ID   VF232_IIV6              Reviewed;         671 AA.
AC   Q91FU0;
DT   16-JUN-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   03-AUG-2022, entry version 72.
DE   RecName: Full=Putative ubiquitin thioesterase 232R;
DE            EC=3.4.19.12 {ECO:0000250|UniProtKB:Q5VVQ6};
GN   ORFNames=IIV6-232R;
OS   Invertebrate iridescent virus 6 (IIV-6) (Chilo iridescent virus).
OC   Viruses; Varidnaviria; Bamfordvirae; Nucleocytoviricota; Megaviricetes;
OC   Pimascovirales; Iridoviridae; Betairidovirinae; Iridovirus.
OX   NCBI_TaxID=176652;
OH   NCBI_TaxID=6997; Acheta domesticus (House cricket).
OH   NCBI_TaxID=168631; Chilo suppressalis (Asiatic rice borer moth).
OH   NCBI_TaxID=6999; Gryllus bimaculatus (Two-spotted cricket).
OH   NCBI_TaxID=58607; Gryllus campestris.
OH   NCBI_TaxID=7108; Spodoptera frugiperda (Fall armyworm).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=11448171; DOI=10.1006/viro.2001.0963;
RA   Jakob N.J., Mueller K., Bahr U., Darai G.;
RT   "Analysis of the first complete DNA sequence of an invertebrate iridovirus:
RT   coding strategy of the genome of Chilo iridescent virus.";
RL   Virology 286:182-196(2001).
RN   [2]
RP   GENOME REANNOTATION.
RX   PubMed=17239238; DOI=10.1186/1743-422x-4-11;
RA   Eaton H.E., Metcalf J., Penny E., Tcherepanov V., Upton C., Brunetti C.R.;
RT   "Comparative genomic analysis of the family Iridoviridae: re-annotating and
RT   defining the core set of iridovirus genes.";
RL   Virol. J. 4:11-11(2007).
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; AF303741; AAK82093.1; -; Genomic_DNA.
DR   RefSeq; NP_149695.1; NC_003038.1.
DR   SMR; Q91FU0; -.
DR   GeneID; 1733388; -.
DR   KEGG; vg:1733388; -.
DR   Proteomes; UP000001359; 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; IPR014901; 2-cysteine_adaptor.
DR   InterPro; IPR003323; OTU_dom.
DR   InterPro; IPR038765; Papain-like_cys_pep_sf.
DR   InterPro; IPR011112; Rho_N.
DR   Pfam; PF08793; 2C_adapt; 1.
DR   Pfam; PF02338; OTU; 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..671
FT                   /note="Putative ubiquitin thioesterase 232R"
FT                   /id="PRO_0000377774"
FT   DOMAIN          392..521
FT                   /note="OTU"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00139"
FT   REGION          36..62
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          100..123
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          171..203
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          250..319
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          589..625
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        105..119
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        178..198
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        250..274
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        275..314
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        400
FT                   /evidence="ECO:0000250|UniProtKB:Q96FW1"
FT   ACT_SITE        403
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250|UniProtKB:Q5VVQ6"
FT   ACT_SITE        514
FT                   /evidence="ECO:0000250|UniProtKB:Q5VVQ6"
SQ   SEQUENCE   671 AA;  75605 MW;  1FD36D7AC7D67CCA CRC64;
     MNNNQCMRKK LDELRNIARS YNISITGKKK QQLCDEIIDY QKNNPPRRSP SPRRSPSPRR
     ISPECEQWLA NKGINPRTGK AIKIGGPTYK KLEMECKEAS PKIPSPVRQP SPVHSPVRSP
     VRQPSPVRFV EKTKGALNKM KKDQLIDFAQ SLGLNPGKLL KPALVDLIFV NQKPPRRSPS
     PRRSPSPRRS PSPRRSPSPR PVFVEKTKGA LNKMKKDQLI DLAQSLGLNP GKLLKPALVD
     LIFVNQKPVE PIRASSSSRS SRSTRRSSST KPSRRSSSRS RRSSSRSRRS SSRSRRSSSR
     SRRSSRRSTS RSRSLSKRSI RNISTVGDLE DLVASNLPIA IPESLSRSLS PSRTDFHEAE
     IELGSDFDLN NLPENRIAEL KQLNVLAKQN GFRMINVPLD GNCMFSVIGR AFNTSSSVIR
     QHTVDYLRRC KGSFDHIPAN IDDPTINWND YIDRLEEDAC WGDNTALFAA SLALNFQAHI
     LQVAGGDEGS WIRFGVNETN MGRIVNMGYL DNFHYIALEP FSGRLDILSI PSTHSKCPPP
     EISNRRDEEI RRDEEVEDEV IGERIVREAE VIERELRQEE ELTSIVSTKR SLRPSIPPKI
     STEHRRTPKL RPSVPRPSSI RQSQPNVAAL ARLETLTKIK DIIDALQRPL ENKLSTLTNT
     EKAIMQCIGV A