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Database: UniProt
Entry: Q6CX69_KLULA
LinkDB: Q6CX69_KLULA
Original site: Q6CX69_KLULA 
ID   Q6CX69_KLULA            Unreviewed;       484 AA.
AC   Q6CX69;
DT   16-AUG-2004, integrated into UniProtKB/TrEMBL.
DT   16-AUG-2004, sequence version 1.
DT   27-MAR-2024, entry version 118.
DE   RecName: Full=Ubiquitin carboxyl-terminal hydrolase {ECO:0000256|RuleBase:RU366025};
DE            EC=3.4.19.12 {ECO:0000256|RuleBase:RU366025};
GN   ORFNames=KLLA0_A10791g {ECO:0000313|EMBL:CAH03058.1};
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:CAH03058.1, ECO:0000313|Proteomes:UP000000598};
RN   [1] {ECO:0000313|EMBL:CAH03058.1, 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:RU366025};
CC   -!- SIMILARITY: Belongs to the peptidase C19 family.
CC       {ECO:0000256|RuleBase:RU366025}.
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DR   EMBL; CR382121; CAH03058.1; -; Genomic_DNA.
DR   RefSeq; XP_451470.1; XM_451470.1.
DR   AlphaFoldDB; Q6CX69; -.
DR   STRING; 284590.Q6CX69; -.
DR   MEROPS; C19.079; -.
DR   PaxDb; 284590-Q6CX69; -.
DR   GeneID; 2896629; -.
DR   KEGG; kla:KLLA0_A10791g; -.
DR   eggNOG; KOG1872; Eukaryota.
DR   HOGENOM; CLU_017549_2_1_1; -.
DR   InParanoid; Q6CX69; -.
DR   OMA; RKVQFPF; -.
DR   Proteomes; UP000000598; Chromosome A.
DR   GO; GO:0004843; F:cysteine-type deubiquitinase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IEA:InterPro.
DR   Gene3D; 6.10.140.1140; -; 1.
DR   Gene3D; 3.90.70.10; Cysteine proteinases; 1.
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; IPR044635; UBP14-like.
DR   InterPro; IPR018200; USP_CS.
DR   InterPro; IPR028889; USP_dom.
DR   PANTHER; PTHR43982; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE; 1.
DR   PANTHER; PTHR43982:SF1; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE 14; 1.
DR   Pfam; PF00443; UCH; 1.
DR   SMART; SM00213; UBQ; 1.
DR   SUPFAM; SSF54001; Cysteine proteinases; 1.
DR   SUPFAM; SSF54236; Ubiquitin-like; 1.
DR   PROSITE; PS00972; USP_1; 1.
DR   PROSITE; PS00973; USP_2; 1.
DR   PROSITE; PS50235; USP_3; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000256|RuleBase:RU366025};
KW   Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|RuleBase:RU366025};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000598};
KW   Thiol protease {ECO:0000256|ARBA:ARBA00022807,
KW   ECO:0000256|RuleBase:RU366025};
KW   Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786,
KW   ECO:0000256|RuleBase:RU366025}.
FT   DOMAIN          106..482
FT                   /note="USP"
FT                   /evidence="ECO:0000259|PROSITE:PS50235"
SQ   SEQUENCE   484 AA;  55373 MW;  2A2EF8BC57288EB5 CRC64;
     MSDLEFNIKH AGKVYPITIN ADAKAADLRA KVEALTLVPQ ERQKYMVKGG LTDNETLVSS
     VIKAKATVMV LGTPDANLVF KPTDDTKFLE DLTDKERLMQ EDTIPMGLRN MGNTCYFNAS
     LQALYRIKPL REKVLAYNEP NPDLHGQLVI QLRNCFNAFA QRKEKEFTPI ILLTVLRKIY
     PQFAEKDPST GFYKQQDAEE LFTQLLHTID TVFGESLSSK FEIEFQTTVK DTLNETDVQT
     KIESDKKLQC HISGTTNFLK NGLTESLVEK VEKRSEATGS NSIFENSKKI TKLPEYLTVQ
     FVRFYWKRST GKKSKILRKV QFPFQLDVAD LLTPEYATAK IKVRDELREV DKQREDDLKE
     FNQNILEHVP LSLTPAERYE TQMALEESKR EHWLAEFAKK FPKDLRQGEN PSSVYNLIGV
     VTHQGANSDS GHYQAFVRDD ADENKWYKYN DDKVYVVTRE KVEQLAGGGE SDSALILIYK
     GFGL
//
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