ID   CCR4_ENCCU              Reviewed;         493 AA.
AC   Q8SU52;
DT   03-NOV-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2002, sequence version 1.
DT   03-AUG-2022, entry version 117.
DE   RecName: Full=Probable 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=ECU11_0770;
OS   Encephalitozoon cuniculi (strain GB-M1) (Microsporidian parasite).
OC   Eukaryota; Fungi; Fungi incertae sedis; Microsporidia; Unikaryonidae;
OC   Encephalitozoon.
OX   NCBI_TaxID=284813;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=GB-M1;
RX   PubMed=11719806; DOI=10.1038/35106579;
RA   Katinka M.D., Duprat S., Cornillot E., Metenier G., Thomarat F.,
RA   Prensier G., Barbe V., Peyretaillade E., Brottier P., Wincker P.,
RA   Delbac F., El Alaoui H., Peyret P., Saurin W., Gouy M., Weissenbach J.,
RA   Vivares C.P.;
RT   "Genome sequence and gene compaction of the eukaryote parasite
RT   Encephalitozoon cuniculi.";
RL   Nature 414:450-453(2001).
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   -!- SUBUNIT: Component of the CCR4-NOT core complex. {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; AL590450; CAD25987.1; -; Genomic_DNA.
DR   RefSeq; NP_586383.1; NM_001042216.1.
DR   AlphaFoldDB; Q8SU52; -.
DR   SMR; Q8SU52; -.
DR   STRING; 284813.Q8SU52; -.
DR   PRIDE; Q8SU52; -.
DR   GeneID; 860036; -.
DR   KEGG; ecu:ECU11_0770; -.
DR   VEuPathDB; MicrosporidiaDB:ECU11_0770; -.
DR   HOGENOM; CLU_016428_4_2_1; -.
DR   InParanoid; Q8SU52; -.
DR   OMA; DHFLMLT; -.
DR   OrthoDB; 724242at2759; -.
DR   Proteomes; UP000000819; Chromosome XI.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
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   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; 3.
PE   3: Inferred from homology;
KW   Activator; Cytoplasm; Exonuclease; Hydrolase; Leucine-rich repeat;
KW   Magnesium; Metal-binding; Nuclease; Nucleus; Reference proteome; Repeat;
KW   Repressor; RNA-binding; Transcription; Transcription regulation.
FT   CHAIN           1..493
FT                   /note="Probable CCR4-Not complex 3'-5'-exoribonuclease
FT                   subunit Ccr4"
FT                   /id="PRO_0000388439"
FT   REPEAT          23..44
FT                   /note="LRR 1"
FT   REPEAT          46..67
FT                   /note="LRR 2"
FT   REPEAT          69..90
FT                   /note="LRR 3"
FT   REPEAT          92..113
FT                   /note="LRR 4"
FT   REPEAT          115..134
FT                   /note="LRR 5"
FT   BINDING         221
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250|UniProtKB:O95551"
SQ   SEQUENCE   493 AA;  56489 MW;  C8C4E4A040A1D52D CRC64;
     MAEECLVSRK KFGGKAMEVR SEMWTGLDLC SQGIKNISKS LFDMRFIRTL NLANNEIEVI
     PREICNLRHL EVLNLSKNKI RSIPPEIGKI VSLRELNLSD NLISNIPMEM GTLYNLEVFE
     IANNPLIVPF NTLIRDKKLL QFCREHNTGY PPPNDRLWIE CTGKNVFYGD TVSVGTFNIL
     SNIYATRMTY APSWVINSEF RREGVLQEIV LYNVDILCLQ EIELYSFFDF YKEQLEMRCN
     YDSIIYPRGR VKSVPDKKNV DGCAIFWRRS KFRLIAQFPI DFHQKVIQDT RFNTNQELLD
     RYGKKDNIAI GALLERPNGQ QVLVMNTHIF WDPDYPDIKL LQVLLLVEEI KRVSSRHPNA
     CLLLQGDFNS LRSSSVYKSI TTPVIDFADF GDTMQHLSNQ QFGDGLGLND AYSNQDLGFT
     NFTPGFKGVI DYIFYGGGIS LASVLSPVED EYTENVAGLP NMHFPSDHIF LGAKFAFPNK
     NISQNAFGRN SRQ