(data stored in SCRATCH zone)

SWISSPROT: Q751L5_ASHGO

ID   Q751L5_ASHGO            Unreviewed;       231 AA.
AC   Q751L5;
DT   05-JUL-2004, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2004, sequence version 1.
DT   11-DEC-2019, entry version 89.
DE   RecName: Full=Ubiquitin carboxyl-terminal hydrolase {ECO:0000256|RuleBase:RU361215};
DE            EC=3.4.19.12 {ECO:0000256|RuleBase:RU361215};
GN   ORFNames=AGOS_AGL314C {ECO:0000313|EMBL:AAS54177.1};
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:AAS54177.1, ECO:0000313|Proteomes:UP000000591};
RN   [1] {ECO:0000313|EMBL:AAS54177.1, 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   -!- 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:RU361215};
CC   -!- SIMILARITY: Belongs to the peptidase C12 family.
CC       {ECO:0000256|RuleBase:RU361215}.
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DR   EMBL; AE016820; AAS54177.1; -; Genomic_DNA.
DR   RefSeq; NP_986353.1; NM_211415.1.
DR   STRING; 33169.AAS54177; -.
DR   MEROPS; C12.002; -.
DR   EnsemblFungi; AAS54177; AAS54177; AGOS_AGL314C.
DR   GeneID; 4622646; -.
DR   KEGG; ago:AGOS_AGL314C; -.
DR   HOGENOM; HOG000182400; -.
DR   InParanoid; Q751L5; -.
DR   KO; K05609; -.
DR   OMA; YVCFVKG; -.
DR   Proteomes; UP000000591; Chromosome VII.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0004843; F:thiol-dependent ubiquitin-specific protease activity; IBA:GO_Central.
DR   GO; GO:0016579; P:protein deubiquitination; IBA:GO_Central.
DR   GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IEA:UniProtKB-UniRule.
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   PANTHER; PTHR10589; PTHR10589; 1.
DR   Pfam; PF01088; Peptidase_C12; 1.
DR   PRINTS; PR00707; UBCTHYDRLASE.
DR   SUPFAM; SSF54001; SSF54001; 1.
DR   PROSITE; PS00140; UCH_1; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q751L5.
DR   SWISS-2DPAGE; Q751L5.
KW   Hydrolase {ECO:0000256|RuleBase:RU361215};
KW   Protease {ECO:0000256|RuleBase:RU361215};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000591};
KW   Thiol protease {ECO:0000256|RuleBase:RU361215};
KW   Ubl conjugation pathway {ECO:0000256|RuleBase:RU361215}.
FT   DOMAIN          85..101
FT                   /note="UCH_1"
FT                   /evidence="ECO:0000259|PROSITE:PS00140"
SQ   SEQUENCE   231 AA;  25802 MW;  6CD023295990A1D7 CRC64;
     MACCPDSVTP LESSPEVFTD FAHALGLQSD MAFHDIYSLT DPDMLAFLSR PMKSVILLFP
     LNAFFRELIC PEYHGGDKSP IWFKQTIRNA CGMYALLHSL ANNRELVMQD SPLDRFLAQN
     PSADGRYDDQ NTVDFLVANG ELYQRSSLQG QTEAPDPEEE VELHFITFLV SGGQVFELDG
     RGKGPYLLGA ASDGDVLEQP LVKDRIQWFM DNADDEAKNQ FSLLGLGPSW K
//

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