UBPL1_MIMIV
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 03-AUG-2022, entry version 71.
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; Mimivirus.
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 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 GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IEA:InterPro.
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 Pfam; PF00443; UCH; 1.
DR SUPFAM; SSF54001; SSF54001; 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