(data stored in ACNUC7421 zone)

SWISSPROT: Q757P1_ASHGO

ID   Q757P1_ASHGO            Unreviewed;       491 AA.
AC   Q757P1;
DT   05-JUL-2004, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2010, sequence version 2.
DT   11-DEC-2019, entry version 111.
DE   RecName: Full=Ubiquitin carboxyl-terminal hydrolase {ECO:0000256|RuleBase:RU366025};
DE            EC=3.4.19.12 {ECO:0000256|RuleBase:RU366025};
GN   ORFNames=AGOS_AEL029W {ECO:0000313|EMBL:AAS52656.2};
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:AAS52656.2, ECO:0000313|Proteomes:UP000000591};
RN   [1] {ECO:0000313|EMBL:AAS52656.2, 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   -!- CATALYTIC ACTIVITY:
CC       Reaction=Thiol-dependent hydrolysis of ester, thioester, amide, peptide
CC         and isopeptide bonds formed by the C-terminal Gly of ubiquitin (a 76-
CC         residue protein attached to proteins as an intracellular targeting
CC         signal).; EC=3.4.19.12; Evidence={ECO:0000256|RuleBase:RU366025};
CC   -!- SIMILARITY: Belongs to the peptidase C19 family.
CC       {ECO:0000256|RuleBase:RU366025, ECO:0000256|SAAS:SAAS01045498}.
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DR   EMBL; AE016818; AAS52656.2; -; Genomic_DNA.
DR   RefSeq; NP_984832.2; NM_210186.2.
DR   STRING; 33169.AAS52656; -.
DR   MEROPS; C19.079; -.
DR   EnsemblFungi; AAS52656; AAS52656; AGOS_AEL029W.
DR   GeneID; 4621029; -.
DR   KEGG; ago:AGOS_AEL029W; -.
DR   HOGENOM; HOG000202292; -.
DR   InParanoid; Q757P1; -.
DR   KO; K11843; -.
DR   OMA; NNSGYYE; -.
DR   Proteomes; UP000000591; Chromosome V.
DR   GO; GO:0005838; C:proteasome regulatory particle; IEA:EnsemblFungi.
DR   GO; GO:0004843; F:thiol-dependent ubiquitin-specific protease activity; IEA:EnsemblFungi.
DR   GO; GO:0072671; P:mitochondria-associated ubiquitin-dependent protein catabolic process; IEA:EnsemblFungi.
DR   GO; GO:1901799; P:negative regulation of proteasomal protein catabolic process; IEA:EnsemblFungi.
DR   GO; GO:0016579; P:protein deubiquitination; IEA:UniProtKB-UniRule.
DR   GO; GO:0032434; P:regulation of proteasomal ubiquitin-dependent protein catabolic process; IEA:EnsemblFungi.
DR   InterPro; IPR038765; Papain-like_cys_pep_sf.
DR   InterPro; IPR001394; Peptidase_C19_UCH.
DR   InterPro; IPR000626; Ubiquitin-like_dom.
DR   InterPro; IPR029071; Ubiquitin-like_domsf.
DR   InterPro; IPR018200; USP_CS.
DR   InterPro; IPR028889; USP_dom.
DR   Pfam; PF00443; UCH; 1.
DR   SMART; SM00213; UBQ; 1.
DR   SUPFAM; SSF54001; SSF54001; 1.
DR   SUPFAM; SSF54236; SSF54236; 1.
DR   PROSITE; PS00972; USP_1; 1.
DR   PROSITE; PS00973; USP_2; 1.
DR   PROSITE; PS50235; USP_3; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q757P1.
DR   SWISS-2DPAGE; Q757P1.
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Hydrolase {ECO:0000256|RuleBase:RU366025};
KW   Protease {ECO:0000256|RuleBase:RU366025};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000591};
KW   Thiol protease {ECO:0000256|RuleBase:RU366025};
KW   Ubl conjugation pathway {ECO:0000256|RuleBase:RU366025}.
FT   DOMAIN          105..489
FT                   /note="USP"
FT                   /evidence="ECO:0000259|PROSITE:PS50235"
FT   REGION          363..383
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          341..361
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   491 AA;  55038 MW;  E31E14AE54857867 CRC64;
     MGDFEFSIKH AGKVLPIKLP AGSTGADLRK AVEELVQIPA DRQKYMVKGG LGDETAVADV
     VKPGSSVLLL GTPDKDMVVK PRTAEKFIED LGADAQSGQL SRVPMGIVNM GNTCYMNATL
     QGLYGIVPLR EQILAFDDKK ATAEGMDLYH VQLIREIQAT FRKLRDKKGE AITPMLLLEI
     LRRVFPQFSE MDRQGGFYKQ QDAEELFTQL FHTMQTVFGE ELIDRFKIGF KTTIKDTMNE
     GDVTEKTEDD LKLRCHITGA TNFMKAGIKE SLKETIEKRS DVTGASSTYS VEKKITKLPE
     YLTVQYVRFF WKKSTGKKSK ILRKVQFPFQ LDVADLLTPE YAQTKIQVRE AFREVDKERA
     ESIRERKRSK FNPAPAEGGS TPAEAAEIAR SLEESTREKW ARAFAAKTPA DLGRGENPSC
     VYDLIGVITH QGANSESGHY QAFMRDEFDD DKWYKFNDDK VTAIEKEKIE SLAGGGESDS
     ALILIYKGFG L
//

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