ID G9MQK9_HYPVG Unreviewed; 431 AA.
AC G9MQK9;
DT 22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT 22-FEB-2012, sequence version 1.
DT 24-JAN-2024, entry version 51.
DE RecName: Full=Ubiquitin carboxyl-terminal hydrolase {ECO:0000256|RuleBase:RU361215};
DE EC=3.4.19.12 {ECO:0000256|RuleBase:RU361215};
DE Flags: Fragment;
GN ORFNames=TRIVIDRAFT_116373 {ECO:0000313|EMBL:EHK23277.1};
OS Hypocrea virens (strain Gv29-8 / FGSC 10586) (Gliocladium virens)
OS (Trichoderma virens).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Hypocreaceae; Trichoderma.
OX NCBI_TaxID=413071 {ECO:0000313|EMBL:EHK23277.1, ECO:0000313|Proteomes:UP000007115};
RN [1] {ECO:0000313|EMBL:EHK23277.1, ECO:0000313|Proteomes:UP000007115}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Gv29-8 / FGSC 10586 {ECO:0000313|Proteomes:UP000007115};
RX PubMed=21501500; DOI=10.1186/gb-2011-12-4-r40;
RA Kubicek C.P., Herrera-Estrella A., Seidl-Seiboth V., Martinez D.A.,
RA Druzhinina I.S., Thon M., Zeilinger S., Casas-Flores S., Horwitz B.A.,
RA Mukherjee P.K., Mukherjee M., Kredics L., Alcaraz L.D., Aerts A., Antal Z.,
RA Atanasova L., Cervantes-Badillo M.G., Challacombe J., Chertkov O.,
RA McCluskey K., Coulpier F., Deshpande N., von Doehren H., Ebbole D.J.,
RA Esquivel-Naranjo E.U., Fekete E., Flipphi M., Glaser F.,
RA Gomez-Rodriguez E.Y., Gruber S., Han C., Henrissat B., Hermosa R.,
RA Hernandez-Onate M., Karaffa L., Kosti I., Le Crom S., Lindquist E.,
RA Lucas S., Luebeck M., Luebeck P.S., Margeot A., Metz B., Misra M.,
RA Nevalainen H., Omann M., Packer N., Perrone G., Uresti-Rivera E.E.,
RA Salamov A., Schmoll M., Seiboth B., Shapiro H., Sukno S.,
RA Tamayo-Ramos J.A., Tisch D., Wiest A., Wilkinson H.H., Zhang M.,
RA Coutinho P.M., Kenerley C.M., Monte E., Baker S.E., Grigoriev I.V.;
RT "Comparative genome sequence analysis underscores mycoparasitism as the
RT ancestral life style of Trichoderma.";
RL Genome Biol. 12:R40.1-R40.15(2011).
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|ARBA:ARBA00000707,
CC ECO:0000256|RuleBase:RU361215};
CC -!- SIMILARITY: Belongs to the peptidase C12 family.
CC {ECO:0000256|RuleBase:RU361215}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EHK23277.1}.
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DR EMBL; ABDF02000005; EHK23277.1; -; Genomic_DNA.
DR RefSeq; XP_013957511.1; XM_014102036.1.
DR AlphaFoldDB; G9MQK9; -.
DR STRING; 413071.G9MQK9; -.
DR EnsemblFungi; EHK23277; EHK23277; TRIVIDRAFT_116373.
DR GeneID; 25787040; -.
DR VEuPathDB; FungiDB:TRIVIDRAFT_116373; -.
DR eggNOG; KOG2778; Eukaryota.
DR HOGENOM; CLU_018316_3_1_1; -.
DR InParanoid; G9MQK9; -.
DR OMA; GYHFIAY; -.
DR OrthoDB; 2714324at2759; -.
DR Proteomes; UP000007115; Unassembled WGS sequence.
DR GO; GO:0004843; F:cysteine-type deubiquitinase activity; IEA:UniProtKB-EC.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IEA:UniProtKB-UniRule.
DR Gene3D; 3.40.532.10; Peptidase C12, ubiquitin carboxyl-terminal hydrolase; 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; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE; 1.
DR PANTHER; PTHR10589:SF29; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE; 1.
DR Pfam; PF01088; Peptidase_C12; 1.
DR PRINTS; PR00707; UBCTHYDRLASE.
DR SUPFAM; SSF54001; Cysteine proteinases; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU361215};
KW Protease {ECO:0000256|RuleBase:RU361215};
KW Reference proteome {ECO:0000313|Proteomes:UP000007115};
KW Thiol protease {ECO:0000256|RuleBase:RU361215};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786,
KW ECO:0000256|RuleBase:RU361215}.
FT DOMAIN 46..271
FT /note="Ubiquitin carboxyl-terminal hydrolase family 1
FT cysteine active-site"
FT /evidence="ECO:0000259|Pfam:PF01088"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:EHK23277.1"
FT NON_TER 431
FT /evidence="ECO:0000313|EMBL:EHK23277.1"
SQ SEQUENCE 431 AA; 48895 MW; 50649C781337DB48 CRC64;
SLNERRRNPK RKAAEAAIES LNLPDNLLDE ALRPLTSTDI EEWEGWVELE SEPAFFNTIL
HDLGVKDVKV QELFSIDQSW LDTLLKPIYG LIFLFQYTPS VEEDEGEDET GSLWFANQTT
NNACATFALL NIVMNAPEVE LGDKLREFKE ATKNLNTVLR GHEVSNNKFM RSIHNSFTRR
MDHLNVDLCL ENAVSDTKSK KAKTGSKAAK KTSRKKRADD SYGFHFIAYV PVDGYVWELD
GLRSKPHRIG PIEADETCWT NIARPQIEGR ILQYEESQIS FNLLALCQRP VALHSHSIAQ
AAAAIRLLQE QMEHNSEFSG LINGQLPVLE KPAELSEFNL RSSDIENIAI PKEIQTKISH
ATANVDDAYD LYQQLVVDLK VAIGEHRAEM ISLGVDEQRV KDRKKDYGQA LHRWVQKLAE
KGILEDIIEN S
//
