ID   Q6C1K8_YARLI            Unreviewed;       992 AA.
AC   Q6C1K8;
DT   16-AUG-2004, integrated into UniProtKB/TrEMBL.
DT   16-AUG-2004, sequence version 1.
DT   01-MAY-2013, entry version 51.
DE   RecName: Full=Ubiquitin carboxyl-terminal hydrolase;
DE            EC=3.4.19.12;
GN   OrderedLocusNames=YALI0F15367g; ORFNames=YALI0_F15367g;
OS   Yarrowia lipolytica (strain CLIB 122 / E 150) (Yeast) (Candida
OS   lipolytica).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
OC   Saccharomycetes; Saccharomycetales; Dipodascaceae; Yarrowia.
OX   NCBI_TaxID=284591;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CLIB 122 / E 150;
RX   PubMed=15229592; DOI=10.1038/nature02579;
RG   Genolevures;
RA   Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S.,
RA   Lafontaine I., de Montigny J., Marck C., Neuveglise C., Talla E.,
RA   Goffard N., Frangeul L., Aigle M., Anthouard V., Babour A., Barbe V.,
RA   Barnay S., Blanchin S., Beckerich J.-M., Beyne E., Bleykasten C.,
RA   Boisrame A., Boyer J., Cattolico L., Confanioleri F., de Daruvar A.,
RA   Despons L., Fabre E., Fairhead C., Ferry-Dumazet H., Groppi A.,
RA   Hantraye F., Hennequin C., Jauniaux N., Joyet P., Kachouri R.,
RA   Kerrest A., Koszul R., Lemaire M., Lesur I., Ma L., Muller H.,
RA   Nicaud J.-M., Nikolski M., Oztas S., Ozier-Kalogeropoulos O.,
RA   Pellenz S., Potier S., Richard G.-F., Straub M.-L., Suleau A.,
RA   Swennen D., Tekaia F., Wesolowski-Louvel M., Westhof E., Wirth B.,
RA   Zeniou-Meyer M., Zivanovic Y., 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: Thiol-dependent hydrolysis of ester,
CC       thioester, amide, peptide and isopeptide bonds formed by the C-
CC       terminal Gly of ubiquitin (a 76-residue protein attached to
CC       proteins as an intracellular targeting signal).
CC   -!- SIMILARITY: Belongs to the peptidase C19 family.
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DR   EMBL; CR382132; CAG78263.1; -; Genomic_DNA.
DR   RefSeq; XP_505454.1; XM_505454.1.
DR   ProteinModelPortal; Q6C1K8; -.
DR   STRING; 4952.Q6C1K8; -.
DR   GeneID; 2908061; -.
DR   KEGG; yli:YALI0F15367g; -.
DR   KO; K11839; -.
DR   OMA; YIVFYER; -.
DR   OrthoDB; EOG4HX88F; -.
DR   GO; GO:0008234; F:cysteine-type peptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0004221; F:ubiquitin thiolesterase activity; IEA:InterPro.
DR   GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IEA:InterPro.
DR   Gene3D; 3.40.250.10; -; 1.
DR   InterPro; IPR018200; Pept_C19ubi-hydrolase_C_CS.
DR   InterPro; IPR001394; Peptidase_C19.
DR   InterPro; IPR001763; Rhodanese-like_dom.
DR   Pfam; PF00581; Rhodanese; 1.
DR   Pfam; PF00443; UCH; 1.
DR   SMART; SM00450; RHOD; 1.
DR   SUPFAM; SSF52821; Rhodanese-like; 1.
DR   PROSITE; PS50206; RHODANESE_3; 1.
DR   PROSITE; PS00972; UCH_2_1; 1.
DR   PROSITE; PS00973; UCH_2_2; 1.
DR   PROSITE; PS50235; UCH_2_3; 1.
PE   3: Inferred from homology;
KW   Complete proteome; Hydrolase; Protease; Reference proteome;
KW   Thiol protease; Ubl conjugation pathway.
SQ   SEQUENCE   992 AA;  111194 MW;  27E1DC759B181325 CRC64;
     MSSAVHYAAL SPHRGCGLSL SPQLRDDVSH CATQGGAKPN NHGQPHTNHH FQLNRTPVVP
     MRYTNLEELG KAARQATGAV SGFKPKRMVD LALSQIEQYK QMLEMDLELA AYHIFQAREI
     LFVCIPRHPD YDKFQAKKGP FHETYVELCD LAETDRRVLE LISTVKGKYV REKTSGVRRQ
     SNDDLLQSID DTIRGFSHLD VQQQSAPPTE TDPLKDKLEK LRGRSPEVQR ATLTTNGSST
     TTTKNGVMPP PKISPPPVPV PQNGGYVRQS YVGPASVPSP PPHSVTPPTP PRHTITLKAP
     QLISYLGHAP ETLLLLDIRP RADFQKCHIA APNVVCVEPH LLEADMTDEQ VEEKMLAALT
     TEEFERFMAR SAFEIVVFYD QNSTSYQTRP LKILLKALYS QAFKRPLQRP PCLLVGGLDE
     WRHSGAATSF IDTRSPLQQR AELARTQTDP TPVASYDPNR VYSHPYASNY ASYAYSYGPN
     QSSPTPPPVP TTPPPKPPSA MSSSSSLNLP QSMALSSSTS LPDPSSYKNQ MYSCHPYLNE
     PLPESRHHTH GVSQPAQAAR SSHGYYSHAL PQLSVNTASS PIKQPPSAYS PKEKHNGEFP
     SYKSVRQPIP QSPYLPHLAP MSGSPPPMSL TFTTGLKNLG NTCYINCIIQ CLATSQLTKI
     IVNQAYKHRV NMKSKLGYKG ALIAKYADLV QALVANAYPY LVPTSFKGII AHVNSQFSGM
     EQHDCQEFLT FILDGLHEEL NSVGDGQYKP RELTESEEKR REEMSVRIVS SLEWERYLKS
     ASSFIVDEFQ GQYQSKLQCT VCKMTSTTYT AFSSLTLPIP KYAGATLPTL YDCFNQFTQP
     ELLEGENMWQ CPTCKKPRPT IKSMKISRLP ETLIIHLKRF DHSRGYGDKL NTFVTYPLEM
     DLTRYWPPPT SEDEPFLKKL LPRGQTAPFR YSLFGVANHY GTLRGGHYTS FCKRGKLGWC
     YFDDTVVNRN VNERAVVNKN AYVLFYQRRH NP
//