ID   VL96_IRV1               Reviewed;         867 AA.
AC   P22856;
DT   01-AUG-1991, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1991, sequence version 1.
DT   27-MAR-2024, entry version 71.
DE   RecName: Full=Putative ubiquitin thioesterase L96;
DE            EC=3.4.19.12 {ECO:0000250|UniProtKB:Q5VVQ6};
GN   ORFNames=L96;
OS   Tipula iridescent virus (TIV) (Insect iridescent virus type 1).
OC   Viruses; Varidnaviria; Bamfordvirae; Nucleocytoviricota; Megaviricetes;
OC   Pimascovirales; Iridoviridae; Betairidovirinae; Iridovirus;
OC   Invertebrate iridescent virus 1.
OX   NCBI_TaxID=10490;
OH   NCBI_TaxID=41043; Tipula.
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RX   PubMed=1701750; DOI=10.1016/0378-1119(90)90394-7;
RA   Home W.A., Tajbakhsh S., Seligy V.L.;
RT   "Molecular cloning and characterization of a late Tipula iridescent virus
RT   gene.";
RL   Gene 94:243-248(1990).
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 (By similarity). May be
CC       involved in TIV genomic DNA packaging in a manner related to the Gag
CC       polyproteins of the mammalian viruses. {ECO:0000250,
CC       ECO:0000269|PubMed:1701750}.
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; M62953; AAA47919.1; -; Genomic_DNA.
DR   PIR; JH0225; JH0225.
DR   SMR; P22856; -.
DR   GO; GO:0004843; F:cysteine-type deubiquitinase activity; IEA:UniProtKB-EC.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0006353; P:DNA-templated transcription termination; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   CDD; cd22758; OTU_232R-like; 1.
DR   Gene3D; 3.90.70.80; -; 1.
DR   InterPro; IPR003323; OTU_dom.
DR   InterPro; IPR038765; Papain-like_cys_pep_sf.
DR   InterPro; IPR011112; Rho_N.
DR   PANTHER; PTHR12419; OTU DOMAIN CONTAINING PROTEIN; 1.
DR   PANTHER; PTHR12419:SF11; OTU DOMAIN-CONTAINING PROTEIN DDB_G0284757; 1.
DR   Pfam; PF02338; OTU; 1.
DR   PRINTS; PR01217; PRICHEXTENSN.
DR   SMART; SM00959; Rho_N; 3.
DR   SUPFAM; SSF54001; Cysteine proteinases; 1.
DR   PROSITE; PS50802; OTU; 1.
PE   3: Inferred from homology;
KW   DNA-binding; Hydrolase; Protease; Repeat; Thiol protease;
KW   Ubl conjugation pathway; Viral genome packaging;
KW   Viral release from host cell.
FT   CHAIN           1..867
FT                   /note="Putative ubiquitin thioesterase L96"
FT                   /id="PRO_0000222389"
FT   DOMAIN          606..745
FT                   /note="OTU"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00139"
FT   REGION          49..73
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          177..204
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          231..271
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          379..591
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        177..200
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        243..263
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        379..397
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        399..423
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        435..455
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        459..473
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        475..547
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        548..563
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        614
FT                   /evidence="ECO:0000250|UniProtKB:Q96FW1"
FT   ACT_SITE        617
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250|UniProtKB:Q5VVQ6"
FT   ACT_SITE        738
FT                   /evidence="ECO:0000250|UniProtKB:Q5VVQ6"
SQ   SEQUENCE   867 AA;  96012 MW;  F19DBDE8FE5CA103 CRC64;
     MCDIDLKTCE KSSKYKKKDI VDLGKKCGVD PYLPNGREKT RQVICTEIVN QYSTNPPSSS
     SESDDDEDMG KQDQDPICGI SEKECNKLDN VNLLALGEYC GVDIYTPEGN LKTSKTICKS
     VSLKQSSPKA QKSPNKNDLI NMDPANLKKL AKKLDIDWKK KDIKELQYLI AKKLNSIKSV
     SPSRSPSPRR SRSPSPNIQN MKKKELKALA KALGASDKKL DKMDKNQLIE YILSRKKSPS
     PVRKSRSPSL RQRSRSPGRS RSNSPVRPKY RAADLLGKKV VELKELAKME GLKKWKDKTP
     SKMLKQDLVD FLLHVGGGGQ LPKTPSPVKP SASPKTRAEL ALLKVPELKA MALSYGLKNF
     KDKTPSQLRK NDFIDFIILS TQKSQSPPPS IRSKPRSSSP KYKTKDLVTT DESDGEIVVK
     KITRKPKSPR RSPPASVRRS RTPSVPKSPS ARPRSKSPSV RAEITDDEGE TPPSSVRPKS
     PSVRPKSPSV RPRSKSPSVR PKSPSARPRS KSPSVRSKSP SVRPKSPSVR PKSPSVRPRS
     KSPSVRPKSP SVRPPPPDPS NSPSITVDPS VTPPSSVKIK KRPELPEYKG GNADRDLEIL
     ARRRGYKVIP VKGDGNCLFR AVGKSLRLNQ NIKYSHEDLR AQVVTYLTSH KEFLEPYLEY
     VTESGDTTPQ EYAKNVERYI KNISKPGTWG DFICLRVLSE ILKVKFNLLI LNTRNFQVIS
     NNDTFKPLIP LGFIDDYHYT ALTPLYAEPI AVLENETPTP SIAPSIRPPP SIIPSIAPSV
     RPSIAPSVRP SIVPATPSIV PSLKPSVVPK LTPSIAPKIP PPVFGPVKPL SSTRELLEEA
     DKVHPYVRED ISQLARAEEQ ILVSLGM
//