CCR4_ASPTN
ID CCR4_ASPTN Reviewed; 677 AA.
AC Q0CT27;
DT 12-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT 17-OCT-2006, sequence version 1.
DT 03-AUG-2022, entry version 90.
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=ATEG_03157;
OS Aspergillus terreus (strain NIH 2624 / FGSC A1156).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=341663;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NIH 2624 / FGSC A1156;
RA Birren B.W., Lander E.S., Galagan J.E., Nusbaum C., Devon K., Henn M.,
RA Ma L.-J., Jaffe D.B., Butler J., Alvarez P., Gnerre S., Grabherr M.,
RA Kleber M., Mauceli E.W., Brockman W., Rounsley S., Young S.K., LaButti K.,
RA Pushparaj V., DeCaprio D., Crawford M., Koehrsen M., Engels R.,
RA Montgomery P., Pearson M., Howarth C., Larson L., Luoma S., White J.,
RA Alvarado L., Kodira C.D., Zeng Q., Oleary S., Yandava C., Denning D.W.,
RA Nierman W.C., Milne T., Madden K.;
RT "Annotation of the Aspergillus terreus NIH2624 genome.";
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
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; CH476597; EAU36431.1; -; Genomic_DNA.
DR RefSeq; XP_001212335.1; XM_001212335.1.
DR AlphaFoldDB; Q0CT27; -.
DR SMR; Q0CT27; -.
DR STRING; 341663.Q0CT27; -.
DR EnsemblFungi; EAU36431; EAU36431; ATEG_03157.
DR GeneID; 4317897; -.
DR VEuPathDB; FungiDB:ATEG_03157; -.
DR eggNOG; KOG0620; Eukaryota.
DR HOGENOM; CLU_016428_4_0_1; -.
DR OMA; YHFPSDH; -.
DR OrthoDB; 724242at2759; -.
DR Proteomes; UP000007963; Unassembled WGS sequence.
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; IPR025875; Leu-rich_rpt_4.
DR InterPro; IPR003591; Leu-rich_rpt_typical-subtyp.
DR InterPro; IPR032675; LRR_dom_sf.
DR Pfam; PF03372; Exo_endo_phos; 1.
DR Pfam; PF12799; LRR_4; 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..677
FT /note="CCR4-Not complex 3'-5'-exoribonuclease subunit Ccr4"
FT /id="PRO_0000290606"
FT REPEAT 180..201
FT /note="LRR 1"
FT REPEAT 203..224
FT /note="LRR 2"
FT REPEAT 226..247
FT /note="LRR 3"
FT REPEAT 249..270
FT /note="LRR 4"
FT REGION 30..49
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 128..155
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 128..152
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 359
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:O95551"
SQ SEQUENCE 677 AA; 76457 MW; DFCDC12D9CCE4115 CRC64;
MYSQTHQGQH VLMNGGQAHQ RFGMQIPKFQ SQGHHHPAQQ PHHHAHHNQA THNITHQHNF
SSGALAAATP HFTPSHMQNG AHANVDEDID ESMNEHWQQQ LQLAAESRQA SSPHYYARAV
AQQTKGIQIA PSQPDGQENG TDNRNGTVKT KSKPRQGWHA LDFGGQGLRA LSTSLFNYVF
LEKLYLNHNK LKALPQTIGQ LRKLEHLDLS GNDLTELPEE IGMLTSLKKL YLFDNNIRTL
PYEMGYLYRL DTLGIEGNPL NDILKSQIMK EGTKALIRYL REEMPVHLPP PDRDWVILDD
TSSSTEKVTV LSHNALCDSS ATSSHFGYTP SRALSWEFRR ELILSELRSH DSDIVCLQEV
DQGSYNGFFR EQLAYNDYKG VYWPRGRAMG MQEEEAKNVD GCATFFKGSK FILLDKQMIN
FGQTAVRRPD AKGQDDIYNR LWQKDHIAVV VFLENRLTGS RFIVVNAHLY WDPAFKDVKL
IQTAILMEEI TKLSDGYAKW PPCTDKTAFR FSEAEGGGES ENQPEPAPSM EYASGDQIPL
FMCGDFNSSP GSAAYNLIAN GRLTEEHPDL EKRLYGNLSR VGMTHPFKLK SAYGSIGELS
FTNYTPDFKD ILDYIWYTSN TLHVSALLGE VDKDYLQKVP GFPNFHFPSD HIALFAEFSV
KGKKGKVVEA DFGPQRS
