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Database: UniProt
Entry: C5FN51_ARTOC
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Original site: C5FN51_ARTOC 
ID   C5FN51_ARTOC            Unreviewed;       797 AA.
AC   C5FN51;
DT   28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT   28-JUL-2009, sequence version 1.
DT   27-MAR-2024, entry version 58.
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=MCYG_04106 {ECO:0000313|EMBL:EEQ31287.1};
OS   Arthroderma otae (strain ATCC MYA-4605 / CBS 113480) (Microsporum canis).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Arthrodermataceae; Microsporum.
OX   NCBI_TaxID=554155 {ECO:0000313|EMBL:EEQ31287.1, ECO:0000313|Proteomes:UP000002035};
RN   [1] {ECO:0000313|Proteomes:UP000002035}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC MYA-4605 / CBS 113480 {ECO:0000313|Proteomes:UP000002035};
RX   PubMed=22951933; DOI=10.1128/mbio.00259-12;
RA   Martinez D.A., Oliver B.G., Graeser Y., Goldberg J.M., Li W.,
RA   Martinez-Rossi N.M., Monod M., Shelest E., Barton R.C., Birch E.,
RA   Brakhage A.A., Chen Z., Gurr S.J., Heiman D., Heitman J., Kosti I.,
RA   Rossi A., Saif S., Samalova M., Saunders C.W., Shea T., Summerbell R.C.,
RA   Xu J., Young S., Zeng Q., Birren B.W., Cuomo C.A., White T.C.;
RT   "Comparative genome analysis of Trichophyton rubrum and related
RT   dermatophytes reveals candidate genes involved in infection.";
RL   MBio 3:E259-E259(2012).
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}.
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DR   EMBL; DS995704; EEQ31287.1; -; Genomic_DNA.
DR   RefSeq; XP_002846369.1; XM_002846323.1.
DR   AlphaFoldDB; C5FN51; -.
DR   STRING; 554155.C5FN51; -.
DR   GeneID; 9224438; -.
DR   VEuPathDB; FungiDB:MCYG_04106; -.
DR   eggNOG; KOG1325; Eukaryota.
DR   HOGENOM; CLU_013227_1_0_1; -.
DR   OMA; WALGRRF; -.
DR   OrthoDB; 1997175at2759; -.
DR   Proteomes; UP000002035; 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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002035}.
FT   DOMAIN          174..797
FT                   /note="PLA2c"
FT                   /evidence="ECO:0000259|PROSITE:PS51210"
FT   REGION          616..646
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          663..683
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        616..644
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        663..677
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   797 AA;  87137 MW;  587D509C27940322 CRC64;
     MAGGQKAGDV NSQAVMAASE FLQARWRQAL KGALFVTGSA SLALLGKQSV RCDAGRSAAA
     WNAKKTPQTA EESALDKLIK NSINNAGEKE EKKADEDAMS AWETMTDRLG TAEGYFSSSD
     WSADWSAVFK DYISPGWTFF SPEILRNLQR ELSMAPGSVA DDVWKEACDP SFNPSIVEEA
     NVRIGDTLCP EEESFLADRR KVVARNLASY LGLPEDQVHP DDVPVIAMCA SGGGLRALIA
     GTGSYMAAKE AGLWDCLTYT AGVSGSCWLQ TLFNSSIGGQ DFGKMINHLK ARLHTHIAFP
     PEALDILTTS PTNKYLLRGV IEKLKGDPKA DFGLVDVYGI LLAARLMVPQ DTAALTDSDL
     QLSSQRAVVK GGANPMPIYT AVRHEIPKPS QMDASEDELE EISRRESWFQ WFEFTPYELF
     CEEFAAGIPT WAVGRNFMNG KGVAAPHGYA VPELRVPALM GVWGSAFCAT LAHYYKEIRP
     AFMGLAGFSS IDALIEGKSE DLTRVHPIDP ATVPNFVLGL EGKLPDSCPA SVFQDSHLRL
     MDAGMSNNLP IYPLLRPGRN VDLIVAFDVS ADSKEANWLS VVDGYAHQRG IKGWPIGAGW
     PKSNATPQET ADIIAEESQT TKEEADRKVA SAQEASKART RDSSGNDPDL TFCNIWLGTT
     EESISSAESP PSKRLFHAST TNEEESEYHL TQPHAGIAVA YFPLLPNPAC LALPNPDKDE
     KDGERKILNP LEEDYLSTWN FIYTAEQIDS AVHLAKSNFA EGEDQLKRVV RGIYERKKRE
     RLQREMDGAR VSASYLA
//
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