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CCR4_NEUCR
ID   CCR4_NEUCR              Reviewed;         793 AA.
AC   Q9C2R2; V5ILT7;
DT   12-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT   04-DEC-2007, sequence version 2.
DT   03-AUG-2022, entry version 119.
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=NCU07779;
OS   Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 /
OS   FGSC 987).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Sordariomycetidae; Sordariales; Sordariaceae; Neurospora.
OX   NCBI_TaxID=367110;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987;
RX   PubMed=12655011; DOI=10.1093/nar/gkg293;
RA   Mannhaupt G., Montrone C., Haase D., Mewes H.-W., Aign V., Hoheisel J.D.,
RA   Fartmann B., Nyakatura G., Kempken F., Maier J., Schulte U.;
RT   "What's in the genome of a filamentous fungus? Analysis of the Neurospora
RT   genome sequence.";
RL   Nucleic Acids Res. 31:1944-1954(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987;
RX   PubMed=12712197; DOI=10.1038/nature01554;
RA   Galagan J.E., Calvo S.E., Borkovich K.A., Selker E.U., Read N.D.,
RA   Jaffe D.B., FitzHugh W., Ma L.-J., Smirnov S., Purcell S., Rehman B.,
RA   Elkins T., Engels R., Wang S., Nielsen C.B., Butler J., Endrizzi M.,
RA   Qui D., Ianakiev P., Bell-Pedersen D., Nelson M.A., Werner-Washburne M.,
RA   Selitrennikoff C.P., Kinsey J.A., Braun E.L., Zelter A., Schulte U.,
RA   Kothe G.O., Jedd G., Mewes H.-W., Staben C., Marcotte E., Greenberg D.,
RA   Roy A., Foley K., Naylor J., Stange-Thomann N., Barrett R., Gnerre S.,
RA   Kamal M., Kamvysselis M., Mauceli E.W., Bielke C., Rudd S., Frishman D.,
RA   Krystofova S., Rasmussen C., Metzenberg R.L., Perkins D.D., Kroken S.,
RA   Cogoni C., Macino G., Catcheside D.E.A., Li W., Pratt R.J., Osmani S.A.,
RA   DeSouza C.P.C., Glass N.L., Orbach M.J., Berglund J.A., Voelker R.,
RA   Yarden O., Plamann M., Seiler S., Dunlap J.C., Radford A., Aramayo R.,
RA   Natvig D.O., Alex L.A., Mannhaupt G., Ebbole D.J., Freitag M., Paulsen I.,
RA   Sachs M.S., Lander E.S., Nusbaum C., Birren B.W.;
RT   "The genome sequence of the filamentous fungus Neurospora crassa.";
RL   Nature 422:859-868(2003).
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   -!- SEQUENCE CAUTION:
CC       Sequence=CAC28578.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; AL513410; CAC28578.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; CM002240; ESA42355.1; -; Genomic_DNA.
DR   EMBL; CM002240; ESA42356.1; -; Genomic_DNA.
DR   RefSeq; XP_011394724.1; XM_011396422.1.
DR   RefSeq; XP_011394725.1; XM_011396423.1.
DR   AlphaFoldDB; Q9C2R2; -.
DR   SMR; Q9C2R2; -.
DR   STRING; 5141.EFNCRP00000007975; -.
DR   PRIDE; Q9C2R2; -.
DR   EnsemblFungi; ESA42355; ESA42355; NCU07779.
DR   EnsemblFungi; ESA42356; ESA42356; NCU07779.
DR   GeneID; 3874847; -.
DR   KEGG; ncr:NCU07779; -.
DR   VEuPathDB; FungiDB:NCU07779; -.
DR   HOGENOM; CLU_016428_4_0_1; -.
DR   InParanoid; Q9C2R2; -.
DR   Proteomes; UP000001805; Chromosome 2, Linkage Group V.
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   SMART; SM00369; LRR_TYP; 2.
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..793
FT                   /note="CCR4-Not complex 3'-5'-exoribonuclease subunit Ccr4"
FT                   /id="PRO_0000290615"
FT   REPEAT          241..264
FT                   /note="LRR 1"
FT   REPEAT          266..287
FT                   /note="LRR 2"
FT   REPEAT          289..310
FT                   /note="LRR 3"
FT   REPEAT          312..334
FT                   /note="LRR 4"
FT   REPEAT          335..354
FT                   /note="LRR 5"
FT   REGION          50..85
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          208..239
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          764..793
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        50..78
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        223..239
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        770..793
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         446
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250|UniProtKB:O95551"
SQ   SEQUENCE   793 AA;  88752 MW;  78E3900D086A6D48 CRC64;
     MADGHRYMQQ SFSTPLPTQF ASNNNLATGL LLNSLLNQFI ADPSAAQQQA AAQANPAHSS
     ATQINRGMYG QNHPQGHNPR LNGAAPGRQP NMPMFYNHVP QQGHPHQGHN AHHQVLQAGH
     SGHGARNDLM SHSTFSSGIM GNASPYTTNN LQNGHSVAAR GGPAEQPANE HWQKQMRLKE
     ESDRAHSAMT EQHQPHYYAR LKAPENKGIG GSLTAGGANA SGDSEEEVRR RPYQVEKRNR
     RQDWHNLDMS GQGLRALSSA LFSYDFLVEL YIASNRLTFL PAEIGKLRHL KILEASNNLL
     SELPPEIGMC TSLEKLLLFD NQIRDLPYEL GSLYKLDILG IEGNPINPGL REEIVERGTK
     SLINSLLEQA PVPLPPSPRK PIVVQEDVSP SLERIKVMTW NILCDKFATT NMYGYTPTGA
     LSWEYRKERI LQEIRDRDVD MLCLQEIATD VFRDFFSPEL AQNDYKGVHW PRPKAKTMNE
     KDAAAVDGCA IFYKGSKWIL LDKQLIDYAN IAINRPDMKN QHDIFNRVMP KDNIGIICFF
     ESRRTGARVI VANTHLAWEP TLADVKLVQT AILMENITKY AEKYVRWQPL KDKRGIQIPQ
     SVSVESDIPK PEMPEPGPSQ EYRSNTDIPL IVCGDYNSTQ ESSVYELLSM GRVTPEQSDF
     GGHQYGNFTR DGVAHPFSMR SAYVHLNGTP DELSFTNYVP GFQEVIDYIW YSTNTLEVVE
     LLGPPDQNHL KRVPGFPNYH FPADHIQIMA EFVIKQRKGE KVKVIHGSGG GASGQQQQQQ
     QLEGGQDFGS GSK
 
 
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