(data stored in ACNUC7421 zone)

SWISSPROT: Q751S0_ASHGO

ID   Q751S0_ASHGO            Unreviewed;       321 AA.
AC   Q751S0;
DT   05-JUL-2004, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2010, sequence version 2.
DT   11-DEC-2019, entry version 98.
DE   RecName: Full=Ubiquitin carboxyl-terminal hydrolase {ECO:0000256|PIRNR:PIRNR038120, ECO:0000256|RuleBase:RU361215};
DE            EC=3.4.19.12 {ECO:0000256|PIRNR:PIRNR038120, ECO:0000256|RuleBase:RU361215};
GN   ORFNames=AGOS_AGL316W {ECO:0000313|EMBL:AAS54175.2};
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:AAS54175.2, ECO:0000313|Proteomes:UP000000591};
RN   [1] {ECO:0000313|EMBL:AAS54175.2, 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|PIRNR:PIRNR038120,
CC         ECO:0000256|RuleBase:RU361215};
CC   -!- SIMILARITY: Belongs to the peptidase C12 family.
CC       {ECO:0000256|PIRNR:PIRNR038120, ECO:0000256|RuleBase:RU361215}.
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DR   EMBL; AE016820; AAS54175.2; -; Genomic_DNA.
DR   RefSeq; NP_986351.2; NM_211413.2.
DR   STRING; 33169.AAS54175; -.
DR   EnsemblFungi; AAS54175; AAS54175; AGOS_AGL316W.
DR   GeneID; 4622644; -.
DR   KEGG; ago:AGOS_AGL316W; -.
DR   HOGENOM; HOG000203918; -.
DR   InParanoid; Q751S0; -.
DR   KO; K05610; -.
DR   Proteomes; UP000000591; Chromosome VII.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0019784; F:NEDD8-specific protease activity; IEA:EnsemblFungi.
DR   GO; GO:0004843; F:thiol-dependent ubiquitin-specific protease activity; IBA:GO_Central.
DR   GO; GO:0071629; P:cytoplasm protein quality control by the ubiquitin-proteasome system; IEA:EnsemblFungi.
DR   GO; GO:0000338; P:protein deneddylation; IEA:EnsemblFungi.
DR   GO; GO:0016579; P:protein deubiquitination; IBA:GO_Central.
DR   Gene3D; 3.40.532.10; -; 1.
DR   InterPro; IPR038765; Papain-like_cys_pep_sf.
DR   InterPro; IPR001578; Peptidase_C12_UCH.
DR   InterPro; IPR036959; Peptidase_C12_UCH_sf.
DR   InterPro; IPR017390; Ubiquitinyl_hydrolase_UCH37.
DR   PANTHER; PTHR10589; PTHR10589; 1.
DR   Pfam; PF01088; Peptidase_C12; 1.
DR   PIRSF; PIRSF038120; Ubiquitinyl_hydrolase_UCH37; 1.
DR   PRINTS; PR00707; UBCTHYDRLASE.
DR   SUPFAM; SSF54001; SSF54001; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q751S0.
DR   SWISS-2DPAGE; Q751S0.
KW   Hydrolase {ECO:0000256|PIRNR:PIRNR038120, ECO:0000256|RuleBase:RU361215};
KW   Protease {ECO:0000256|PIRNR:PIRNR038120, ECO:0000256|RuleBase:RU361215};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000591};
KW   Thiol protease {ECO:0000256|PIRNR:PIRNR038120,
KW   ECO:0000256|RuleBase:RU361215};
KW   Ubl conjugation pathway {ECO:0000256|PIRNR:PIRNR038120,
KW   ECO:0000256|RuleBase:RU361215}.
FT   DOMAIN          4..201
FT                   /note="UCH_1"
FT                   /evidence="ECO:0000259|Pfam:PF01088"
FT   ACT_SITE        87
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR038120-1"
FT   ACT_SITE        169
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR038120-1"
FT   SITE            184
FT                   /note="Important for enzyme activity"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR038120-2"
SQ   SEQUENCE   321 AA;  35793 MW;  235816DA020BEBEC CRC64;
     MSSWQTIEND AGVFTQLVKD LGVEGVQFEE VPLVEHLATL NSPLYGVIFL FKYERQNYAG
     EAPVQGEFEQ ACPEGLFFAQ QTIPNACATQ AVLNTLLSIG NDHRNSIRLG TVLSDFLQFT
     AGFSDPALRG ETITNSVAIR NVHNSFTSPD PFEHEEPSPS AQSSEAAFHY SGFVPYNGYI
     YELDGLHPRP IIHRAYGANN DDPAVFAANL AALLSARMSM VADSSFSVTA IVRDKLEHLT
     EQLDAPDVDD GRRFWLQDLI QDELRVRDRW AKEIALRRDG LVGLVYAVFK QMLGSMSDDE
     FAQRRAAAAA RTNERERRRT C
//

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