CCR4_YARLI
ID CCR4_YARLI Reviewed; 705 AA.
AC Q6CEJ6;
DT 12-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 1.
DT 03-AUG-2022, entry version 115.
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=YALI0B15147g;
OS Yarrowia lipolytica (strain CLIB 122 / E 150) (Yeast) (Candida lipolytica).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Dipodascaceae; Yarrowia.
OX NCBI_TaxID=284591;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CLIB 122 / E 150;
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; CR382128; CAG83167.1; -; Genomic_DNA.
DR RefSeq; XP_500917.1; XM_500917.1.
DR AlphaFoldDB; Q6CEJ6; -.
DR SMR; Q6CEJ6; -.
DR STRING; 4952.CAG83167; -.
DR EnsemblFungi; CAG83167; CAG83167; YALI0_B15147g.
DR GeneID; 2907333; -.
DR KEGG; yli:YALI0B15147g; -.
DR VEuPathDB; FungiDB:YALI0_B15147g; -.
DR HOGENOM; CLU_016428_4_0_1; -.
DR InParanoid; Q6CEJ6; -.
DR OMA; YHFPSDH; -.
DR Proteomes; UP000001300; Chromosome B.
DR GO; GO:0030014; C:CCR4-NOT complex; IBA:GO_Central.
DR GO; GO:0030015; C:CCR4-NOT core complex; IEA:EnsemblFungi.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0000932; C:P-body; IEA:EnsemblFungi.
DR GO; GO:0000175; F:3'-5'-exoribonuclease activity; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004535; F:poly(A)-specific ribonuclease activity; IBA:GO_Central.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0000289; P:nuclear-transcribed mRNA poly(A) tail shortening; IBA:GO_Central.
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; IPR003591; Leu-rich_rpt_typical-subtyp.
DR InterPro; IPR032675; LRR_dom_sf.
DR Pfam; PF03372; Exo_endo_phos; 1.
DR SMART; SM00369; LRR_TYP; 3.
DR SUPFAM; SSF56219; SSF56219; 1.
DR PROSITE; PS51450; LRR; 3.
PE 3: Inferred from homology;
KW Activator; Cytoplasm; Exonuclease; Hydrolase; Leucine-rich repeat;
KW Magnesium; Metal-binding; Nuclease; Nucleus; Reference proteome; Repeat;
KW Repressor; RNA-binding; Transcription; Transcription regulation.
FT CHAIN 1..705
FT /note="CCR4-Not complex 3'-5'-exoribonuclease subunit Ccr4"
FT /id="PRO_0000290619"
FT REPEAT 152..175
FT /note="LRR 1"
FT REPEAT 178..199
FT /note="LRR 2"
FT REPEAT 201..222
FT /note="LRR 3"
FT REPEAT 224..245
FT /note="LRR 4"
FT REPEAT 247..267
FT /note="LRR 5"
FT REGION 15..42
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 75..94
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 117..137
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 679..705
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 27..42
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 117..132
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 392
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:O95551"
SQ SEQUENCE 705 AA; 77553 MW; B7B09B76DEECF183 CRC64;
MNHNTSFQQQ LLQQLHQPGG SNPGGVGATG AGNNSPSYPE ASLMGSKFWQ KQMQLAQLSR
QTGPTSHGYA RAAAINSRQQ HGRDGAQVDA DKDQGPSQLT LVDLAVQTVQ QDLVEQQQAT
AASTPQRGYT NQQKKDQLEE ERQMTLMQQE KHQYWADLDM SGQGLMCLSP PLFRSYEFLL
KLYINHNKLT TLPPAIRSLR QLRVLDVSSN MLTKLPPEIG MLHNLRYLFA FDNYLSTLPH
QVGQLYQLEV IGLEGNPINQ PIKEKLAQGG TKELVAELRE SAPMPAAPKP REWIVLEEAG
GRGGAATAAA ATEGESGSTV ATATAGANAA AAGASASSDT FTVMSYNTLC DKYTTVQMHG
YTPLWALGWK HRSETLLKEV IGYDSDILCF QEVDGASFED FWSPKLHQLG YAGLYHPKTR
ARTMSKEKDA KRVDGCAIFY KTKSFCLIEK LSLDFSSLAL KNNDFKKTAD TYNRVLNKDN
IALIALLEHV TTGQKIIVTN THLHWDPAFN DVKLIQVALL LDEVEKFAER VAKDSNRVSA
RNQDGNNVKY ESGKKLPLVI CGDFNSTTDS GVYSLFSQGT VTNHKDMSGR AYGKFTDEGM
NHGFTLKSAY SNIGELAFTN YTPNFVDVID YVWYSSNALS VRGLLGGIDP DYTSNMVGFP
SVHYPSDHIS LLAEFSFKKQ KGGDGQPKKA LDFGNSGSHS GSRKT
