ID   463L_IIV6               Reviewed;         290 AA.
AC   Q91F63;
DT   16-JUN-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   23-FEB-2022, entry version 65.
DE   RecName: Full=Probable lipid hydrolase 463L;
DE            EC=3.1.1.-;
GN   ORFNames=IIV6-463L;
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: Probable lipid hydrolase. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane
CC       protein {ECO:0000305}.
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DR   EMBL; AF303741; AAK82323.1; -; Genomic_DNA.
DR   RefSeq; NP_149926.1; NC_003038.1.
DR   SMR; Q91F63; -.
DR   GeneID; 1733292; -.
DR   KEGG; vg:1733292; -.
DR   Proteomes; UP000001359; Genome.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-KW.
DR   InterPro; IPR016035; Acyl_Trfase/lysoPLipase.
DR   InterPro; IPR002641; PNPLA_dom.
DR   Pfam; PF01734; Patatin; 1.
DR   SUPFAM; SSF52151; SSF52151; 1.
DR   PROSITE; PS51635; PNPLA; 1.
PE   3: Inferred from homology;
KW   Hydrolase; Lipid degradation; Lipid metabolism; Membrane;
KW   Reference proteome; Transmembrane; Transmembrane helix.
FT   CHAIN           1..290
FT                   /note="Probable lipid hydrolase 463L"
FT                   /id="PRO_0000377511"
FT   TRANSMEM        26..46
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        53..73
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          27..207
FT                   /note="PNPLA"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT   MOTIF           58..62
FT                   /note="GXSXG"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT   MOTIF           194..196
FT                   /note="DGA/G"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT   ACT_SITE        60
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT   ACT_SITE        194
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
SQ   SEQUENCE   290 AA;  33407 MW;  41A971D6FD060B5A CRC64;
     MNHFVYLMDK YGNPYSFSLK PKYYKTLVLS GGAMRGVYLL GALNGLKIKI NKISTFIGIS
     SGSIICFLLS IGYTPYEIFI SLLKYDNLLT INLDKLYSGD TRNEGGLFSS ENIFKHLETQ
     MRLKEISRSI TFKEHFEKTG KILIVMAFNI TKCKEDIFTY ETTPDMEILN SLKLSARIPI
     IFGPIKYNNN FYIDGGVWNN FPIDIAIKYH NKKNKKKSDW IIAVTTLFST YKQNIHQWYK
     FSNINIVMVN DTPDLNPSLV SSDLEKLTMF NKGEEKASLI KKQNIRRNSI