CCR4_ASPOR
ID CCR4_ASPOR Reviewed; 746 AA.
AC Q2UUI3;
DT 12-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT 24-JAN-2006, sequence version 1.
DT 03-AUG-2022, entry version 108.
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=AO090009000303;
OS Aspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=510516;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 42149 / RIB 40;
RX PubMed=16372010; DOI=10.1038/nature04300;
RA Machida M., Asai K., Sano M., Tanaka T., Kumagai T., Terai G., Kusumoto K.,
RA Arima T., Akita O., Kashiwagi Y., Abe K., Gomi K., Horiuchi H.,
RA Kitamoto K., Kobayashi T., Takeuchi M., Denning D.W., Galagan J.E.,
RA Nierman W.C., Yu J., Archer D.B., Bennett J.W., Bhatnagar D.,
RA Cleveland T.E., Fedorova N.D., Gotoh O., Horikawa H., Hosoyama A.,
RA Ichinomiya M., Igarashi R., Iwashita K., Juvvadi P.R., Kato M., Kato Y.,
RA Kin T., Kokubun A., Maeda H., Maeyama N., Maruyama J., Nagasaki H.,
RA Nakajima T., Oda K., Okada K., Paulsen I., Sakamoto K., Sawano T.,
RA Takahashi M., Takase K., Terabayashi Y., Wortman J.R., Yamada O.,
RA Yamagata Y., Anazawa H., Hata Y., Koide Y., Komori T., Koyama Y.,
RA Minetoki T., Suharnan S., Tanaka A., Isono K., Kuhara S., Ogasawara N.,
RA Kikuchi H.;
RT "Genome sequencing and analysis of Aspergillus oryzae.";
RL Nature 438:1157-1161(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; AP007150; BAE54782.1; -; Genomic_DNA.
DR RefSeq; XP_001816784.1; XM_001816732.2.
DR AlphaFoldDB; Q2UUI3; -.
DR SMR; Q2UUI3; -.
DR STRING; 510516.Q2UUI3; -.
DR EnsemblFungi; BAE54782; BAE54782; AO090009000303.
DR GeneID; 5988714; -.
DR KEGG; aor:AO090009000303; -.
DR VEuPathDB; FungiDB:AO090009000303; -.
DR HOGENOM; CLU_016428_4_0_1; -.
DR OMA; YHFPSDH; -.
DR Proteomes; UP000006564; Chromosome 1.
DR GO; GO:0030015; C:CCR4-NOT core complex; IEA:EnsemblFungi.
DR GO; GO:0016593; C:Cdc73/Paf1 complex; IEA:EnsemblFungi.
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:0000076; P:DNA replication checkpoint signaling; IEA:EnsemblFungi.
DR GO; GO:0000289; P:nuclear-transcribed mRNA poly(A) tail shortening; IEA:EnsemblFungi.
DR GO; GO:0032968; P:positive regulation of transcription elongation from RNA polymerase II promoter; IEA:EnsemblFungi.
DR GO; GO:0048478; P:replication fork protection; IEA:EnsemblFungi.
DR GO; GO:0006368; P:transcription elongation from RNA polymerase II promoter; IEA:EnsemblFungi.
DR GO; GO:0007089; P:traversing start control point of mitotic cell cycle; 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..746
FT /note="CCR4-Not complex 3'-5'-exoribonuclease subunit Ccr4"
FT /id="PRO_0000290605"
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 24..61
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 96..124
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 24..58
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 106..120
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 429
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:O95551"
SQ SEQUENCE 746 AA; 84117 MW; BB4397A33EF968F4 CRC64;
MADGTYRFQQ PGAGQFFFQT QQQQPSHQRH LVRNGTNSPT GRLKFSHDTP SPSRSPPLGQ
AAALNPFTMY SQTHQGQHVL MNGGQAHQRF GMQMPKFQSQ SHHPHPAQQA HHHTHHNQAS
HNINHQHNFS SGALAAATPH FTPSHMQNGA HANVDEDIDE SMNEHWQQQL QLAAESRQAS
SPHYYARAVA QQTKGIQIAP SQPEPQENGG DVKNGLTKVK ASPRQGWYAL DFGGQGLRAL
STSLFSYDFL KELYLNHNKL KALPQTIGQL RKLEHLDLSG NDLTELPEEI GMLTSLKKLY
LFDNNIRTLP YEMGYLYRLD TLGIEGNPLN DILKSQIMKE GTRALIKYLR EEMPENPPPP
DRDWVILDET AGTSTEKITV LSYNALCDSS ATQSHFGYTP SRALSWEFRR DVILSELRSH
DSDIVCLQEV DQGSYNGYFR EQLAYNGYKG VYWPRGRAMG MQEEEAKSVD GCATFFKGTK
FILLDKQMIN FGQTAVRRPD AKGQDDIYNR LWQKDHIAVV VFLENRLTGS RFIVVNAHLY
WDPAFKDVKL IQTAILMEEI TKLSETYAKW PACTDKTAFR FSEAEGGEAQ TPPEPAPSME
YSSGDQIPLF MCGDFNSSPG SAAYNLIANG RLTEEHPDLE KRLYGNLSRV GMTHPFKLKS
AYNSIGELSF TNYTPDFKDI LDYIWFTSNT LHVSALLGEV DKDYLQKVPG FPNFHFPSDH
IALFAEFVVK GKKGKVVEAD FGPQRN
