(data stored in ACNUC7421 zone)

SWISSPROT: Q750Z0_ASHGO

ID   Q750Z0_ASHGO            Unreviewed;       270 AA.
AC   Q750Z0;
DT   05-JUL-2004, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2004, sequence version 1.
DT   11-DEC-2019, entry version 115.
DE   SubName: Full=AGL203Cp {ECO:0000313|EMBL:AAS54288.1};
GN   ORFNames=AGOS_AGL203C {ECO:0000313|EMBL:AAS54288.1};
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 {ECO:0000313|EMBL:AAS54288.1, ECO:0000313|Proteomes:UP000000591};
RN   [1] {ECO:0000313|EMBL:AAS54288.1, ECO:0000313|Proteomes:UP000000591}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056
RC   {ECO:0000313|Proteomes:UP000000591};
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., Pohlmann 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] {ECO:0000313|Proteomes:UP000000591}
RP   GENOME REANNOTATION.
RC   STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056
RC   {ECO:0000313|Proteomes:UP000000591};
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   -!- SIMILARITY: Belongs to the ubiquitin-conjugating enzyme family.
CC       {ECO:0000256|RuleBase:RU362109, ECO:0000256|SAAS:SAAS00805669}.
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DR   EMBL; AE016820; AAS54288.1; -; Genomic_DNA.
DR   RefSeq; NP_986464.1; NM_211526.1.
DR   STRING; 33169.AAS54288; -.
DR   EnsemblFungi; AAS54288; AAS54288; AGOS_AGL203C.
DR   GeneID; 4622757; -.
DR   KEGG; ago:AGOS_AGL203C; -.
DR   HOGENOM; HOG000233454; -.
DR   InParanoid; Q750Z0; -.
DR   KO; K02207; -.
DR   OMA; AFNGGYF; -.
DR   Proteomes; UP000000591; Chromosome VII.
DR   GO; GO:0005737; C:cytoplasm; IEA:EnsemblFungi.
DR   GO; GO:0005634; C:nucleus; IEA:EnsemblFungi.
DR   GO; GO:0019005; C:SCF ubiquitin ligase complex; IEA:EnsemblFungi.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0061631; F:ubiquitin conjugating enzyme activity; IBA:GO_Central.
DR   GO; GO:0061630; F:ubiquitin protein ligase activity; IEA:EnsemblFungi.
DR   GO; GO:0000086; P:G2/M transition of mitotic cell cycle; IEA:EnsemblFungi.
DR   GO; GO:0051865; P:protein autoubiquitination; IEA:EnsemblFungi.
DR   GO; GO:0000209; P:protein polyubiquitination; IBA:GO_Central.
DR   GO; GO:0031146; P:SCF-dependent proteasomal ubiquitin-dependent protein catabolic process; IEA:EnsemblFungi.
DR   GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IBA:GO_Central.
DR   CDD; cd00195; UBCc; 1.
DR   Gene3D; 3.10.110.10; -; 1.
DR   InterPro; IPR000608; UBQ-conjugat_E2.
DR   InterPro; IPR023313; UBQ-conjugating_AS.
DR   InterPro; IPR016135; UBQ-conjugating_enzyme/RWD.
DR   Pfam; PF00179; UQ_con; 1.
DR   SUPFAM; SSF54495; SSF54495; 1.
DR   PROSITE; PS00183; UBIQUITIN_CONJUGAT_1; 1.
DR   PROSITE; PS50127; UBIQUITIN_CONJUGAT_2; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q750Z0.
DR   SWISS-2DPAGE; Q750Z0.
KW   ATP-binding {ECO:0000256|RuleBase:RU362109, ECO:0000256|SAAS:SAAS01166781};
KW   Nucleotide-binding {ECO:0000256|RuleBase:RU362109,
KW   ECO:0000256|SAAS:SAAS01166768};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000591};
KW   Transferase {ECO:0000256|SAAS:SAAS01018623};
KW   Ubl conjugation pathway {ECO:0000256|RuleBase:RU362109,
KW   ECO:0000256|SAAS:SAAS00805691}.
FT   DOMAIN          10..158
FT                   /note="UBIQUITIN_CONJUGAT_2"
FT                   /evidence="ECO:0000259|PROSITE:PS50127"
FT   REGION          186..270
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        203..241
FT                   /note="Acidic"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        242..256
FT                   /note="Polyampholyte"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        95
FT                   /note="Glycyl thioester intermediate"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10133"
SQ   SEQUENCE   270 AA;  30908 MW;  4A7980B11B4C5DFD CRC64;
     MSNRKNTAAS LLLRQYRELT DPKKAIPSFH IELDDDSNIF SWNIGVMVLN EDSIYHGGYF
     KAQMRFPEDF PFSPPSFRFT PAIYHPNVYR DGRLCISILH QSGDPTSDEP DSETWSPVQT
     VESVLISIVS LLEDPNISSP ANVDAAVDYR KNPEQYKQRV KLEVERSKQD IPPGFVMPTS
     QTAYISQRNT EPEEAKDVGD NFWYDSEEDD DMYGDDDDDA DNGHSNEEPE FEEEDDDDSM
     DNDSVMDKRK PDKADEESED VDDVKLDINK
//

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