ID A0A0D2J1D4_9EURO Unreviewed; 747 AA.
AC A0A0D2J1D4;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 36.
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=Z518_08652 {ECO:0000313|EMBL:KIX02710.1};
OS Rhinocladiella mackenziei CBS 650.93.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae;
OC Rhinocladiella.
OX NCBI_TaxID=1442369 {ECO:0000313|EMBL:KIX02710.1, ECO:0000313|Proteomes:UP000053617};
RN [1] {ECO:0000313|EMBL:KIX02710.1, ECO:0000313|Proteomes:UP000053617}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 650.93 {ECO:0000313|EMBL:KIX02710.1,
RC ECO:0000313|Proteomes:UP000053617};
RG The Broad Institute Genomics Platform;
RA Cuomo C., de Hoog S., Gorbushina A., Stielow B., Teixiera M.,
RA Abouelleil A., Chapman S.B., Priest M., Young S.K., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Rhinocladiella mackenzie CBS 650.93.";
RL Submitted (JAN-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 ---------------------------------------------------------------------------
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; KN847480; KIX02710.1; -; Genomic_DNA.
DR RefSeq; XP_013269846.1; XM_013414392.1.
DR AlphaFoldDB; A0A0D2J1D4; -.
DR STRING; 1442369.A0A0D2J1D4; -.
DR GeneID; 25296723; -.
DR VEuPathDB; FungiDB:Z518_08652; -.
DR HOGENOM; CLU_016428_4_0_1; -.
DR OrthoDB; 37764at2759; -.
DR Proteomes; UP000053617; 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; 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; 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:UP000053617};
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 382..718
FT /note="Endonuclease/exonuclease/phosphatase"
FT /evidence="ECO:0000259|Pfam:PF03372"
FT REGION 1..62
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 86..161
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 16..30
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 43..62
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 93..113
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 115..149
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 747 AA; 84168 MW; FF47250362C8110E CRC64;
MADGAFQFHQ PGAGQFYPAQ HTNHRNPNRA SSPPGPRRPF NHDTPSPSRS PVGHSVGHTF
NMYSQNGYQT QHGLMNGAQN HQRYGNIHLP KYQPPHHGHH NVSQHHGQHH HGGQLGHQHN
ISSGGFQSTT PHLPTYSHEH LQNGNGNGLS HEDVDEPDNE HWREQKQFWE ESKDLNGPNQ
RARTVAHHSK GVSYVPLGAA AEDLQTEHSR VVTSNEQTSS RQTWDELDLG GQGLCALSPV
LFNPSYHFLK RLDLVYNQLE ALPSEIGQLK NLEHLDVSFN QLTELPEEIG MLTNLKQLLL
FNNHIQTLCY ELGFLYKLEV LGVYGNPLEQ GQRDKITEGG TRKLIEYLRE SMPEPPPPRE
RAWHQLEEIA DNDPTQDTVK ALSYNILCDR YATQSQYGYV AERVLGWGFR KTLILEEIRE
INADIVCLQE LDRTSYDDYF RPELSVSGYK GYYAQKSRAE TLGDLAKFVD GCGTFWKDKK
YVVLDTQHLV LGRKAVERPG AKASADMLNR VWQRDDIATV VFLENRLTGS RLIVVNAHIY
WDPAYKDVKL IQAAVLMEEL SKLADKYAKI PPATNKQVYR FSDAEDEQQP EPGPSLTYGS
GPQIPMVICG DFNSGAGSAV YDLFTKKGMN AEHADLDGRD YGAFSRAGMS HQFTLKSSYA
AIEGEMPFTN YTPSFADVLD YVWYSANSLR VVGLLGAIDP DYLKRVPGFP NFHFPSDHIA
IVAEFKVEKQ RNAQKTVEAD FGPTTKK
//
