CCR4_NEOFI
ID CCR4_NEOFI Reviewed; 750 AA.
AC A1CW67;
DT 12-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 1.
DT 03-AUG-2022, entry version 99.
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=NFIA_103570;
OS Neosartorya fischeri (strain ATCC 1020 / DSM 3700 / CBS 544.65 / FGSC A1164
OS / JCM 1740 / NRRL 181 / WB 181) (Aspergillus fischerianus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Fumigati.
OX NCBI_TaxID=331117;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 1020 / DSM 3700 / CBS 544.65 / FGSC A1164 / JCM 1740 / NRRL 181
RC / WB 181;
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; DS027685; EAW24869.1; -; Genomic_DNA.
DR RefSeq; XP_001266766.1; XM_001266765.1.
DR AlphaFoldDB; A1CW67; -.
DR SMR; A1CW67; -.
DR STRING; 36630.CADNFIAP00010012; -.
DR EnsemblFungi; EAW24869; EAW24869; NFIA_103570.
DR GeneID; 4593323; -.
DR KEGG; nfi:NFIA_103570; -.
DR VEuPathDB; FungiDB:NFIA_103570; -.
DR eggNOG; KOG0620; Eukaryota.
DR HOGENOM; CLU_016428_4_0_1; -.
DR OMA; YHFPSDH; -.
DR OrthoDB; 724242at2759; -.
DR Proteomes; UP000006702; Unassembled WGS sequence.
DR GO; GO:0030015; C:CCR4-NOT core complex; IEA:EnsemblFungi.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
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:0000289; P:nuclear-transcribed mRNA poly(A) tail shortening; 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; 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; 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..750
FT /note="CCR4-Not complex 3'-5'-exoribonuclease subunit Ccr4"
FT /id="PRO_0000290614"
FT REPEAT 249..270
FT /note="LRR 1"
FT REPEAT 272..293
FT /note="LRR 2"
FT REPEAT 295..316
FT /note="LRR 3"
FT REPEAT 318..339
FT /note="LRR 4"
FT REGION 31..60
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 98..124
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 175..194
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 105..120
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 432
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:O95551"
SQ SEQUENCE 750 AA; 84921 MW; 62F7AB33D9C1130D CRC64;
MADGTYRFQQ PGAGQFFFQT QPQQHSHQRH IARNGTNSPT GRLKFNHDTP SPSRSPPLSQ
AAALNPFNMY SQTHQGQHVM MNGGQAHQRF GMQIPKFQSQ SHHPHHTQQP HHHTHHNQAS
HNINHQHNFS SGALASATPH FTPSHIQNGA HTNVDEDIDE SMNEHWQQQL QLAAESRQAS
SPHYHARSVA QQAKGIQIAP SQPETQEQVP DGQNGVVKAK ASSRQGWHAL DFGGQGLRAL
STSLFNYVFL EKLYLNHNKL KALPPTIGQL RKLNHLDLSG NDLTELPEEI GMLTNLKKLY
LFDNNIRTLP YEMGYLYRLE TLGVEGNPLN DVLKSHIMKE GTKALIKYLK EEMPVHLPPP
DRDWIVLDET ASSSNHRTDK VTVLSYNTLC DSSATQSHYG YAPARVLSWE FRRELILNEL
RSHDSDIICL QEIDQGSYNE YFREQLAYND YKGVYWPRGR AMGMQEEDAK CVDGCATFFK
ASKFILLDKQ LINFGQTAVR RPDAKGQDDI YNRLWQKDHI AVVVFLENRQ TGSRFIVVNA
HLYWDPAFKD VKLIQTAILM EELTKLSETY AKWPPCTDKA AFRFSKEEGQ SETPPLEEPA
PSMQYASGDQ IPLLMCGDLN SSPGSAAYNL IAHGRLDEEH PDLEKRLYGN LSKVGMTHPF
KLKSAYGAIG ELPFTNYTPD FKDILDYIWY SSNSLHVSAL LGEVDKDYLQ RVPGFPNYHF
PSDHIALLAE FTVKGKKGKV VEADFGPQRN
