ID   UBPL2_MIMIV             Reviewed;         445 AA.
AC   Q5UPW7;
DT   03-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   07-DEC-2004, sequence version 1.
DT   03-AUG-2022, entry version 66.
DE   RecName: Full=Putative ubiquitin carboxyl-terminal hydrolase L293;
DE            EC=3.4.19.12;
DE   AltName: Full=Deubiquitinating enzyme L293;
DE   AltName: Full=Ubiquitin thioesterase L293;
DE   AltName: Full=Ubiquitin-specific-processing protease L293;
GN   OrderedLocusNames=MIMI_L293;
OS   Acanthamoeba polyphaga mimivirus (APMV).
OC   Viruses; Varidnaviria; Bamfordvirae; Nucleocytoviricota; Megaviricetes;
OC   Imitervirales; Mimiviridae; Mimivirus.
OX   NCBI_TaxID=212035;
OH   NCBI_TaxID=5757; Acanthamoeba polyphaga (Amoeba).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=Rowbotham-Bradford;
RX   PubMed=15486256; DOI=10.1126/science.1101485;
RA   Raoult D., Audic S., Robert C., Abergel C., Renesto P., Ogata H.,
RA   La Scola B., Susan M., Claverie J.-M.;
RT   "The 1.2-megabase genome sequence of Mimivirus.";
RL   Science 306:1344-1350(2004).
RN   [2]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], AND SUBCELLULAR
RP   LOCATION.
RX   PubMed=16971431; DOI=10.1128/jvi.00940-06;
RA   Renesto P., Abergel C., Decloquement P., Moinier D., Azza S., Ogata H.,
RA   Fourquet P., Gorvel J.-P., Claverie J.-M., Raoult D.;
RT   "Mimivirus giant particles incorporate a large fraction of anonymous and
RT   unique gene products.";
RL   J. Virol. 80:11678-11685(2006).
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;
CC   -!- SUBCELLULAR LOCATION: Virion {ECO:0000269|PubMed:16971431}.
CC   -!- SIMILARITY: Belongs to the peptidase C19 family. {ECO:0000305}.
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DR   EMBL; AY653733; AAV50565.1; -; Genomic_DNA.
DR   RefSeq; YP_003986795.1; NC_014649.1.
DR   SMR; Q5UPW7; -.
DR   GeneID; 9924908; -.
DR   KEGG; vg:9924908; -.
DR   Proteomes; UP000001134; Genome.
DR   GO; GO:0004843; F:cysteine-type deubiquitinase activity; IEA:UniProtKB-EC.
DR   GO; GO:0016579; P:protein deubiquitination; IEA:InterPro.
DR   InterPro; IPR038765; Papain-like_cys_pep_sf.
DR   InterPro; IPR001394; Peptidase_C19_UCH.
DR   InterPro; IPR028889; USP_dom.
DR   Pfam; PF00443; UCH; 1.
DR   SUPFAM; SSF54001; SSF54001; 1.
DR   PROSITE; PS50235; USP_3; 1.
PE   1: Evidence at protein level;
KW   Hydrolase; Protease; Reference proteome; Thiol protease;
KW   Ubl conjugation pathway; Virion.
FT   CHAIN           1..445
FT                   /note="Putative ubiquitin carboxyl-terminal hydrolase L293"
FT                   /id="PRO_0000251133"
FT   DOMAIN          133..441
FT                   /note="USP"
FT   ACT_SITE        142
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        384
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   445 AA;  50458 MW;  E5C2D9653139DCE4 CRC64;
     MCVEMKNKTN TTIPSQPQIP IQPSILPTQQ TISPIPQIIP PTQPTLPKLQ LDPILGSNGI
     PIANQEWSGT EYVRTNDPTK FIVITKTLDP KIARFLPTFK KPVITDIINK TSNSTLDMNK
     IITTNNFNVE NAKALANFGN SCYFGTSMQL LFVMFHVRNF IVKNSNFTET GISIDLKNAY
     DSIKNLFITM NTAPKNDPIK SFPDYPNVKK QIMKEPDPVQ MLEEDAEEFI TQFMSDLDPK
     ARNLALIKGN EYIYDVSNAQ LNRQQSFSNI FNLIPLDIIK SNPTDTLENI LSKTYTMVEL
     REGVNTIQNP ITSDYEFTYF VNQPTILPEY FLVRLNMVDP TSTNKLRHNI QINTTLVLTI
     NGQTTTYFAL AIIVHRGNSI RTGHYTCLVF DNQTGSQFQY IFYDDSLSSL VSIPTNSKII
     PSNLYLKNIT DSAYIILYGD ITKLR