ID A0A1J9RCU7_9EURO Unreviewed; 777 AA.
AC A0A1J9RCU7;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=CCR4-Not complex 3'-5'-exoribonuclease subunit Ccr4 {ECO:0000256|ARBA:ARBA00023475};
DE EC=3.1.13.4 {ECO:0000256|ARBA:ARBA00012161};
DE AltName: Full=Carbon catabolite repressor protein 4 {ECO:0000256|ARBA:ARBA00030493};
DE AltName: Full=Cytoplasmic deadenylase {ECO:0000256|ARBA:ARBA00031469};
DE AltName: Full=Glucose-repressible alcohol dehydrogenase transcriptional effector {ECO:0000256|ARBA:ARBA00033317};
GN ORFNames=ACJ73_03124 {ECO:0000313|EMBL:OJD25501.1};
OS Blastomyces percursus.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Ajellomycetaceae; Blastomyces.
OX NCBI_TaxID=1658174 {ECO:0000313|EMBL:OJD25501.1, ECO:0000313|Proteomes:UP000242791};
RN [1] {ECO:0000313|EMBL:OJD25501.1, ECO:0000313|Proteomes:UP000242791}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=EI222 {ECO:0000313|EMBL:OJD25501.1,
RC ECO:0000313|Proteomes:UP000242791};
RA Cuomo C.A., Schwartz I.S., Kenyon C., De Hoog G.S., Govender N.P.,
RA Botha A., Moreno L., De Vries M., Munoz J.F., Stielow J.B.;
RT "Emmonsia species relationships and genome sequence.";
RL Submitted (AUG-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Acts as a 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. {ECO:0000256|ARBA:ARBA00043931}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Exonucleolytic cleavage of poly(A) to 5'-AMP.; EC=3.1.13.4;
CC Evidence={ECO:0000256|ARBA:ARBA00001663};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC -!- SIMILARITY: Belongs to the CCR4/nocturin family.
CC {ECO:0000256|ARBA:ARBA00010774}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OJD25501.1}.
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; LGTZ01000364; OJD25501.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1J9RCU7; -.
DR STRING; 1658174.A0A1J9RCU7; -.
DR VEuPathDB; FungiDB:ACJ73_03124; -.
DR OrthoDB; 37764at2759; -.
DR Proteomes; UP000242791; 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 CDD; cd09097; Deadenylase_CCR4; 1.
DR Gene3D; 3.60.10.10; Endonuclease/exonuclease/phosphatase; 1.
DR Gene3D; 3.80.10.10; Ribonuclease Inhibitor; 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 PANTHER; PTHR12121; CARBON CATABOLITE REPRESSOR PROTEIN 4; 1.
DR PANTHER; PTHR12121:SF34; POLY(A)-SPECIFIC RIBONUCLEASE; 1.
DR Pfam; PF03372; Exo_endo_phos; 1.
DR Pfam; PF12799; LRR_4; 1.
DR SMART; SM00369; LRR_TYP; 3.
DR SUPFAM; SSF56219; DNase I-like; 1.
DR SUPFAM; SSF52058; L domain-like; 1.
DR PROSITE; PS51450; LRR; 2.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Exonuclease {ECO:0000256|ARBA:ARBA00022839};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Leucine-rich repeat {ECO:0000256|ARBA:ARBA00022614};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nuclease {ECO:0000256|ARBA:ARBA00022722};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000242791};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW RNA-binding {ECO:0000256|ARBA:ARBA00022884};
KW Transcription {ECO:0000256|ARBA:ARBA00023163};
KW Transcription regulation {ECO:0000256|ARBA:ARBA00023015}.
FT DOMAIN 389..732
FT /note="Endonuclease/exonuclease/phosphatase"
FT /evidence="ECO:0000259|Pfam:PF03372"
FT REGION 21..76
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 96..182
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 205..229
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 752..777
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 114..159
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 167..181
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 209..223
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 777 AA; 88173 MW; 1CE3B6E3D427013C CRC64;
MADGTYRFQQ PVAGQFYFQQ QTQQHNHTNA HQRHLARNGT GSPTGRLKFN TDTPSPSRSP
PLNQSPGHNP YNMYSQGQHV MMNGGQAHQR FGMPMQKFQH PSHHPHHTQQ NPHHQHPHSQ
TSHAAIGHQH NFSSGTLSST APHFTPTHIP NGTTTNVDEE VEEPMNEHWQ QQLQLAAESR
QANSPHYYAR AVAQQTKGIQ LTANQAETDE NGTEERNRTK TSKSTPGRQD WMALDFGGQG
LRAISPALFN YTFLEKLYLN HNKLKTLPPT IGQLKSLTHL DVSGNELTEL PEEIGMLINL
KKLLLFDNNL HSLPYEMGYL YQLDTLGIEG NPLNDVFKSR IMQEGTKALI TYLKEEMPVH
LPPSERDWVV LDDSSRNPAK GQSDKFTALS YNTLCDRSAT HQQHGYAPSR ALAWGYRRDL
ILNEIKGYNA DIVCLQEIDQ GSYHGFFREQ LAYNDYKGVY WPKGRAQGMP EEEAKVVDGC
ATFFKGSKYI LLEKNMIHFG QTAVRRPDAK GQDDIYNRLW QKDNIAVVTY LENRLSGERL
IVVNVHLYWD PAYKDVKLIQ AAILMEEVTQ LAEKYSKIPA CTDKTAFRFS ELENSADGDG
TTTPVEPAPS VEYSSGSQIP LIICGDFNSY PGSAVYELMS RGYLIEDHPD LEKRLYGNLS
RRGMSYPFNL KSAYGAIGEL DFTNYTPDFA DVIDYIWYTS NALQVTGLLG AVDKEYLQRV
PGFPNYHFPS DHLALMAEFS FKSKKGKVVE VDFGPQRDRD RDRDKNRDRD RDRGRVT
//
