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CCR4_ASPFU
ID   CCR4_ASPFU              Reviewed;         696 AA.
AC   Q4WQG5;
DT   12-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2005, sequence version 1.
DT   03-AUG-2022, entry version 119.
DE   RecName: Full=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=AFUA_4G12750;
OS   Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC
OS   A1100) (Aspergillus fumigatus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Fumigati.
OX   NCBI_TaxID=330879;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100;
RX   PubMed=16372009; DOI=10.1038/nature04332;
RA   Nierman W.C., Pain A., Anderson M.J., Wortman J.R., Kim H.S., Arroyo J.,
RA   Berriman M., Abe K., Archer D.B., Bermejo C., Bennett J.W., Bowyer P.,
RA   Chen D., Collins M., Coulsen R., Davies R., Dyer P.S., Farman M.L.,
RA   Fedorova N., Fedorova N.D., Feldblyum T.V., Fischer R., Fosker N.,
RA   Fraser A., Garcia J.L., Garcia M.J., Goble A., Goldman G.H., Gomi K.,
RA   Griffith-Jones S., Gwilliam R., Haas B.J., Haas H., Harris D.E.,
RA   Horiuchi H., Huang J., Humphray S., Jimenez J., Keller N., Khouri H.,
RA   Kitamoto K., Kobayashi T., Konzack S., Kulkarni R., Kumagai T., Lafton A.,
RA   Latge J.-P., Li W., Lord A., Lu C., Majoros W.H., May G.S., Miller B.L.,
RA   Mohamoud Y., Molina M., Monod M., Mouyna I., Mulligan S., Murphy L.D.,
RA   O'Neil S., Paulsen I., Penalva M.A., Pertea M., Price C., Pritchard B.L.,
RA   Quail M.A., Rabbinowitsch E., Rawlins N., Rajandream M.A., Reichard U.,
RA   Renauld H., Robson G.D., Rodriguez de Cordoba S., Rodriguez-Pena J.M.,
RA   Ronning C.M., Rutter S., Salzberg S.L., Sanchez M., Sanchez-Ferrero J.C.,
RA   Saunders D., Seeger K., Squares R., Squares S., Takeuchi M., Tekaia F.,
RA   Turner G., Vazquez de Aldana C.R., Weidman J., White O., Woodward J.R.,
RA   Yu J.-H., Fraser C.M., Galagan J.E., Asai K., Machida M., Hall N.,
RA   Barrell B.G., Denning D.W.;
RT   "Genomic sequence of the pathogenic and allergenic filamentous fungus
RT   Aspergillus fumigatus.";
RL   Nature 438:1151-1156(2005).
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   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the CCR4/nocturin family. {ECO:0000305}.
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DR   EMBL; AAHF01000005; EAL89519.1; -; Genomic_DNA.
DR   RefSeq; XP_751557.1; XM_746464.1.
DR   AlphaFoldDB; Q4WQG5; -.
DR   SMR; Q4WQG5; -.
DR   STRING; 746128.CADAFUBP00006787; -.
DR   EnsemblFungi; EAL89519; EAL89519; AFUA_4G12750.
DR   GeneID; 3508916; -.
DR   KEGG; afm:AFUA_4G12750; -.
DR   eggNOG; KOG0620; Eukaryota.
DR   HOGENOM; CLU_016428_4_0_1; -.
DR   InParanoid; Q4WQG5; -.
DR   OMA; YHFPSDH; -.
DR   OrthoDB; 724242at2759; -.
DR   Proteomes; UP000002530; Chromosome 4.
DR   GO; GO:0030014; C:CCR4-NOT complex; IBA:GO_Central.
DR   GO; GO:0030015; C:CCR4-NOT core complex; IEA:EnsemblFungi.
DR   GO; GO:0016593; C:Cdc73/Paf1 complex; IEA:EnsemblFungi.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0000932; C:P-body; IEA:EnsemblFungi.
DR   GO; GO:0000175; F:3'-5'-exoribonuclease activity; IBA:GO_Central.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004535; F:poly(A)-specific ribonuclease activity; IBA:GO_Central.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0000076; P:DNA replication checkpoint signaling; IEA:EnsemblFungi.
DR   GO; GO:0000289; P:nuclear-transcribed mRNA poly(A) tail shortening; IBA:GO_Central.
DR   GO; GO:0032968; P:positive regulation of transcription elongation from RNA polymerase II promoter; IEA:EnsemblFungi.
DR   GO; GO:0048478; P:replication fork protection; IEA:EnsemblFungi.
DR   GO; GO:0006368; P:transcription elongation from RNA polymerase II promoter; IEA:EnsemblFungi.
DR   GO; GO:0007089; P:traversing start control point of mitotic cell cycle; IEA:EnsemblFungi.
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..696
FT                   /note="CCR4-Not complex 3'-5'-exoribonuclease subunit Ccr4"
FT                   /id="PRO_0000290603"
FT   REPEAT          181..202
FT                   /note="LRR 1"
FT   REPEAT          204..225
FT                   /note="LRR 2"
FT   REPEAT          227..248
FT                   /note="LRR 3"
FT   REPEAT          250..271
FT                   /note="LRR 4"
FT   REGION          30..56
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          95..126
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        37..52
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        96..119
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         378
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250|UniProtKB:O95551"
SQ   SEQUENCE   696 AA;  78849 MW;  332897F3F2D60271 CRC64;
     MYSQTHQGQH VMMNGGQAHQ RFGMQIPKFQ SQSHHPHHTQ QPHHHTHHNQ ASHNINHQHN
     FSSGALASAT PHFTPSHIQN GAHTNVDEDI DESMNEHWQQ QLQLAAESRQ ASSPHYHARS
     VAQQAKGIQI APSQPETQEQ VPDGQNGVVK AKASSRQGWH ALDFGGQGLR ALSTSLFNYI
     FLEKLYLNHN KLKALPPAIG QLRKLNHLDL SGNDLTELPE EIGMLTNLKK LYLFDNNIRT
     LPYEMGYLYR LETLGVEGNP LNDVLKSHIM KEGTKALIKY LKEEMPAFFF SCTTPLTLMA
     VHLPPPDRDW IVLDETASSS NHRTDKVTVL SYNTLCDSSA TQSHYGYAPA RVLSWEFRRE
     LILNELRSHD SDIICLQEID QGSYNEYFRE QLAYNDYKGV YWPRGRAMGM QEEDAKCVDG
     CATFFKGSKF ILLDKQLINF GQTAVRRPDA KGQDDIYNRL WQKDHIAVVV FLENRQTGAR
     FIVVNAHLYW DPAFKDVKLI QTAILMEELT KLSETYAKWP PCTDKAAFRF SKEEGQSETP
     PLEEPAPSMQ YASGDQIPLL MCGDLNSSPG SAAYNLIAHG RLDEEHPDLE KRLYGNLSKV
     GMTHPFKLKS AYGAIGELPF TNYTPDFKDI LDYIWYSSNS LHVSALLGEV DKDYLQRVPG
     FPNYHFPSDH IALLAEFTVK GKKGKVVEAD FGPQRN
 
 
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