UniProt: A0A1L0BSF2

Database: UniProt
Entry: A0A1L0BSF2_9ASCO

LinkDB:  A0A1L0BSF2_9ASCO 
Original site:  A0A1L0BSF2_9ASCO

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Ontology (5)   
   GO (5)   
Chemical reaction (1)   
   KEGG ENZYME (1)   
DNA sequence (1)   
   EMBL (1)   
Protein domain (10)   
   InterPro (5)   
   Pfam (3)   
   PROSITE (1)   
   SMART (1)   
All databases (17)   

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ID   A0A1L0BSF2_9ASCO        Unreviewed;       731 AA.
AC   A0A1L0BSF2;
DT   15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT   15-FEB-2017, sequence version 1.
DT   27-MAR-2024, entry version 24.
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=SAMEA4029010_CIC11G00000003097 {ECO:0000313|EMBL:SGZ53154.1};
OS   [Candida] intermedia.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Metschnikowiaceae; Metschnikowiaceae incertae sedis;
OC   Candida/Metschnikowiaceae.
OX   NCBI_TaxID=45354 {ECO:0000313|EMBL:SGZ53154.1, ECO:0000313|Proteomes:UP000182334};
RN   [1] {ECO:0000313|EMBL:SGZ53154.1, ECO:0000313|Proteomes:UP000182334}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 141442 {ECO:0000313|EMBL:SGZ53154.1,
RC   ECO:0000313|Proteomes:UP000182334};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
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; LT635759; SGZ53154.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1L0BSF2; -.
DR   STRING; 45354.A0A1L0BSF2; -.
DR   OrthoDB; 37764at2759; -.
DR   Proteomes; UP000182334; Chromosome iv.
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; 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; 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:UP000182334};
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          385..696
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"
SQ   SEQUENCE   731 AA;  84061 MW;  AF1E891EED260C03 CRC64;
     MNSNHKFQQQ PGLPSQQILL QQLQQPQGNQ PSQQQQQQQQ QQQQQQQPQQ QQQPLGHYSG
     QSQVFNQHPQ LSQQKFVNQQ TMLQPPSLGM PMTGGNQGFP APVKVNSINV DDPNTVYWQN
     QVQLCQLSRS EDIPHFYARQ YAQNSRKNKN PYGDVKAVTL IDATKTVVAA LDEQEKQQSA
     AQASAALMRN KKVDLEEDEE QRMMARTQGK QLWCHLDLSG QGLLNISPKL FQYDFLESLY
     LNNNKLTTVP TVIKKLRGLR VLDLSHNRIS EVPGELGLCY NLRYLYLFDN NIKTLPNEFR
     NLIELLFLGI EGNPIDLKIA NLIAEKGTKE LISYFRDMEP TYPEPKPRQW LLLKEDGEII
     DPVTNPGIYS EDLMNSDSHD TFTLLTYNTL CQHYATTKLY KYTPSWALDW NFRRNSLKEE
     IVRLGTDVIC LQEVETRTFH EFWVPVMEAI GYKGYFFSKT RSKTMSELES KKVDGCATFY
     RMSKFQLVQK QHLEYNTVCM GSDRYKKTKD LFNRFMNKDH IALITYLQHV ETGEKIVIVN
     THLHWDPAFN DVKALQVGIL LEELQVIIKK FLHTNSMDDV KNSSLIICGD FNSTKKSAVY
     QLISTGSVSN HEDLHGRDYG RFTDEGFHHN FKLKSAYDHI ASDFPFSNFT PTFTSEIDYV
     WYSTGTLQVK GLLGKADEEY SSHQVGFPSA HFPSDHIPLV TKFQIRKKGS VAANKKTDFK
     PDFKSGSSRK T
//

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