CCR4_PHANO
ID CCR4_PHANO Reviewed; 597 AA.
AC Q0U7W4;
DT 12-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT 08-APR-2008, sequence version 2.
DT 03-AUG-2022, entry version 91.
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=SNOG_12150;
OS Phaeosphaeria nodorum (strain SN15 / ATCC MYA-4574 / FGSC 10173) (Glume
OS blotch fungus) (Parastagonospora nodorum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Pleosporineae; Phaeosphaeriaceae;
OC Parastagonospora.
OX NCBI_TaxID=321614;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SN15 / ATCC MYA-4574 / FGSC 10173;
RX PubMed=18024570; DOI=10.1105/tpc.107.052829;
RA Hane J.K., Lowe R.G.T., Solomon P.S., Tan K.-C., Schoch C.L.,
RA Spatafora J.W., Crous P.W., Kodira C.D., Birren B.W., Galagan J.E.,
RA Torriani S.F.F., McDonald B.A., Oliver R.P.;
RT "Dothideomycete-plant interactions illuminated by genome sequencing and EST
RT analysis of the wheat pathogen Stagonospora nodorum.";
RL Plant Cell 19:3347-3368(2007).
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; CH445345; EAT80562.2; -; Genomic_DNA.
DR RefSeq; XP_001802381.1; XM_001802329.1.
DR AlphaFoldDB; Q0U7W4; -.
DR SMR; Q0U7W4; -.
DR STRING; 13684.SNOT_12150; -.
DR EnsemblFungi; SNOT_12150; SNOT_12150; SNOG_12150.
DR GeneID; 5979291; -.
DR KEGG; pno:SNOG_12150; -.
DR eggNOG; KOG0620; Eukaryota.
DR HOGENOM; CLU_016428_4_0_1; -.
DR InParanoid; Q0U7W4; -.
DR OrthoDB; 724242at2759; -.
DR Proteomes; UP000001055; Unassembled WGS sequence.
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..597
FT /note="CCR4-Not complex 3'-5'-exoribonuclease subunit Ccr4"
FT /id="PRO_0000290616"
FT REPEAT 66..89
FT /note="LRR 1"
FT REPEAT 92..113
FT /note="LRR 2"
FT REPEAT 115..136
FT /note="LRR 3"
FT REPEAT 138..159
FT /note="LRR 4"
FT REPEAT 161..183
FT /note="LRR 5"
FT REGION 1..69
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..31
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 32..54
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 55..69
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 272
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:O95551"
SQ SEQUENCE 597 AA; 67713 MW; DC1F60759BA5544C CRC64;
MSNAQPHFAP SHLQNGTPNS VHSGVNRPTT EHWAEQRTRS ADSTKRRTRK SATGQQHSEP
RTARTTSRGQ YVDFGGQNLK VITPTLFINY SFLTKLYLNA NKLTYLHQAI GQLRNLTHLD
LSLNNLHSLP PEIGMLVNLK QLLVFDNQLT DLPEELGSLY QLELLGIEGN PIPDDIKQIM
MEQGTVELIK HFRETAAGPE APPERDWIVL DEITDPAQET VTALSYNILC DKYCTQSQYG
YTPSSALAWE TRRELILGEL KQRNADIVCL QEIDQDSFNE YFREKLAHYD YKGVFWPKSR
ARTMAEREAK LVDGCAIFYK NSKYVLLDKQ LIDFANTAIN RPDMKGEHDI FNRVMPRDDI
GVVAFLENRA TGSRFIVGNV HVFWNPAFTD VKLVQVAILM EGISKFATKW SKFPPCKDKV
VYRFTNGDDE DGKEADTTQE PGPSKEYGAG ADIPVILCGD FNSMPSSGVY DLITQGTIAH
SHQDLGSRKY GNFTRDGISH PFSLKSSYSA IGEMTFTNYV PHFQGVLDYI WYSTNTLQVV
GLLGDIDKEY LRRVPGFPNY HFPSDHVALY AQYIVKGRKE KKVSEVDFGP SRDRERR
