ID D5GKN9_TUBMM Unreviewed; 680 AA.
AC D5GKN9;
DT 15-JUN-2010, integrated into UniProtKB/TrEMBL.
DT 15-JUN-2010, sequence version 1.
DT 27-MAR-2024, entry version 66.
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=GSTUM_00009675001 {ECO:0000313|EMBL:CAZ85082.1};
OS Tuber melanosporum (strain Mel28) (Perigord black truffle).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Pezizomycetes;
OC Pezizales; Tuberaceae; Tuber.
OX NCBI_TaxID=656061 {ECO:0000313|EMBL:CAZ85082.1, ECO:0000313|Proteomes:UP000006911};
RN [1] {ECO:0000313|EMBL:CAZ85082.1, ECO:0000313|Proteomes:UP000006911}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Mel28 {ECO:0000313|EMBL:CAZ85082.1,
RC ECO:0000313|Proteomes:UP000006911};
RX PubMed=20348908; DOI=10.1038/nature08867;
RA Martin F., Kohler A., Murat C., Balestrini R., Coutinho P.M., Jaillon O.,
RA Montanini B., Morin E., Noel B., Percudani R., Porcel B., Rubini A.,
RA Amicucci A., Amselem J., Anthouard V., Arcioni S., Artiguenave F.,
RA Aury J.M., Ballario P., Bolchi A., Brenna A., Brun A., Buee M.,
RA Cantarel B., Chevalier G., Couloux A., Da Silva C., Denoeud F.,
RA Duplessis S., Ghignone S., Hilselberger B., Iotti M., Marcais B., Mello A.,
RA Miranda M., Pacioni G., Quesneville H., Riccioni C., Ruotolo R.,
RA Splivallo R., Stocchi V., Tisserant E., Viscomi A.R., Zambonelli A.,
RA Zampieri E., Henrissat B., Lebrun M.H., Paolocci F., Bonfante P.,
RA Ottonello S., Wincker P.;
RT "Perigord black truffle genome uncovers evolutionary origins and mechanisms
RT of symbiosis.";
RL Nature 464:1033-1038(2010).
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 ---------------------------------------------------------------------------
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; FN430340; CAZ85082.1; -; Genomic_DNA.
DR RefSeq; XP_002840891.1; XM_002840845.1.
DR AlphaFoldDB; D5GKN9; -.
DR STRING; 656061.D5GKN9; -.
DR EnsemblFungi; CAZ85082; CAZ85082; GSTUM_00009675001.
DR GeneID; 9184744; -.
DR KEGG; tml:GSTUM_00009675001; -.
DR eggNOG; KOG0620; Eukaryota.
DR HOGENOM; CLU_016428_4_0_1; -.
DR InParanoid; D5GKN9; -.
DR OMA; PHYYARA; -.
DR OrthoDB; 37764at2759; -.
DR Proteomes; UP000006911; 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:0006260; P:DNA replication; IEA:EnsemblFungi.
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 by RNA polymerase II; IEA:EnsemblFungi.
DR GO; GO:0006368; P:transcription elongation by RNA polymerase II; IEA:EnsemblFungi.
DR GO; GO:0007089; P:traversing start control point of mitotic cell cycle; IEA:EnsemblFungi.
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; 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; PF00560; LRR_1; 1.
DR Pfam; PF13855; LRR_8; 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; 1.
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:UP000006911};
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 330..648
FT /note="Endonuclease/exonuclease/phosphatase"
FT /evidence="ECO:0000259|Pfam:PF03372"
FT REGION 40..80
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 95..157
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 659..680
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 95..129
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 139..157
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 666..680
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 680 AA; 76201 MW; 43BE0D21FA67AD6C CRC64;
MLNSQVHRGY MPQQPQNVKF LQQLAQPQGH QVDQAMNHVQ NNAGNNTVGG HSHSYSSGGL
GNPSYASPQH NSNGVTTTLQ NTSPHWQEQQ TLIATSRNSS SPHHHARQAA LSNKNSSQAQ
VTGGINPGAF QPLSAQHRKD GPPVEEKEVR KHDTGELERQ DWKSLDLGGQ GLRALSKSLF
QYTFLDKLYI NHNKLTVLPP AISRLKLLQL LDASGNQLTE VPPELGMLTN LKNLYLFDNQ
LTTLPNEIGS LYHLEVLGVE GNPLQSDLKE VMIKDGSRGV ILSLRESMQV SFSPVERDWI
ILDDSSRSGA KSEADKFQVL CYNILCDKYA TQNMYGYSPS WALSWDYRKK LIHDQLIESK
ADIICLQEVD MENFNEYFMP GLAREEYKGA FYPKSRAKTM NETEKKSVDG CATFFKSTKF
SLLEKQIVDF SSAALNREDM KKTADIYNRV MPKDNIAVIT FLENKITGSR LIVANVHIYW
DPQYRDVKLV QVGILMEDIT KYADQWAKSF PNRARSPGDT SPLEPAVNYS SGSQIPLIIC
GDFNSIADSG VYELLSRGSV ANDHDDLLGR TYGNFTRDGM SHPFPLKSGY SNIGELDFTN
YTPGFTGVID YIWYTTSNLN VTGLMGNVDK EYLARVPGFP NMHFPSDHIL LQTEFQVKPR
KEPIVKPPPP DFGNNPPRKS
//
