CCR4_ASHGO
ID CCR4_ASHGO Reviewed; 736 AA.
AC Q75BI3;
DT 12-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 122.
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=ACR288W;
OS Ashbya gossypii (strain ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056)
OS (Yeast) (Eremothecium gossypii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Eremothecium.
OX NCBI_TaxID=284811;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX PubMed=15001715; DOI=10.1126/science.1095781;
RA Dietrich F.S., Voegeli S., Brachat S., Lerch A., Gates K., Steiner S.,
RA Mohr C., Poehlmann R., Luedi P., Choi S., Wing R.A., Flavier A.,
RA Gaffney T.D., Philippsen P.;
RT "The Ashbya gossypii genome as a tool for mapping the ancient Saccharomyces
RT cerevisiae genome.";
RL Science 304:304-307(2004).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX PubMed=23749448; DOI=10.1534/g3.112.002881;
RA Dietrich F.S., Voegeli S., Kuo S., Philippsen P.;
RT "Genomes of Ashbya fungi isolated from insects reveal four mating-type
RT loci, numerous translocations, lack of transposons, and distinct gene
RT duplications.";
RL G3 (Bethesda) 3:1225-1239(2013).
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; AE016816; AAS51514.1; -; Genomic_DNA.
DR RefSeq; NP_983690.1; NM_209043.1.
DR AlphaFoldDB; Q75BI3; -.
DR SMR; Q75BI3; -.
DR STRING; 33169.AAS51514; -.
DR PRIDE; Q75BI3; -.
DR EnsemblFungi; AAS51514; AAS51514; AGOS_ACR288W.
DR GeneID; 4619825; -.
DR KEGG; ago:AGOS_ACR288W; -.
DR eggNOG; KOG0620; Eukaryota.
DR HOGENOM; CLU_016428_4_1_1; -.
DR InParanoid; Q75BI3; -.
DR OMA; YHFPSDH; -.
DR Proteomes; UP000000591; Chromosome III.
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:0016593; C:Cdc73/Paf1 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:0000076; P:DNA replication checkpoint signaling; IEA:EnsemblFungi.
DR GO; GO:0000289; P:nuclear-transcribed mRNA poly(A) tail shortening; IBA:GO_Central.
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 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..736
FT /note="CCR4-Not complex 3'-5'-exoribonuclease subunit Ccr4"
FT /id="PRO_0000290601"
FT REPEAT 251..272
FT /note="LRR 1"
FT REPEAT 274..295
FT /note="LRR 2"
FT REPEAT 297..318
FT /note="LRR 3"
FT REPEAT 320..342
FT /note="LRR 4"
FT REGION 1..52
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 160..182
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 13..52
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 449
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:O95551"
SQ SEQUENCE 736 AA; 83441 MW; 5B6807BA33596907 CRC64;
MNNPPPMMGY QPSGGGSVTQ MLGTPQPLAQ PLHQTGPTQQ AQQMLQQPPG LVSSGTRQML
GQIGQVGSNP LCHPHQSDPT LVNNPIWKLQ LQLAAISRQS VGQANVYARQ NAMKKYLMTQ
TNGSQQPADM AKSLVDFTKQ YLLEMAADPA VPNNAALAAS GQQIQRPHGT PVSTPSTPKA
ELANNAQTTP SILLQQQQKK LSQFNIDEDD EVEHRMMAPV NTKYDEQLWH TIDLSNLSVY
NLNENLFKYD FLTRLYLNGN NLTHLPASIK QLQNLRVLDV SHNRLTELPP ELGMCYQLKY
LYFFDNMVST LPWEFGNLFN LQFLGCEGNP LDRQLIKILT EKSVTGLIFY LRDNAPEIPL
PEPRRFIEVN ADGESVETYR CIEESTNHLN EELLKKSFTL LSYNTLCQHY ATPKMYRFVP
SWALSWDYRR EKLKDEVLAY QTDIICLQEV ESKTYEEFWL PILEKQGYSG IFHAKTRART
MQSKDAKKVD GCCIFYKNSE FTAVFKDAID FSSVWMKHKK FQRTEDYLNR AMNKDNVALI
IKLRHERTGE HVWVVTTHLH WDPHFNDVKT FQVAVMLDYI EKLLKQHGGV GSPQDKKKIP
LVICGDFNSQ LDSAVVELFN TGSVRSHKDI EGRDFGYMSQ KNFAHGLALK SSYGSIGELP
FTNLSPTFTD VIDYIWYSTQ ALRVRGLLGE IDPAYAAKFI GLPNDKIPSD HIPLLARFEF
TKGSSATINT NGNKTV
