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Database: UniProt
Entry: A0A317VEQ5_ASPEC
LinkDB: A0A317VEQ5_ASPEC
Original site: A0A317VEQ5_ASPEC 
ID   A0A317VEQ5_ASPEC        Unreviewed;       836 AA.
AC   A0A317VEQ5;
DT   10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT   10-OCT-2018, sequence version 1.
DT   27-MAR-2024, entry version 18.
DE   RecName: Full=Lysophospholipase {ECO:0000256|ARBA:ARBA00013274, ECO:0000256|RuleBase:RU362103};
DE            EC=3.1.1.5 {ECO:0000256|ARBA:ARBA00013274, ECO:0000256|RuleBase:RU362103};
GN   ORFNames=BO83DRAFT_378914 {ECO:0000313|EMBL:PWY71929.1};
OS   Aspergillus eucalypticola (strain CBS 122712 / IBT 29274).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX   NCBI_TaxID=1448314 {ECO:0000313|EMBL:PWY71929.1, ECO:0000313|Proteomes:UP000246171};
RN   [1] {ECO:0000313|EMBL:PWY71929.1, ECO:0000313|Proteomes:UP000246171}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 122712 {ECO:0000313|EMBL:PWY71929.1,
RC   ECO:0000313|Proteomes:UP000246171};
RG   DOE Joint Genome Institute;
RA   Vesth T.C., Nybo J., Theobald S., Brandl J., Frisvad J.C., Nielsen K.F.,
RA   Lyhne E.K., Kogle M.E., Kuo A., Riley R., Clum A., Nolan M., Lipzen A.,
RA   Salamov A., Henrissat B., Wiebenga A., De Vries R.P., Grigoriev I.V.,
RA   Mortensen U.H., Andersen M.R., Baker S.E.;
RT   "The genomes of Aspergillus section Nigri reveals drivers in fungal
RT   speciation.";
RL   Submitted (DEC-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the release of fatty acids from lysophospholipids.
CC       {ECO:0000256|ARBA:ARBA00002169}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a 1-acyl-sn-glycero-3-phosphocholine + H2O = a fatty acid +
CC         H(+) + sn-glycerol 3-phosphocholine; Xref=Rhea:RHEA:15177,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16870,
CC         ChEBI:CHEBI:28868, ChEBI:CHEBI:58168; EC=3.1.1.5;
CC         Evidence={ECO:0000256|ARBA:ARBA00000960,
CC         ECO:0000256|RuleBase:RU362103};
CC   -!- SIMILARITY: Belongs to the lysophospholipase family.
CC       {ECO:0000256|ARBA:ARBA00008780, ECO:0000256|RuleBase:RU362103}.
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:PWY71929.1}.
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DR   EMBL; MSFU01000014; PWY71929.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A317VEQ5; -.
DR   VEuPathDB; FungiDB:BO83DRAFT_378914; -.
DR   OrthoDB; 1997175at2759; -.
DR   Proteomes; UP000246171; Unassembled WGS sequence.
DR   GO; GO:0004622; F:lysophospholipase activity; IEA:UniProtKB-EC.
DR   GO; GO:0102545; F:phosphatidyl phospholipase B activity; IEA:UniProtKB-EC.
DR   GO; GO:0009395; P:phospholipid catabolic process; IEA:InterPro.
DR   CDD; cd00147; cPLA2_like; 1.
DR   Gene3D; 3.40.1090.10; Cytosolic phospholipase A2 catalytic domain; 1.
DR   InterPro; IPR016035; Acyl_Trfase/lysoPLipase.
DR   InterPro; IPR002642; LysoPLipase_cat_dom.
DR   PANTHER; PTHR10728; CYTOSOLIC PHOSPHOLIPASE A2; 1.
DR   PANTHER; PTHR10728:SF40; LYSOPHOSPHOLIPASE; 1.
DR   Pfam; PF01735; PLA2_B; 1.
DR   SMART; SM00022; PLAc; 1.
DR   SUPFAM; SSF52151; FabD/lysophospholipase-like; 1.
DR   PROSITE; PS51210; PLA2C; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000256|PROSITE-ProRule:PRU00555,
KW   ECO:0000256|RuleBase:RU362103};
KW   Lipid degradation {ECO:0000256|ARBA:ARBA00022963, ECO:0000256|PROSITE-
KW   ProRule:PRU00555};
KW   Lipid metabolism {ECO:0000256|PROSITE-ProRule:PRU00555,
KW   ECO:0000256|RuleBase:RU362103}.
FT   DOMAIN          159..700
FT                   /note="PLA2c"
FT                   /evidence="ECO:0000259|PROSITE:PS51210"
FT   REGION          50..84
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          616..664
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          677..699
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          724..763
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          817..836
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        50..72
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        623..664
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        725..740
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   836 AA;  92764 MW;  F7A9E7EC2DAF419B CRC64;
     MGAAKALRLR WTVPPTLLIA LGGGLLYTTS GRTQSNKQLL LQTGPKGFFS TSLNPGSDKR
     SDKSSGSSDW NPLGHGSKED PHHDAGSIWT NVLQKFEGVK QAVGTPDWIE LDNIKNYIIP
     DWTRLLPLSV QKLQRELSMA PGSLADDIWH EAHDPDINPE ILRKAKVRVG DTLCNEELAY
     RQKRQKYATA ALASYLDIPE DEIHPDDVPI IAMCGSGGGL RALVAGTGSY LATQEAGLWD
     CVTYTAGVSG SCWLQTLYHS SITGRNFNKM VDHLKNRLGV HLAFPPAALK LLTNAPTNKY
     LLSGLVEKLK GDPGADFGLV DIYGMLLAAR LLVPKGELGV CDRDLKLSNQ RYNLASGAHP
     LPIYTAVRHE IPVLENQENP EKREKPEDLI KESKNEAWFQ WFEFTPYEFF CEELSAGIPT
     WALGRHFHGG VNVKPEEISP IPELRVPALM GVWGSAFCAT LSHYYKEIRP VIKGITGLSG
     IDSLIQGKTK DLVRVHPIDP ATIPNYVLGM KDQLPPSCPE SIFRSRHLRL MDAGMSNNLP
     IYPLLRPGRD VDVIIAFDAS ADIKQENWLS VVDGYARQRG VKGWPIGAGW PREDEQLKQT
     EEMLRQAQNI SQKELANKMA EAQDKSKPNS PTTNQNTTSN NTTTTPPTSA QNKTKNHPST
     STDLDYCNIW VGTTQEMVSG QEPPPSKRLF HPQDTDHSES DFHLMRPDAG IAVVYFPLLP
     NPSAPELPTS SSLQKSRTPA RKSENTSKAR VSDPAKPLTP YPGTINPDVD DFLSTWNFVY
     TPEQIDSVVG LAKANFAQGE DQVKRVVRAV YERKKNDRLQ REERESRQRM EGFVPL
//
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