位置:首页 > 蛋白库 > ESC2_ASHGO
ESC2_ASHGO
ID   ESC2_ASHGO              Reviewed;         407 AA.
AC   Q756K3;
DT   21-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   25-MAY-2022, entry version 89.
DE   RecName: Full=Protein ESC2;
DE   AltName: Full=Establishes silent chromatin protein 2;
GN   Name=ESC2; OrderedLocusNames=AER251W;
OS   Ashbya gossypii (strain ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056)
OS   (Yeast) (Eremothecium gossypii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Eremothecium.
OX   NCBI_TaxID=284811;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX   PubMed=15001715; DOI=10.1126/science.1095781;
RA   Dietrich F.S., Voegeli S., Brachat S., Lerch A., Gates K., Steiner S.,
RA   Mohr C., Poehlmann R., Luedi P., Choi S., Wing R.A., Flavier A.,
RA   Gaffney T.D., Philippsen P.;
RT   "The Ashbya gossypii genome as a tool for mapping the ancient Saccharomyces
RT   cerevisiae genome.";
RL   Science 304:304-307(2004).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX   PubMed=23749448; DOI=10.1534/g3.112.002881;
RA   Dietrich F.S., Voegeli S., Kuo S., Philippsen P.;
RT   "Genomes of Ashbya fungi isolated from insects reveal four mating-type
RT   loci, numerous translocations, lack of transposons, and distinct gene
RT   duplications.";
RL   G3 (Bethesda) 3:1225-1239(2013).
CC   -!- FUNCTION: May be a substrate targeting component of a cullin-RING-based
CC       E3 ubiquitin-protein ligase complex RTT101(MMS1-ESC2). Involved in HMR
CC       and telomere silencing via the recruitment or stabilizing of the SIR
CC       (silent information regulators) complex (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Component of a cullin-RING ligase (CRL)-like complex composed
CC       of at least the cullin RTT101, a linker protein MMS1, and the potential
CC       substrate receptor ESC2. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.
CC   -!- DOMAIN: The 2 SUMO-like regions, although related to ubiquitin domains
CC       lack the conserved acceptor Gly residue in position 456.
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; AE016818; AAS52932.1; -; Genomic_DNA.
DR   RefSeq; NP_985108.1; NM_210462.1.
DR   AlphaFoldDB; Q756K3; -.
DR   SMR; Q756K3; -.
DR   STRING; 33169.AAS52932; -.
DR   PRIDE; Q756K3; -.
DR   EnsemblFungi; AAS52932; AAS52932; AGOS_AER251W.
DR   GeneID; 4621318; -.
DR   KEGG; ago:AGOS_AER251W; -.
DR   eggNOG; ENOG502QS09; Eukaryota.
DR   HOGENOM; CLU_048318_0_0_1; -.
DR   InParanoid; Q756K3; -.
DR   OMA; FENEVTN; -.
DR   Proteomes; UP000000591; Chromosome V.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   InterPro; IPR022617; Rad60/SUMO-like_dom.
DR   InterPro; IPR000626; Ubiquitin-like_dom.
DR   InterPro; IPR029071; Ubiquitin-like_domsf.
DR   Pfam; PF11976; Rad60-SLD; 1.
DR   SUPFAM; SSF54236; SSF54236; 1.
DR   PROSITE; PS50053; UBIQUITIN_2; 1.
PE   3: Inferred from homology;
KW   Coiled coil; Cytoplasm; Nucleus; Reference proteome; Repeat; Repressor;
KW   Transcription; Transcription regulation.
FT   CHAIN           1..407
FT                   /note="Protein ESC2"
FT                   /id="PRO_0000227692"
FT   REPEAT          129..253
FT                   /note="SUMO-like region 1"
FT   REPEAT          334..407
FT                   /note="SUMO-like region 2"
FT   REGION          19..130
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        48..85
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        86..111
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        115..130
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   407 AA;  45434 MW;  F82222FD7454FF09 CRC64;
     MGEFNEYDDI DDFFCNDISP LHDEADEFGS TDIALPSQLY GKGPKPRAGE SKALRDRNKE
     SGSGTESEAK GDTLATKRGR SSWRRGASES SRSSSLGSSS PSDSSSGRSL SPVRPAKRKR
     TDEQQPESEA NRFLAEMERD IELSAGPGGG ETATGKGGRD TDARVYNVGF ISRIEGSRNR
     RVNVKVTGQK QFATFLAIAL AAFSKQHNIR KSLKPKYQAD QVKIYREGVE VFKFMTCDSF
     NIEEPYNASA TDIEVYIVPV DEATAFEQEW KRKFEERVRM LSNSSFLEVM DDIEDDNDDF
     LVNEYEKALV NARSLNETEL AVREGTPADE SSQLLKIVLL GSDNKKVFIH VRPTTTLLKV
     AEHYRVAKEL PPTVQLSLMF DHEEIDLDDT ICNIDIEDGD IIEVVVK
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2024