ID   CCR4_ENTBH              Reviewed;         481 AA.
AC   B7XK66;
DT   03-NOV-2009, integrated into UniProtKB/Swiss-Prot.
DT   03-MAR-2009, sequence version 1.
DT   03-AUG-2022, entry version 58.
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; ORFNames=EBI_22918;
OS   Enterocytozoon bieneusi (strain H348) (Microsporidian parasite).
OC   Eukaryota; Fungi; Fungi incertae sedis; Microsporidia; Enterocytozoonidae;
OC   Enterocytozoon.
OX   NCBI_TaxID=481877;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=H348;
RX   PubMed=18060071; DOI=10.1371/journal.pone.0001277;
RA   Corradi N., Akiyoshi D.E., Morrison H.G., Feng X., Weiss L.M., Tzipori S.,
RA   Keeling P.J.;
RT   "Patterns of genome evolution among the microsporidian parasites
RT   Encephalitozoon cuniculi, Antonospora locustae and Enterocytozoon
RT   bieneusi.";
RL   PLoS ONE 2:E1277-E1277(2007).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=H348;
RX   PubMed=19132089; DOI=10.1371/journal.ppat.1000261;
RA   Akiyoshi D.E., Morrison H.G., Lei S., Feng X., Zhang Q., Corradi N.,
RA   Mayanja H., Tumwine J.K., Keeling P.J., Weiss L.M., Tzipori S.;
RT   "Genomic survey of the non-cultivatable opportunistic human pathogen,
RT   Enterocytozoon bieneusi.";
RL   PLoS Pathog. 5:E1000261-E1000261(2009).
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; ABGB01000044; EED43664.1; -; Genomic_DNA.
DR   RefSeq; XP_002650396.1; XM_002650350.1.
DR   AlphaFoldDB; B7XK66; -.
DR   SMR; B7XK66; -.
DR   STRING; 481877.B7XK66; -.
DR   EnsemblFungi; EED43664; EED43664; EBI_22918.
DR   VEuPathDB; MicrosporidiaDB:EBI_22918; -.
DR   HOGENOM; CLU_016428_4_2_1; -.
DR   InParanoid; B7XK66; -.
DR   Proteomes; UP000001742; Unassembled WGS sequence.
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; 4.
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..481
FT                   /note="Probable CCR4-Not complex 3'-5'-exoribonuclease
FT                   subunit Ccr4"
FT                   /id="PRO_0000388440"
FT   REPEAT          20..41
FT                   /note="LRR 1"
FT   REPEAT          43..64
FT                   /note="LRR 2"
FT   REPEAT          66..87
FT                   /note="LRR 3"
FT   REPEAT          89..111
FT                   /note="LRR 4"
FT   REPEAT          112..133
FT                   /note="LRR 5"
FT   BINDING         218
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250|UniProtKB:O95551"
SQ   SEQUENCE   481 AA;  56348 MW;  41270CB604D38E7A CRC64;
     MEEKIKKKDY NKDIDNCDDE LEGLDMSFQG IKVIGKEITL LVSLKQLILN NNDIETIPED
     ISNLIRLEVL DFSYNKIEKI PTELGRLINL KELYLNNNMI VEVPMELGTL YKLENFSILN
     NPLVHPYGIM SKDKSLLRFC RENNTNYKQP NDRVWIDTVL KIDQSLETYS FGTFNILCSL
     YASNLTYAPS WVINLECRKD ILMQTFIAYN LDILCLQEVD INVFNTFYKE QLAQKLDYDG
     VILPKKSFDK VTDQPKKFHG IVTFWKKNKF KLIEQVSIDF FQKIINDKRF KYLSDIHTRI
     FQKTNVGLIT IFETCNTNII IIVANVHLYW NPEFNDIKIL QTIIYLEEIE FLKEKYKHAH
     IVLQGDFNSL QNSHVYQYII NRKLPTNIFD PWDYGSLNNG VTHSLTLRNA YDGHDITFTN
     FTPSFKAVID YIFYSKYLNL ISIISPIEDE YTKTTIGLPN IHFPSDHILI GAKFQFKSSK
     K