CCR4_COCIM
ID CCR4_COCIM Reviewed; 758 AA.
AC Q1EA11; J3KHF3;
DT 12-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT 09-JAN-2013, sequence version 2.
DT 03-AUG-2022, entry version 102.
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=CIMG_00602;
OS Coccidioides immitis (strain RS) (Valley fever fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Onygenaceae; Coccidioides.
OX NCBI_TaxID=246410;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RS;
RX PubMed=19717792; DOI=10.1101/gr.087551.108;
RA Sharpton T.J., Stajich J.E., Rounsley S.D., Gardner M.J., Wortman J.R.,
RA Jordar V.S., Maiti R., Kodira C.D., Neafsey D.E., Zeng Q., Hung C.-Y.,
RA McMahan C., Muszewska A., Grynberg M., Mandel M.A., Kellner E.M.,
RA Barker B.M., Galgiani J.N., Orbach M.J., Kirkland T.N., Cole G.T.,
RA Henn M.R., Birren B.W., Taylor J.W.;
RT "Comparative genomic analyses of the human fungal pathogens Coccidioides
RT and their relatives.";
RL Genome Res. 19:1722-1731(2009).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=RS;
RX PubMed=20516208; DOI=10.1101/gr.103911.109;
RA Neafsey D.E., Barker B.M., Sharpton T.J., Stajich J.E., Park D.J.,
RA Whiston E., Hung C.-Y., McMahan C., White J., Sykes S., Heiman D.,
RA Young S., Zeng Q., Abouelleil A., Aftuck L., Bessette D., Brown A.,
RA FitzGerald M., Lui A., Macdonald J.P., Priest M., Orbach M.J.,
RA Galgiani J.N., Kirkland T.N., Cole G.T., Birren B.W., Henn M.R.,
RA Taylor J.W., Rounsley S.D.;
RT "Population genomic sequencing of Coccidioides fungi reveals recent
RT hybridization and transposon control.";
RL Genome Res. 20:938-946(2010).
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; GG704911; EAS35248.2; -; Genomic_DNA.
DR RefSeq; XP_001246831.2; XM_001246830.2.
DR AlphaFoldDB; Q1EA11; -.
DR SMR; Q1EA11; -.
DR STRING; 246410.Q1EA11; -.
DR EnsemblFungi; EAS35248; EAS35248; CIMG_00602.
DR GeneID; 4565344; -.
DR KEGG; cim:CIMG_00602; -.
DR VEuPathDB; FungiDB:CIMG_00602; -.
DR InParanoid; Q1EA11; -.
DR OMA; YHFPSDH; -.
DR OrthoDB; 724242at2759; -.
DR Proteomes; UP000001261; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
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 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 Pfam; PF13855; LRR_8; 1.
DR SMART; SM00369; LRR_TYP; 3.
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..758
FT /note="CCR4-Not complex 3'-5'-exoribonuclease subunit Ccr4"
FT /id="PRO_0000290609"
FT REPEAT 224..247
FT /note="LRR 1"
FT REPEAT 248..270
FT /note="LRR 2"
FT REPEAT 271..294
FT /note="LRR 3"
FT REPEAT 296..319
FT /note="LRR 4"
FT REGION 22..123
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 146..179
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 196..217
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 584..606
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 33..87
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 164..178
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 434
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:O95551"
SQ SEQUENCE 758 AA; 85806 MW; 2DCD9A7144017E8B CRC64;
MADGTYRFQQ PGAGQFYFQT QQHNHHPAHQ RHLIRNGTSS PTGRLKFNNT DTPSPSRSPP
LNQSPSHNSY TMYSQGHQGQ PVMMNGQSHQ RFGMPMPKFQ HPTHHPHHAQ QPHHPHSQST
QNLAHQHNFS GGALSNAAQH FTPAHLQNGT TSNVEDEIEE PMNEHWQQQL QLAAESRQAS
SPHYYARAVA QQTKGLQLSS NQADPNENGT EERNRATAVK DHRRQDWVAL DFGGQGLRAL
SNGLFHYSFL DKLYLNHNKL KSLPSSIGEL KNLTHLDISS NELTEIPEEI GMLTNLKKLL
LFDNSLQTLP FELGYLYQLD TLGIEGNPLA DVLKSRIMQE GTKSLIKYLK EEMPVHLPPS
NRDWLILDET GKNSANGGND NKFTALTYNT LCDRYATNQQ YGYAPSRALA WEFRRDLLLN
EIRGHDADIV CLQEIDQGSY HGFFREQLAY NDYKGVYWPK GRAQGMPEEE AKLVDGCATF
FKGSKYILLE KNMIHFGQTA VRRPDAKGQD DIYNRLWQKD NIAVIVFLEN RLTGERLIVV
NAHIYWDPAY KDVKLIQVAI MMEEVTQLAE KYVKIPPCTD KTAFRFSEPE DGKESQGTST
PVEPAPSVEY SSASQIPILV CGDFNSCPGS AVYNLLAHGR MAEEHPDLEQ RLYGNLSRMG
MSHPFTLKSA YSTIGELSFT NYTPGFTDVI DYIWYSSNTL QVTALLGEVD KEYLKRVPGF
PNYHFPSDHL ALMAEFSVKS KKNKPVEADF GPQREKTM
