ID A0A093YPW4_9PEZI Unreviewed; 1218 AA.
AC A0A093YPW4;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 39.
DE RecName: Full=phospholipase A2 {ECO:0000256|ARBA:ARBA00013278};
DE EC=3.1.1.4 {ECO:0000256|ARBA:ARBA00013278};
DE Flags: Fragment;
GN ORFNames=V492_07500 {ECO:0000313|EMBL:KFY07041.1};
OS Pseudogymnoascus sp. VKM F-4246.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Leotiomycetes incertae sedis; Pseudeurotiaceae; Pseudogymnoascus.
OX NCBI_TaxID=1420902 {ECO:0000313|EMBL:KFY07041.1, ECO:0000313|Proteomes:UP000029299};
RN [1] {ECO:0000313|EMBL:KFY07041.1, ECO:0000313|Proteomes:UP000029299}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VKM F-4246 {ECO:0000313|EMBL:KFY07041.1,
RC ECO:0000313|Proteomes:UP000029299};
RA Leushkin E.V., Logacheva M.D., Penin A.A., Sutormin R.A., Gerasimov E.S.,
RA Kochkina G.A., Ivanushkina N.E., Vasilenko O.V., Kondrashov A.S.,
RA Ozerskaya S.M.;
RT "Population genomics of a fungus Geomyces pannorum provides evidence of
RT horizontal gene transfer but not of sexual reproduction.";
RL Submitted (JUL-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1,2-diacyl-sn-glycero-3-phosphocholine + H2O = a 1-acyl-sn-
CC glycero-3-phosphocholine + a fatty acid + H(+); Xref=Rhea:RHEA:15801,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:28868,
CC ChEBI:CHEBI:57643, ChEBI:CHEBI:58168; EC=3.1.1.4;
CC Evidence={ECO:0000256|ARBA:ARBA00023422};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:15802;
CC Evidence={ECO:0000256|ARBA:ARBA00023422};
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KFY07041.1}.
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DR EMBL; JPJU01002656; KFY07041.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A093YPW4; -.
DR STRING; 1420902.A0A093YPW4; -.
DR HOGENOM; CLU_003496_0_0_1; -.
DR Proteomes; UP000029299; Unassembled WGS sequence.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0046486; P:glycerolipid metabolic process; IEA:UniProt.
DR GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-UniRule.
DR CDD; cd07216; Pat17_PNPLA8_PNPLA9_like3; 1.
DR Gene3D; 1.25.40.20; Ankyrin repeat-containing domain; 2.
DR Gene3D; 3.40.1090.10; Cytosolic phospholipase A2 catalytic domain; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR InterPro; IPR016035; Acyl_Trfase/lysoPLipase.
DR InterPro; IPR002110; Ankyrin_rpt.
DR InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR InterPro; IPR007111; NACHT_NTPase.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR002641; PNPLA_dom.
DR PANTHER; PTHR24185; CALCIUM-INDEPENDENT PHOSPHOLIPASE A2-GAMMA; 1.
DR PANTHER; PTHR24185:SF1; CALCIUM-INDEPENDENT PHOSPHOLIPASE A2-GAMMA; 1.
DR Pfam; PF12796; Ank_2; 3.
DR Pfam; PF01734; Patatin; 1.
DR PRINTS; PR01415; ANKYRIN.
DR SMART; SM00248; ANK; 9.
DR SUPFAM; SSF48403; Ankyrin repeat; 1.
DR SUPFAM; SSF52151; FabD/lysophospholipase-like; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR PROSITE; PS50297; ANK_REP_REGION; 5.
DR PROSITE; PS50088; ANK_REPEAT; 5.
DR PROSITE; PS50837; NACHT; 1.
DR PROSITE; PS51635; PNPLA; 1.
PE 4: Predicted;
KW ANK repeat {ECO:0000256|PROSITE-ProRule:PRU00023};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Lipid degradation {ECO:0000256|ARBA:ARBA00022963};
KW Lipid metabolism {ECO:0000256|ARBA:ARBA00023098};
KW Reference proteome {ECO:0000313|Proteomes:UP000029299}.
FT DOMAIN 1..192
FT /note="PNPLA"
FT /evidence="ECO:0000259|PROSITE:PS51635"
FT DOMAIN 387..511
FT /note="NACHT"
FT /evidence="ECO:0000259|PROSITE:PS50837"
FT REPEAT 878..910
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 945..977
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 1004..1036
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 1103..1135
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 1141..1168
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT NON_TER 1218
FT /evidence="ECO:0000313|EMBL:KFY07041.1"
SQ SEQUENCE 1218 AA; 134664 MW; 7EAB48C522EAD50F CRC64;
MRNINTQRKA DGKEPQEPWQ YFDLMGGTST GGIIAIMLGR LRMTTDECID AYTQLSKTIF
TPKHSRRSPA RPVNFVNGDE KFDSKAFEGE IKTQIKNSKV ANEDDQILLR DANSTCGVCV
VALHEENSAP AIFRTYDYTH ASHTLFDECK VWEACRATSA APTFFDPIQI GRFKQSFIDG
GLGFNNPIFQ VYQEAQNMWP DRTIIVTSIG TGEVPGAKFG GNLKKIAKSI KEMVTDCDKV
ANVFYKANKT MADEGHYFRF SVTHGLGDIG LEEYKNIPVI ASRTQTYLAT GEPEVKLRRC
VEALLQELEH GNSISLLNSD SVQAPSSSVT ADDSATIDDS DLLQCLESLK FEGMNFREGN
IVSADHDTCE WLLQDENYSR WIRDDNGILW IQGKAGAGKS TLMKYIYKRI EGPTADASSL
KLSFFFHARG TELQKSTLGM FKSLLLQLYK RDLTARREIK KEFDKASEDI MANLKLEWTE
DMVRELFSSV ICHISGSKKN ITIFVDALDE AGVAANTLAI YLVSLYDKVR QSNRAVKICF
SCRHYPIVSA KVTDDQKVIL ELKNEPGIRS FLKNEFKKSK VEEIDGELKD DIAKKANGLF
QWVCLVLPMI FDAYKTAKPP VYIQKMLHML PEGLNNMYQY ILRDLIHQEQ PAEILKLFRW
VYFAARPLSV QEIQHALAVV DKLPQCRVYN LKSSAEYVED RVETRITALS GGLVEVRAHG
SETILQFTHQ TVRDFLLEKG FEILAGSEYP ANKEKQQFEG SCHDILARSC INYLWAEDVQ
QHSTATDVKG SSSKRSWIQL PTSETLPLLQ YAVAALFWHA SKAEQYECCQ NKLLEQLDYK
YTSKFLKDHS LEEGIFSLWR SAGEIYCARE YFGVLPSAGS TLLHIASMAN IHSAVNILLK
KGAQVDEKDQ RGQQAIHYAA RGGATEVSRI LIKISRSVIN AEDNNSITPL QMAARHYRSN
TLRLLITKGA KIKYFKKTHP WKADKICFGI EKTIQLLIED AAELNAQSLQ SAAASGNLET
VQLLLAEGTD VNIQSGGYGS ALVAAAYNGH NAVADALLQK GAEINSQGGI YGCALVAAAT
SGLDEMVRIL LQAGAEIDAK GGEHPSALAA AIDRGHVRVI KILLGEGAKI NSQSGKFGNI
LAIAASKGHT DIVRILLAGG ANINAQGGEY GNALVAAICN GHIEMSMILL EGGANINAQG
GEHGNALVAA ICNGHIEM
//
