ID Q6CNU0_KLULA Unreviewed; 245 AA.
AC Q6CNU0;
DT 16-AUG-2004, integrated into UniProtKB/TrEMBL.
DT 16-AUG-2004, sequence version 1.
DT 24-JAN-2024, entry version 100.
DE RecName: Full=Ubiquitin carboxyl-terminal hydrolase {ECO:0000256|RuleBase:RU361215};
DE EC=3.4.19.12 {ECO:0000256|RuleBase:RU361215};
GN ORFNames=KLLA0_E09967g {ECO:0000313|EMBL:CAG99486.1};
OS Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 /
OS NRRL Y-1140 / WM37) (Yeast) (Candida sphaerica).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Kluyveromyces.
OX NCBI_TaxID=284590 {ECO:0000313|EMBL:CAG99486.1, ECO:0000313|Proteomes:UP000000598};
RN [1] {ECO:0000313|EMBL:CAG99486.1, ECO:0000313|Proteomes:UP000000598}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 /
RC WM37 {ECO:0000313|Proteomes:UP000000598};
RX PubMed=15229592; DOI=10.1038/nature02579;
RG Genolevures;
RA Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA Beckerich J.M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA Lesur I., Ma L., Muller H., Nicaud J.M., Nikolski M., Oztas S.,
RA Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.F., Straub M.L.,
RA Suleau A., Swennene D., Tekaia F., Wesolowski-Louvel M., Westhof E.,
RA Wirth B., Zeniou-Meyer M., Zivanovic I., Bolotin-Fukuhara M., Thierry A.,
RA Bouchier C., Caudron B., Scarpelli C., Gaillardin C., Weissenbach J.,
RA Wincker P., Souciet J.L.;
RT "Genome evolution in yeasts.";
RL Nature 430:35-44(2004).
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|ARBA:ARBA00009326, ECO:0000256|RuleBase:RU361215}.
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DR EMBL; CR382125; CAG99486.1; -; Genomic_DNA.
DR RefSeq; XP_454399.1; XM_454399.1.
DR AlphaFoldDB; Q6CNU0; -.
DR STRING; 284590.Q6CNU0; -.
DR MEROPS; C12.002; -.
DR PaxDb; 284590-Q6CNU0; -.
DR GeneID; 2893995; -.
DR KEGG; kla:KLLA0_E09967g; -.
DR eggNOG; KOG1415; Eukaryota.
DR HOGENOM; CLU_054406_0_2_1; -.
DR InParanoid; Q6CNU0; -.
DR OMA; EFTADHQ; -.
DR Proteomes; UP000000598; Chromosome E.
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:SF17; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE; 1.
DR Pfam; PF01088; Peptidase_C12; 1.
DR PRINTS; PR00707; UBCTHYDRLASE.
DR SUPFAM; SSF54001; Cysteine proteinases; 1.
DR PROSITE; PS00140; UCH_1; 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:UP000000598};
KW Thiol protease {ECO:0000256|RuleBase:RU361215};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786,
KW ECO:0000256|RuleBase:RU361215}.
FT DOMAIN 96..112
FT /note="Ubiquitin carboxyl-terminal hydrolase family 1
FT cysteine active-site"
FT /evidence="ECO:0000259|PROSITE:PS00140"
SQ SEQUENCE 245 AA; 27027 MW; 16664C531927B323 CRC64;
MSQGKKEQKV RSVVPLESNP QVFTNFANSL GLSSDWALMD IYSLTDPDLL AFIPRPVKAV
ILLFPLNETI DSLTDSFKSD VPESKNGSSA PIWFKQNVRN ACGLYALLHS LSNNANLLTD
GSILKQFLTE NPASDGQYSD DDAVDDFLVS ISEIYNENSQ QGDTAAPSAE EDVELHFITF
IEKDGLLYEL DGRSKTGPRC LGKISPDSDL LTEPLVKQRF EWYHGNASES MKLQFSLLGL
GPSLD
//
