ID   VF232_IIV3              Reviewed;         844 AA.
AC   Q196X6;
DT   16-JUN-2009, integrated into UniProtKB/Swiss-Prot.
DT   11-JUL-2006, sequence version 1.
DT   03-AUG-2022, entry version 53.
DE   RecName: Full=Putative ubiquitin thioesterase 232R;
DE            EC=3.4.19.12 {ECO:0000250|UniProtKB:Q5VVQ6};
GN   ORFNames=IIV3-084L;
OS   Invertebrate iridescent virus 3 (IIV-3) (Mosquito iridescent virus).
OC   Viruses; Varidnaviria; Bamfordvirae; Nucleocytoviricota; Megaviricetes;
OC   Pimascovirales; Iridoviridae; Betairidovirinae; Chloriridovirus.
OX   NCBI_TaxID=345201;
OH   NCBI_TaxID=7163; Aedes vexans (Inland floodwater mosquito) (Culex vexans).
OH   NCBI_TaxID=42431; Culex territans.
OH   NCBI_TaxID=332058; Culiseta annulata.
OH   NCBI_TaxID=310513; Ochlerotatus sollicitans (eastern saltmarsh mosquito).
OH   NCBI_TaxID=329105; Ochlerotatus taeniorhynchus (Black salt marsh mosquito) (Aedes taeniorhynchus).
OH   NCBI_TaxID=7183; Psorophora ferox.
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16912294; DOI=10.1128/jvi.00464-06;
RA   Delhon G., Tulman E.R., Afonso C.L., Lu Z., Becnel J.J., Moser B.A.,
RA   Kutish G.F., Rock D.L.;
RT   "Genome of invertebrate iridescent virus type 3 (mosquito iridescent
RT   virus).";
RL   J. Virol. 80:8439-8449(2006).
CC   -!- FUNCTION: Hydrolase that can remove conjugated ubiquitin from proteins
CC       and may therefore play an important regulatory role at the level of
CC       protein turnover by preventing degradation. {ECO:0000250}.
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:0000250|UniProtKB:Q5VVQ6};
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DR   EMBL; DQ643392; ABF82114.1; -; Genomic_DNA.
DR   RefSeq; YP_654656.1; NC_008187.1.
DR   GeneID; 4156295; -.
DR   KEGG; vg:4156295; -.
DR   Proteomes; UP000001358; Genome.
DR   GO; GO:0004843; F:cysteine-type deubiquitinase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006353; P:DNA-templated transcription, termination; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   InterPro; IPR003323; OTU_dom.
DR   InterPro; IPR038765; Papain-like_cys_pep_sf.
DR   InterPro; IPR011112; Rho_N.
DR   Pfam; PF02338; OTU; 1.
DR   Pfam; PF07498; Rho_N; 1.
DR   SMART; SM00959; Rho_N; 3.
DR   SUPFAM; SSF54001; SSF54001; 1.
DR   PROSITE; PS50802; OTU; 1.
PE   3: Inferred from homology;
KW   Hydrolase; Protease; Reference proteome; Thiol protease;
KW   Ubl conjugation pathway.
FT   CHAIN           1..844
FT                   /note="Putative ubiquitin thioesterase 232R"
FT                   /id="PRO_0000377773"
FT   DOMAIN          590..725
FT                   /note="OTU"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00139"
FT   REGION          136..223
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          261..287
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          326..377
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          422..541
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        136..152
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        159..222
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        342..356
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        458..485
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        504..523
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        598
FT                   /evidence="ECO:0000250|UniProtKB:Q96FW1"
FT   ACT_SITE        601
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250|UniProtKB:Q5VVQ6"
FT   ACT_SITE        718
FT                   /evidence="ECO:0000250|UniProtKB:Q5VVQ6"
SQ   SEQUENCE   844 AA;  93521 MW;  6E24E9C3EE3C5872 CRC64;
     MCDVDLKTCQ KSSKFKKKDI VELGKQCGVN PYLSNGKEKS RTVICTEIVA SYNPPPGSSQ
     GDDSEHESIS QVNNIPNRNE KFLPKSKYPT YTQVLNMEKR QLKALAKKLG LEYKKQTEQQ
     LQGAINLKIK TLEGLNSSTR SRSPSVRSRC RSPSPRAPSV RSRLPSTRSR CRSPSPRAPS
     TRSRSPSVRS RCRSPSPRAP SVRSRSPSRQ SVRQSSESAD EAEQVALETM KTAHLRMLAT
     TLGASTVTGM KKKDLIDYIK SRRKSPSPSP VPPSTRCDPT TTAPPMEDLF KKKVDELKTM
     AKNAGFVRWN GKTLSKMNKS DLVDFLLNGM NRPSPSLPQS RSRTRSPPPP PRSRSPSVGS
     PSVRDGGAGR RRLPELTRAQ LTAMKVVDLK AMATELGLTR YRGMNRTQMR KGDVINFIIE
     TQKKQKTPSP SPTPPSPVPS VVGSRRPKSP LPYKSRDFVA LADDDSEPGV EVQKKMGKSG
     EREPKSVPNV RIIPSEIPAP TEGSLRSRLS TQQQTQQSVV YEDPNESIKP EESVRAPKLS
     VVDPQLSRKT LKPLPSLVVT DQPSKQPELP KYKGRTPYTD LEQLAQSKGY TVKQVSGDGN
     CLFRSVCKSI RALRGEKFTH RQLRQMVVDY LRENPEFLQV YLEYVARQRD NSLPSTEQYL
     SEMSKCGTWG DLICLKTLSE ILKVQFNLLI LNTKQFQMVS SQDDYPDVIP LGYIDNYHYT
     SLVPIGLDSK GGAASSTTTG LKQLDGPRPP ITLIPESQVP AVAATISTQQ PPSIVAPPIS
     VGGSQLVPSI VPQPQMPKPD FKPVKPLSNL NELLDLMDRV KPQVYNDISQ LEKARQSIKV
     SLGL