CCR4_ASPCL
ID CCR4_ASPCL Reviewed; 667 AA.
AC A1CIJ6;
DT 12-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 1.
DT 03-AUG-2022, entry version 96.
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; ORFNames=ACLA_051730;
OS Aspergillus clavatus (strain ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 /
OS NRRL 1 / QM 1276 / 107).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Fumigati.
OX NCBI_TaxID=344612;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 / NRRL 1;
RX PubMed=18404212; DOI=10.1371/journal.pgen.1000046;
RA Fedorova N.D., Khaldi N., Joardar V.S., Maiti R., Amedeo P., Anderson M.J.,
RA Crabtree J., Silva J.C., Badger J.H., Albarraq A., Angiuoli S., Bussey H.,
RA Bowyer P., Cotty P.J., Dyer P.S., Egan A., Galens K., Fraser-Liggett C.M.,
RA Haas B.J., Inman J.M., Kent R., Lemieux S., Malavazi I., Orvis J.,
RA Roemer T., Ronning C.M., Sundaram J.P., Sutton G., Turner G., Venter J.C.,
RA White O.R., Whitty B.R., Youngman P., Wolfe K.H., Goldman G.H.,
RA Wortman J.R., Jiang B., Denning D.W., Nierman W.C.;
RT "Genomic islands in the pathogenic filamentous fungus Aspergillus
RT fumigatus.";
RL PLoS Genet. 4:E1000046-E1000046(2008).
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; DS027054; EAW10701.1; -; Genomic_DNA.
DR RefSeq; XP_001272127.1; XM_001272126.1.
DR AlphaFoldDB; A1CIJ6; -.
DR SMR; A1CIJ6; -.
DR STRING; 5057.CADACLAP00004259; -.
DR EnsemblFungi; EAW10701; EAW10701; ACLA_051730.
DR GeneID; 4703673; -.
DR KEGG; act:ACLA_051730; -.
DR VEuPathDB; FungiDB:ACLA_051730; -.
DR eggNOG; KOG0620; Eukaryota.
DR HOGENOM; CLU_016428_4_0_1; -.
DR OMA; YHFPSDH; -.
DR OrthoDB; 724242at2759; -.
DR Proteomes; UP000006701; Unassembled WGS sequence.
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; -; 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; 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..667
FT /note="CCR4-Not complex 3'-5'-exoribonuclease subunit Ccr4"
FT /id="PRO_0000290602"
FT REPEAT 169..190
FT /note="LRR 1"
FT REPEAT 192..213
FT /note="LRR 2"
FT REPEAT 215..236
FT /note="LRR 3"
FT REPEAT 238..259
FT /note="LRR 4"
FT REGION 18..40
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 55..140
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 502..522
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 25..40
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 55..71
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 84..107
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 114..140
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 349
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:O95551"
SQ SEQUENCE 667 AA; 75331 MW; 0BADACC2511E68D1 CRC64;
MNGGQAHQRF GMQIPKFQSQ NHHPHHTQQP HHHTHHNQAS HNINHQHQFS SGALASATPH
FTPSHMQNGA HTNVDEDIDD SMNEHWQQQL QLAAESRQAN SPHYHARSVA QQAKGIQIAP
SQPDTQEQGS DGQNGVGKTK AVSRQGWHAL DFGGQGLRAL STSLFNYVFL EKLYLNHNKL
KSLPPTIGHL RKLSHLDLSG NDLTELPDEI GMLTNLRKLY LFDNNIRTLP YEMGYLYRLD
TLGIEGNPLN DVLKSHIMKE GTKALIKYLK EEMPVHLPPP DRDWVVLDET ASASTEKITV
LSYNTLCDSS ATQSHYGYAP ARVLSWEFRR ELILSELRSH GSDIVCLQEI DQGSYNEYFR
EQLAYNDYKG VYWPRGRAMG MQEEDAKGVD GCATFFKGSK FILLDKQLIN FGQTAVRRPD
AKGQDDIYNR LWQKDHIAVV VFLENRQTGS RFIVVNAHLY WDPAFKDVKL IQTAILMEEI
TKLSETYAKW PACTDKAAFR FSKEEGQTEA PPPEEPAPSV QYSSGDQIPL LMCGDLNSSP
GSAAYNLIAH GRLDEEHPDL EKRLYGNLSK VGMTHPFKLK SAYGSIGELP FTNYTPDFKD
ILDYIWYSSN SLHVSALLGE VDKDYLQKVP GFPNYHFPSD HIALFAEFTV KGKKGKVVEA
DFGPQRN
