ID   A0A2I1GNI8_9GLOM        Unreviewed;       653 AA.
AC   A0A2I1GNI8;
DT   28-FEB-2018, integrated into UniProtKB/TrEMBL.
DT   28-FEB-2018, sequence version 1.
DT   27-MAR-2024, entry version 20.
DE   RecName: Full=Lysophospholipase {ECO:0000256|RuleBase:RU362103};
DE            EC=3.1.1.5 {ECO:0000256|RuleBase:RU362103};
GN   ORFNames=RhiirA4_524592 {ECO:0000313|EMBL:PKY48202.1};
OS   Rhizophagus irregularis.
OC   Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Glomeromycotina;
OC   Glomeromycetes; Glomerales; Glomeraceae; Rhizophagus.
OX   NCBI_TaxID=588596 {ECO:0000313|EMBL:PKY48202.1, ECO:0000313|Proteomes:UP000234323};
RN   [1] {ECO:0000313|EMBL:PKY48202.1, ECO:0000313|Proteomes:UP000234323}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=A4 {ECO:0000313|EMBL:PKY48202.1,
RC   ECO:0000313|Proteomes:UP000234323};
RA   Ropars J., Sedzielewska K., Noel J., Charron P., Farinelli L., Marton T.,
RA   Kruger M., Pelin A., Brachmann A., Corradi N.;
RT   "Genome analyses suggest a sexual origin of heterokaryosis in a supposedly
RT   ancient asexual fungus.";
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
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|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:PKY48202.1}.
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DR   EMBL; LLXI01000615; PKY48202.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2I1GNI8; -.
DR   VEuPathDB; FungiDB:FUN_022410; -.
DR   VEuPathDB; FungiDB:GLOIN_2v1773407; -.
DR   VEuPathDB; FungiDB:RhiirA1_414460; -.
DR   OrthoDB; 1997175at2759; -.
DR   Proteomes; UP000234323; 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   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|PROSITE-ProRule:PRU00555,
KW   ECO:0000256|RuleBase:RU362103};
KW   Lipid metabolism {ECO:0000256|PROSITE-ProRule:PRU00555,
KW   ECO:0000256|RuleBase:RU362103};
KW   Reference proteome {ECO:0000313|Proteomes:UP000234323}.
FT   DOMAIN          114..653
FT                   /note="PLA2c"
FT                   /evidence="ECO:0000259|PROSITE:PS51210"
FT   REGION          1..29
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..20
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   653 AA;  74398 MW;  D7F830F4AD6FB1B5 CRC64;
     MDESIESGLK KPENDDVAKV QTTEMTKTTE TTKVVKDEDD GITKDKTLVT ETTTTTTEKT
     ESGTTFYTQI KSKFEQVFHE FIPESLQNNR KVVHAFDNLR ENVLKKTNDK SVNPEIEWDA
     EVRKSNELCE DEKKFLKERK EFIKEAFAKY VGVGIEEIHV DDIPVIAFAG SGGGFRAMIA
     TTAYMRALQD SGLYDCGIYF SGLSGSCWNL ATQYSSICAT KENPVQALLD FFKENLTHNI
     ASPKGLLKAL SNNSSPETAV ELVFGGLVEK KAEGLDLHVV DVYGSLLGAR ILVGHDPESQ
     RLDFKLSQQR RFIEGGKQMM PIYTAIHHNR PWKDLLDEKT SAFVENYEQV WTEYSKKKDH
     MAWYEFTPFE VGCDEQAAWV PTWALGRKFE FGKNVNRLPE INLCQLIGIM GAAPSAPIYI
     DVRQFEHFLP EGWLKTEWKR LYEGAMEDLG EEGRWKFEGH HLVPTAEVYN HIYHLNPPPY
     ELGLVNNQIL ELIDAGASND LPLYPLVHPS REVDIIIGFD CSSQIINHDF FEQEQSVFTS
     RKGITKVARD VENKYCEVYD YVPNGKSDGY TTPAVYHSTF CYLPYLPNDK VDKTFVPSTA
     KFASFANFTY TPDQIDLMVR LAKQNWLEVE EKVKGVVIDA WKKKRDKRLS NSK
//