ID M3BRY0_SPHMS Unreviewed; 764 AA.
AC M3BRY0;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 45.
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=SEPMUDRAFT_151776 {ECO:0000313|EMBL:EMF08868.1};
OS Sphaerulina musiva (strain SO2202) (Poplar stem canker fungus) (Septoria
OS musiva).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetidae; Mycosphaerellales; Mycosphaerellaceae; Sphaerulina.
OX NCBI_TaxID=692275 {ECO:0000313|EMBL:EMF08868.1, ECO:0000313|Proteomes:UP000016931};
RN [1] {ECO:0000313|EMBL:EMF08868.1, ECO:0000313|Proteomes:UP000016931}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SO2202 {ECO:0000313|EMBL:EMF08868.1,
RC ECO:0000313|Proteomes:UP000016931};
RX PubMed=23236275; DOI=10.1371/journal.ppat.1003037;
RA Ohm R.A., Feau N., Henrissat B., Schoch C.L., Horwitz B.A., Barry K.W.,
RA Condon B.J., Copeland A.C., Dhillon B., Glaser F., Hesse C.N., Kosti I.,
RA LaButti K., Lindquist E.A., Lucas S., Salamov A.A., Bradshaw R.E.,
RA Ciuffetti L., Hamelin R.C., Kema G.H.J., Lawrence C., Scott J.A.,
RA Spatafora J.W., Turgeon B.G., de Wit P.J.G.M., Zhong S., Goodwin S.B.,
RA Grigoriev I.V.;
RT "Diverse lifestyles and strategies of plant pathogenesis encoded in the
RT genomes of eighteen Dothideomycetes fungi.";
RL PLoS Pathog. 8:E1003037-E1003037(2012).
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}.
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DR EMBL; KB456270; EMF08868.1; -; Genomic_DNA.
DR RefSeq; XP_016756989.1; XM_016907039.1.
DR AlphaFoldDB; M3BRY0; -.
DR STRING; 692275.M3BRY0; -.
DR GeneID; 27904176; -.
DR eggNOG; KOG0620; Eukaryota.
DR HOGENOM; CLU_016428_4_0_1; -.
DR OMA; PHYYARA; -.
DR OrthoDB; 37764at2759; -.
DR Proteomes; UP000016931; 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; 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; 2.
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; SSF52075; Outer arm dynein light chain 1; 1.
DR PROSITE; PS51450; LRR; 3.
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:UP000016931};
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 390..502
FT /note="Endonuclease/exonuclease/phosphatase"
FT /evidence="ECO:0000259|Pfam:PF03372"
FT DOMAIN 617..733
FT /note="Endonuclease/exonuclease/phosphatase"
FT /evidence="ECO:0000259|Pfam:PF03372"
FT REGION 20..77
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 34..77
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 764 AA; 87100 MW; D8C16929DE2F6BD2 CRC64;
MADGLNRFNP GQQHYLYQNH TSHSRGHPLG GHRNGSPVNN NGRGLYHPNA DTPSPNRSPG
TNSPAHNPYS SSMYNHTSHR QNHNLLNGAA HQTFQPQQTA LGKVFQSSMH GGNQHHMNNQ
HHDNGMGGHT NHFGNHQHNI STSTLSNATP HFTPAHLQNG TTDNSLGKPQ TEHWAEQLRE
YQTLRMADQK AHYYARTAPS VSRLSGNLSK NAAKTDAEDG DRRRIIDESD EMGNFNTIDM
SGQGLKVLAP IVITRYTKLK NLYLSWNRLS SIPPQIGTMR FLTHLDLSFN NLSFLPPEIG
MLTNLKKLSL YDNNLEDLPY ELGTLFQLEM LGIEGNPLRQ EYKDRLMEHG TQELIRHLRE
QAPVPEPPLD RAWMPTVEDG TEFTDTFTVL SWNTLCDRAA SQAMYGYTPS EVLSWPRRRG
MILDEMKGRN ADIMCLQEMD LENFNEFFRP NLGSHDYRGI FNPKGRAATM GEKERNSVDG
CAVFWKNSKY IMLDKQFISF NSEAIKRQDM KGEHDVYNRV MPKDHVAVVL FLENRLTGSR
LIIANTHLTW EPWFQDIKIV QVAILMEQVQ KLSEKYAKWP ALKESEKKMF EFTSEDKPDG
TVTVPNKPGP SVKYDGPTNI PLIVCGDFNS TSHSGVYDLI TQGSLSNSHE ELGKYNYGDF
TRNGMSHPFS LKSAYSHIGE MKFTNYTPDF RQVIDWVFYS TQTMQVTGVL GEVDREYMKR
VPGFPNHYFP SDHLPLFTEF AIKEKKERKV TETSFGNSRR DNRN
//
