CCR4_CRYNB
ID CCR4_CRYNB Reviewed; 744 AA.
AC P0CP23; Q55PW8; Q5KDJ2;
DT 28-JUN-2011, integrated into UniProtKB/Swiss-Prot.
DT 28-JUN-2011, sequence version 1.
DT 03-AUG-2022, entry version 46.
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=CNBG0960;
OS Cryptococcus neoformans var. neoformans serotype D (strain B-3501A)
OS (Filobasidiella neoformans).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Tremellomycetes;
OC Tremellales; Cryptococcaceae; Cryptococcus;
OC Cryptococcus neoformans species complex.
OX NCBI_TaxID=283643;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B-3501A;
RX PubMed=15653466; DOI=10.1126/science.1103773;
RA Loftus B.J., Fung E., Roncaglia P., Rowley D., Amedeo P., Bruno D.,
RA Vamathevan J., Miranda M., Anderson I.J., Fraser J.A., Allen J.E.,
RA Bosdet I.E., Brent M.R., Chiu R., Doering T.L., Donlin M.J., D'Souza C.A.,
RA Fox D.S., Grinberg V., Fu J., Fukushima M., Haas B.J., Huang J.C.,
RA Janbon G., Jones S.J.M., Koo H.L., Krzywinski M.I., Kwon-Chung K.J.,
RA Lengeler K.B., Maiti R., Marra M.A., Marra R.E., Mathewson C.A.,
RA Mitchell T.G., Pertea M., Riggs F.R., Salzberg S.L., Schein J.E.,
RA Shvartsbeyn A., Shin H., Shumway M., Specht C.A., Suh B.B., Tenney A.,
RA Utterback T.R., Wickes B.L., Wortman J.R., Wye N.H., Kronstad J.W.,
RA Lodge J.K., Heitman J., Davis R.W., Fraser C.M., Hyman R.W.;
RT "The genome of the basidiomycetous yeast and human pathogen Cryptococcus
RT neoformans.";
RL Science 307:1321-1324(2005).
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; AAEY01000036; EAL19803.1; -; Genomic_DNA.
DR RefSeq; XP_774450.1; XM_769357.1.
DR AlphaFoldDB; P0CP23; -.
DR SMR; P0CP23; -.
DR PRIDE; P0CP23; -.
DR EnsemblFungi; EAL19803; EAL19803; CNBG0960.
DR GeneID; 4937128; -.
DR KEGG; cnb:CNBG0960; -.
DR VEuPathDB; FungiDB:CNBG0960; -.
DR HOGENOM; CLU_016428_4_0_1; -.
DR Proteomes; UP000001435; Chromosome 7.
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.
PE 3: Inferred from homology;
KW Cytoplasm; Exonuclease; Hydrolase; Leucine-rich repeat; Magnesium;
KW Metal-binding; Nuclease; Nucleus; Repeat; RNA-binding; Transcription;
KW Transcription regulation.
FT CHAIN 1..744
FT /note="CCR4-Not complex 3'-5'-exoribonuclease subunit Ccr4"
FT /id="PRO_0000410168"
FT REPEAT 231..254
FT /note="LRR 1"
FT REPEAT 255..277
FT /note="LRR 2"
FT REPEAT 279..300
FT /note="LRR 3"
FT REPEAT 301..326
FT /note="LRR 4"
FT REGION 1..100
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 132..235
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..18
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 26..41
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 42..58
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 166..197
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 198..212
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 440
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:O95551"
SQ SEQUENCE 744 AA; 82361 MW; DB0C266B5C21058E CRC64;
MFYPHHQSQQ STTTNPSKHH DSQDVRLPGT SSWSRHPSHP SFTPSLPMPS PSGYPPLGSG
YPPGGHHHPN VNVHSGIHGP HPSFGSGMGG NGGMGHGQGF GMGMFQNGVQ TSPPRGEPVP
MTSHWQTQMM RAEASRSASS PHHRARAAAI SSRATNKPAA VPIVDPNNRP SSSYGTNGLH
RKNASSVFNG EPTGTPPLSD PSLTPAQNPA EPATPAPVAG QTESKDEEKP NEPWTGLDLG
GIRLKRLSTA LFSFTHVTSL YINHNALTSI PSAISSLRQL TLLDATGNEL STIPSEIGVL
SKLKDLLLFD NNLTTLPFEL GTLYQLDCLG IDGNPMNADY RKKLVEDGTR GLITYLRDHA
PPPPPPPERQ WIDLETDVDT PTSGKQESFS VLTYNILCAS FAPATTYSYT PSWALDWDYR
KRLLLEEIVT ASADVVCLQE IDCKQYADYF YPMLKKEGYE GQHYPRSRAK TMSVDEQKLV
DGCATFWKEE KFRLVETQVI EFNQLALQKT DMRTEDMFNR VMSRDNIAVV AALEFRASGG
RLLVANSHIY WDHRYRDVKL VQIGMLMEEL EKIVEQFSRY PVKLDTDPEY NNGKPPKYER
SEKGRDIPLI MCVDLNSFSG SAVYDYLSSG SIPGDHEDFM SHLYGRYTAS GLKHHLGLRS
ACAGIGEMRM TNFTPTFAAA IDYVFYTPRT MKVTSVLGDV DKAYLDKTVG FPNAHFPSDH
IPVFTQFRIK GHLDPLPLNG DPYH
