ID   UBPL1_MIMIV             Reviewed;         468 AA.
AC   Q5UQR3;
DT   13-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT   07-DEC-2004, sequence version 1.
DT   27-MAR-2024, entry version 76.
DE   RecName: Full=Probable ubiquitin carboxyl-terminal hydrolase R319;
DE            EC=3.4.19.12;
DE   AltName: Full=Deubiquitinating enzyme R319;
DE   AltName: Full=Ubiquitin thioesterase R319;
DE   AltName: Full=Ubiquitin-specific-processing protease R319;
GN   OrderedLocusNames=MIMI_R319;
OS   Acanthamoeba polyphaga mimivirus (APMV).
OC   Viruses; Varidnaviria; Bamfordvirae; Nucleocytoviricota; Megaviricetes;
OC   Imitervirales; Mimiviridae; Megamimivirinae; Mimivirus;
OC   Mimivirus bradfordmassiliense.
OX   NCBI_TaxID=212035;
OH   NCBI_TaxID=5757; Acanthamoeba polyphaga (Amoeba).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE 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).
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   -!- SIMILARITY: Belongs to the peptidase C19 family. {ECO:0000305}.
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DR   EMBL; AY653733; AAV50588.1; -; Genomic_DNA.
DR   RefSeq; YP_003986822.1; NC_014649.1.
DR   SMR; Q5UQR3; -.
DR   GeneID; 9924936; -.
DR   KEGG; vg:9924936; -.
DR   OrthoDB; 8303at10239; -.
DR   Proteomes; UP000001134; Genome.
DR   GO; GO:0004843; F:cysteine-type deubiquitinase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   CDD; cd02674; Peptidase_C19R; 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; IPR018200; USP_CS.
DR   InterPro; IPR028889; USP_dom.
DR   PANTHER; PTHR21646; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE; 1.
DR   Pfam; PF00443; UCH; 1.
DR   SUPFAM; SSF54001; Cysteine proteinases; 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; Protease; Reference proteome; Thiol protease;
KW   Ubl conjugation pathway.
FT   CHAIN           1..468
FT                   /note="Probable ubiquitin carboxyl-terminal hydrolase R319"
FT                   /id="PRO_0000080700"
FT   DOMAIN          42..462
FT                   /note="USP"
FT   ACT_SITE        51
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10092,
FT                   ECO:0000255|PROSITE-ProRule:PRU10093"
FT   ACT_SITE        420
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10092,
FT                   ECO:0000255|PROSITE-ProRule:PRU10093"
SQ   SEQUENCE   468 AA;  54760 MW;  3BFE646E5BDF206A CRC64;
     MQNMMNTSQS FQNDSVLIGD KNTLQSINKS VDNGSKNTHG ITGIMNLGNT CYMNSALQAL
     SHNYLLINYL FMNKKQIIRT LLTNARKIFK DCDNFKIEST ISPIPLELRK KIQSENYHLS
     MLTVEDVNIL LNNTITAQII RLFECMWKNN CVVVPTSFRK VFGEVRDKFF FGYEQHDAEE
     AYSCIIQKMQ EELAEKRTIR FKTTRHSVGE YIKYMNDVKE KVSCLPNGKE KDIVMNKFKQ
     IKKQMPRESL TAESFREMKK YYEQGYSYIT EIFSGYVHSS ICCPNTSCGF TNDRFDAFTH
     LSLSIPVKNM YEQLNVYDCL REYFSQETLD ADNLWNCEGC HEKVQAIKKT KLWTTPYVLV
     IQFKRFGMTR IAKDNRFINY PMDELDVSSV ICSQQFEDSV QTKYKLQCVI NHHGGLNNGH
     YFTYSKIENT GEWYEFNDTY TGKVTDNHIV NQNAYILFYI RSDLFRSQ
//