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Database: UniProt
Entry: G3GNP3_9PHYC
LinkDB: G3GNP3_9PHYC
Original site: G3GNP3_9PHYC 
ID   G3GNP3_9PHYC            Unreviewed;       243 AA.
AC   G3GNP3;
DT   16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT   16-NOV-2011, sequence version 1.
DT   27-MAR-2024, entry version 36.
DE   RecName: Full=Phosphatidic acid phosphatase type 2/haloperoxidase domain-containing protein {ECO:0000259|SMART:SM00014};
GN   ORFNames=ENVG_00196 {ECO:0000313|EMBL:AEO97891.1};
OS   Emiliania huxleyi virus 84.
OC   Viruses; Varidnaviria; Bamfordvirae; Nucleocytoviricota; Megaviricetes;
OC   Algavirales; Phycodnaviridae; Coccolithovirus.
OX   NCBI_TaxID=181216 {ECO:0000313|EMBL:AEO97891.1, ECO:0000313|Proteomes:UP000249003};
RN   [1] {ECO:0000313|EMBL:AEO97891.1, ECO:0000313|Proteomes:UP000249003}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=84 {ECO:0000313|EMBL:AEO97891.1,
RC   ECO:0000313|Proteomes:UP000249003};
RG   The Broad Institute Genome Sequencing Platform;
RA   Henn M.R., Allen M., Levin J., Malboeuf C., Casali M., Russ C., Lennon N.,
RA   Chapman S.B., Erlich R., Young S.K., Yandava C., Zeng Q., Alvarado L.,
RA   Anderson S., Berlin A., Chen Z., Freedman E., Gellesch M., Goldberg J.,
RA   Green L., Griggs A., Gujja S., Heilman E.R., Heiman D., Hollinger A.,
RA   Howarth C., Larson L., Mehta T., Pearson M., Roberts A., Ryan E., Saif S.,
RA   Shea T., Shenoy N., Sisk P., Stolte C., Sykes S., White J., Haas B.,
RA   Nusbaum C., Birren B.;
RT   "The Genome Sequence of Emiliania huxleyi virus 84.";
RL   Submitted (NOV-2010) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the PA-phosphatase related phosphoesterase
CC       family. {ECO:0000256|ARBA:ARBA00008816}.
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DR   EMBL; JF974290; AEO97891.1; -; Genomic_DNA.
DR   Proteomes; UP000249003; Genome.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0006644; P:phospholipid metabolic process; IEA:InterPro.
DR   Gene3D; 1.20.144.10; Phosphatidic acid phosphatase type 2/haloperoxidase; 1.
DR   InterPro; IPR036938; P_Acid_Pase_2/haloperoxi_sf.
DR   InterPro; IPR000326; P_Acid_Pase_2/haloperoxidase.
DR   InterPro; IPR043216; PA_PP_rel.
DR   PANTHER; PTHR10165; LIPID PHOSPHATE PHOSPHATASE; 1.
DR   PANTHER; PTHR10165:SF35; RE23632P; 1.
DR   Pfam; PF01569; PAP2; 1.
DR   SMART; SM00014; acidPPc; 1.
DR   SUPFAM; SSF48317; Acid phosphatase/Vanadium-dependent haloperoxidase; 1.
DR   PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE   3: Inferred from homology;
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        12..33
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        70..92
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        104..125
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        156..174
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        195..213
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        225..242
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          107..240
FT                   /note="Phosphatidic acid phosphatase type 2/haloperoxidase"
FT                   /evidence="ECO:0000259|SMART:SM00014"
SQ   SEQUENCE   243 AA;  27517 MW;  E17E0B3F08262ABA CRC64;
     MVLNIIRMFL QCEYVMPMIY VIMMACIPLT FIINEEMVPY QTITINGETH LIKDFRYDHP
     LIEETVTTSL LAVINSFGTF VIIAVTWFGA YAELYKWKSA VHTLVAYGLA YMIQDFIVAF
     GNDYIGAFRP NFYDGCGWDN DLGICTVNFE KGRRSFQSGH SSSAAVVFVY LILSMNDIRT
     VLRAQNNVPI IIDKLLFLVT LLSAFVFLFV GASRIHDFWH HPPDVIAGFL IGGLSACACR
     YTL
//
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