EC7D47E CRC64;
MNYPPPLSGF QKPAGQAVPQ MVGTPQAVTQ QLHQHPPGLM GNQGNQHQPA QLNNVLPMMM
NQVQNVITGG AGGPQQAVGP PNVGTPNAAQ AALVAQQLSN ANNPLCHPHL ADPSLLNSPI
WKLQLQLAAV SRQSLGQSNV YARQNAMKKF LNNQNQLGLS TNGQDGVQSQ QQQGQQQQPS
QSGQQQGQQP LGNDASMSLV EHTKQHLMEM ASSGNEATAS AVNVNSDLNS TGFSTPNTPK
AELHPNTPSL LLQHKKLSQY NIDEDDEIEH RMVAPTNSKH DDQLWHALDL SNLALFNLNE
KLFHYEFLTR LYLNGNSLTS LPSSIKKLRN LRVLDLSHNR LTELPKELGM CYQLKYLYFF
DNMITTIPWE FGNLFNLQFL GLEGNPLDKQ LVKIIAEKSV TGLIFYLRDN APEIPYAKDR
KFIEISADGE PTNEYESLQE NTNHMNNTLL KNSFTLLSYN TLCHHYATPK MYRFTPSWAL
SWDYRREKLK EQLLDFDTDV ICLQEVETLT YEEYWVPLME KYNYSCLFHA KTRAKTMHAK
DSKKVDGCAI FYKKDQFQLV FQDSIDFSSA WRSHKKFHRT EDYLNRAMNK DNVALIAELK
HLNTNENVWV VTTHLHWDPQ FNDVKTFQVG VMLDYLETLI KQHHHVNNNN DIKKIPMVIC
GDFNSQLDSA VVELFNSGHV TANHKDIDQR DFGYMSQKNF SHNLSLRSSY GAIGELPFTN
MTPSFTDVID YIWYSSQSLR VRGLLGKIDE EYASKFIGFP NDKFPSDHIP LVTRFEISRG
NATQTSSRKV
