位置:首页 > 蛋白库 > CCR4_CRYNJ
CCR4_CRYNJ
ID   CCR4_CRYNJ              Reviewed;         744 AA.
AC   P0CP22; Q55PW8; Q5KDJ2;
DT   28-JUN-2011, integrated into UniProtKB/Swiss-Prot.
DT   28-JUN-2011, sequence version 1.
DT   03-AUG-2022, entry version 56.
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=CNG03790;
OS   Cryptococcus neoformans var. neoformans serotype D (strain JEC21 / ATCC
OS   MYA-565) (Filobasidiella neoformans).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Tremellomycetes;
OC   Tremellales; Cryptococcaceae; Cryptococcus;
OC   Cryptococcus neoformans species complex.
OX   NCBI_TaxID=214684;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JEC21 / ATCC MYA-565;
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AE017347; AAW44776.1; -; Genomic_DNA.
DR   RefSeq; XP_572083.1; XM_572083.1.
DR   AlphaFoldDB; P0CP22; -.
DR   SMR; P0CP22; -.
DR   STRING; 5207.AAW44776; -.
DR   PaxDb; P0CP22; -.
DR   EnsemblFungi; AAW44776; AAW44776; CNG03790.
DR   GeneID; 3258689; -.
DR   KEGG; cne:CNG03790; -.
DR   VEuPathDB; FungiDB:CNG03790; -.
DR   eggNOG; KOG0620; Eukaryota.
DR   HOGENOM; CLU_016428_4_0_1; -.
DR   InParanoid; P0CP22; -.
DR   OMA; YHFPSDH; -.
DR   OrthoDB; 724242at2759; -.
DR   Proteomes; UP000002149; Chromosome 7.
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: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:0000289; P:nuclear-transcribed mRNA poly(A) tail shortening; IBA:GO_Central.
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; Reference proteome; Repeat; RNA-binding;
KW   Transcription; Transcription regulation.
FT   CHAIN           1..744
FT                   /note="CCR4-Not complex 3'-5'-exoribonuclease subunit Ccr4"
FT                   /id="PRO_0000290610"
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..238
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        152..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;  82377 MW;  CEEAAA44E5B72A31 CRC64;
     MFYPHHQSQQ STTTNPSKHH DSQDVRLPGT SSWSRHPSHP SFTPSLPMPS PSGYPPLGSG
     YPPGGHHHPN VNVHSGIHGP HPSFGSGMGG NGGMGHGQGF GMGMFQNGVQ TSPPRGEPVP
     MTSHWQTQMM RAEASRSASS PHHRARAAAI SSRATNKPSA 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
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2024