ID   K5VI98_PHACS            Unreviewed;       854 AA.
AC   K5VI98;
DT   09-JAN-2013, integrated into UniProtKB/TrEMBL.
DT   09-JAN-2013, sequence version 1.
DT   27-MAR-2024, entry version 35.
DE   RecName: Full=Phospholipase {ECO:0000256|PIRNR:PIRNR009376};
DE            EC=3.1.4.4 {ECO:0000256|PIRNR:PIRNR009376};
GN   ORFNames=PHACADRAFT_151417 {ECO:0000313|EMBL:EKM50988.1};
OS   Phanerochaete carnosa (strain HHB-10118-sp) (White-rot fungus) (Peniophora
OS   carnosa).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Polyporales; Phanerochaetaceae; Phanerochaete.
OX   NCBI_TaxID=650164 {ECO:0000313|EMBL:EKM50988.1, ECO:0000313|Proteomes:UP000008370};
RN   [1] {ECO:0000313|EMBL:EKM50988.1, ECO:0000313|Proteomes:UP000008370}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HHB-10118-sp {ECO:0000313|EMBL:EKM50988.1,
RC   ECO:0000313|Proteomes:UP000008370};
RX   PubMed=22937793; DOI=10.1186/1471-2164-13-444;
RA   Suzuki H., MacDonald J., Syed K., Salamov A., Hori C., Aerts A.,
RA   Henrissat B., Wiebenga A., vanKuyk P.A., Barry K., Lindquist E.,
RA   LaButti K., Lapidus A., Lucas S., Coutinho P., Gong Y., Samejima M.,
RA   Mahadevan R., Abou-Zaid M., de Vries R.P., Igarashi K., Yadav J.S.,
RA   Grigoriev I.V., Master E.R.;
RT   "Comparative genomics of the white-rot fungi, Phanerochaete carnosa and P.
RT   chrysosporium, to elucidate the genetic basis of the distinct wood types
RT   they colonize.";
RL   BMC Genomics 13:444-444(2012).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a 1,2-diacyl-sn-glycero-3-phosphocholine + H2O = a 1,2-diacyl-
CC         sn-glycero-3-phosphate + choline + H(+); Xref=Rhea:RHEA:14445,
CC         ChEBI:CHEBI:15354, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:57643, ChEBI:CHEBI:58608; EC=3.1.4.4;
CC         Evidence={ECO:0000256|PIRNR:PIRNR009376};
CC   -!- SIMILARITY: Belongs to the phospholipase D family.
CC       {ECO:0000256|PIRNR:PIRNR009376}.
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DR   EMBL; JH930477; EKM50988.1; -; Genomic_DNA.
DR   RefSeq; XP_007400151.1; XM_007400089.1.
DR   AlphaFoldDB; K5VI98; -.
DR   STRING; 650164.K5VI98; -.
DR   GeneID; 18908874; -.
DR   KEGG; pco:PHACADRAFT_151417; -.
DR   HOGENOM; CLU_000690_2_2_1; -.
DR   InParanoid; K5VI98; -.
DR   OrthoDB; 335467at2759; -.
DR   Proteomes; UP000008370; Unassembled WGS sequence.
DR   GO; GO:0070290; F:N-acylphosphatidylethanolamine-specific phospholipase D activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0004630; F:phospholipase D activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0035556; P:intracellular signal transduction; IEA:InterPro.
DR   GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0006654; P:phosphatidic acid biosynthetic process; IEA:InterPro.
DR   CDD; cd09138; PLDc_vPLD1_2_yPLD_like_1; 1.
DR   CDD; cd09141; PLDc_vPLD1_2_yPLD_like_2; 1.
DR   Gene3D; 3.30.870.10; Endonuclease Chain A; 3.
DR   InterPro; IPR025202; PLD-like_dom.
DR   InterPro; IPR001736; PLipase_D/transphosphatidylase.
DR   InterPro; IPR016555; PLipase_D_euk.
DR   InterPro; IPR015679; PLipase_D_fam.
DR   PANTHER; PTHR18896; PHOSPHOLIPASE D; 1.
DR   PANTHER; PTHR18896:SF186; PHOSPHOLIPASE D; 1.
DR   Pfam; PF00614; PLDc; 1.
DR   Pfam; PF13091; PLDc_2; 1.
DR   PIRSF; PIRSF009376; Phospholipase_D_euk; 2.
DR   SMART; SM00155; PLDc; 2.
DR   SUPFAM; SSF56024; Phospholipase D/nuclease; 2.
DR   PROSITE; PS50035; PLD; 2.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PIRNR:PIRNR009376};
KW   Lipid degradation {ECO:0000256|ARBA:ARBA00022963,
KW   ECO:0000256|PIRNR:PIRNR009376};
KW   Lipid metabolism {ECO:0000256|ARBA:ARBA00022963,
KW   ECO:0000256|PIRNR:PIRNR009376};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008370}.
FT   DOMAIN          182..209
FT                   /note="PLD phosphodiesterase"
FT                   /evidence="ECO:0000259|PROSITE:PS50035"
FT   DOMAIN          639..666
FT                   /note="PLD phosphodiesterase"
FT                   /evidence="ECO:0000259|PROSITE:PS50035"
SQ   SEQUENCE   854 AA;  98047 MW;  78FB7B7F17E95653 CRC64;
     MSSFLDKLAS EADKLVSKAE EGVSHARNTA IGLLNPNRRH DTPEEQRNDM IRAEINASHR
     FHSFADQRSH NSVKWHIDGH DYMYALSEML DSAREVIYIL DWWLTPELYL RRPPAYNEQW
     RLDRVLKRKA EQGVKIYVVV YKEVTQTMSM SSSHTKHALE ALHPNIACMR HPDHIGSKDD
     VEFWSHHEKV VVVDQHRACI GGLDLCFGRW DTHTHPLADA HPTHFDETLF PGQDYNNARV
     LDFKNVSQYA NNGLSIIDMP RMPWHDMHMT LCGPVVLDIV QHFVERWNEV KRRKYRNENR
     YDWLALPHNI EAAPEESVAR HPLRENWHSM GKRFKQRFNR QYGEWFPEEE EDPIAYQRPP
     NGTCRVQAVR SVSDWSHGVL TERSVQNAYC QLIAEANHFI YIENQFFISS TTTKDPVKNQ
     IANALVQRIV QAARDGQKFK VVVVIPEVPG FAGNIKDASS VQVIMAAQYR TINRGGHSIY
     EEIRRAGYEP MDYIRFYHLR AYDRINAPYP SFIKKMEEAS GVKFQQAMVA LARQWVGQSE
     DGAPQQQSVT IVLPDETLGS SASVEGNKNA LKSETYPLPQ SAAEAREIIE RFEHGADGLR
     SDEDVSDNVV QHMLSDKTNL LDEKWLGSEE EEKNAYVSEL LYIHSKVMIV DDRRVIMGSA
     NINDRSQKGD GDSEIALVVE DDDMIETYMD GQKYMAGRFA ASLRRQIYRE HLGLIPPQFC
     EGPREQVTSF MRPAPIPNRD EFGTPEDNAV ADPLSPHTEA LWNDTARTNR EIFTEIFRPV
     PTNLIRSWSA YGNYVSNGKT DHVVPDIPLA RVKDRLSQVR GALVECPLDF LIDEKEFTEG
     PIWSGFDPVL PLYI
//