ID M2QVJ5_CERS8 Unreviewed; 850 AA.
AC M2QVJ5;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 36.
DE RecName: Full=Phospholipase {ECO:0000256|PIRNR:PIRNR009376};
DE EC=3.1.4.4 {ECO:0000256|PIRNR:PIRNR009376};
GN ORFNames=CERSUDRAFT_116030 {ECO:0000313|EMBL:EMD36120.1};
OS Ceriporiopsis subvermispora (strain B) (White-rot fungus) (Gelatoporia
OS subvermispora).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Polyporales; Gelatoporiaceae; Gelatoporia.
OX NCBI_TaxID=914234 {ECO:0000313|EMBL:EMD36120.1, ECO:0000313|Proteomes:UP000016930};
RN [1] {ECO:0000313|EMBL:EMD36120.1, ECO:0000313|Proteomes:UP000016930}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B {ECO:0000313|EMBL:EMD36120.1,
RC ECO:0000313|Proteomes:UP000016930};
RX PubMed=22434909; DOI=10.1073/pnas.1119912109;
RA Fernandez-Fueyo E., Ruiz-Duenas F.J., Ferreira P., Floudas D.,
RA Hibbett D.S., Canessa P., Larrondo L.F., James T.Y., Seelenfreund D.,
RA Lobos S., Polanco R., Tello M., Honda Y., Watanabe T., Watanabe T.,
RA Ryu J.S., Kubicek C.P., Schmoll M., Gaskell J., Hammel K.E., St John F.J.,
RA Vanden Wymelenberg A., Sabat G., Splinter BonDurant S., Syed K.,
RA Yadav J.S., Doddapaneni H., Subramanian V., Lavin J.L., Oguiza J.A.,
RA Perez G., Pisabarro A.G., Ramirez L., Santoyo F., Master E., Coutinho P.M.,
RA Henrissat B., Lombard V., Magnuson J.K., Kuees U., Hori C., Igarashi K.,
RA Samejima M., Held B.W., Barry K.W., LaButti K.M., Lapidus A.,
RA Lindquist E.A., Lucas S.M., Riley R., Salamov A.A., Hoffmeister D.,
RA Schwenk D., Hadar Y., Yarden O., de Vries R.P., Wiebenga A., Stenlid J.,
RA Eastwood D., Grigoriev I.V., Berka R.M., Blanchette R.A., Kersten P.,
RA Martinez A.T., Vicuna R., Cullen D.;
RT "Comparative genomics of Ceriporiopsis subvermispora and Phanerochaete
RT chrysosporium provide insight into selective ligninolysis.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:5458-5463(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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; KB445799; EMD36120.1; -; Genomic_DNA.
DR AlphaFoldDB; M2QVJ5; -.
DR STRING; 914234.M2QVJ5; -.
DR HOGENOM; CLU_000690_2_2_1; -.
DR OrthoDB; 335467at2759; -.
DR Proteomes; UP000016930; 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:UP000016930}.
FT DOMAIN 178..205
FT /note="PLD phosphodiesterase"
FT /evidence="ECO:0000259|PROSITE:PS50035"
FT DOMAIN 636..663
FT /note="PLD phosphodiesterase"
FT /evidence="ECO:0000259|PROSITE:PS50035"
SQ SEQUENCE 850 AA; 98056 MW; 191FEF0423FB48C3 CRC64;
MASFFHKVEQ MAEKIPDGLG HARDMVIGIL EPNRRHDDPD EKLADEIRAE INASHRFNSF
AAERGQCAVK WHVDGHDYMY AVSELLENAR EAIFILDWWL TPELYLRRPP SLNQEWRLDK
ILKRKAEQGV RVYVVVYKEV TQTMSMSSSH TKHALEALHS NIACMRHPDH IGSKDDVEFW
SHHEKLVVVD NHFACVGGLD LSFGRWDTHT HPLADAHPTQ LDRTLFPGQD YNNARIMDFK
DVWNYVSSGL SVVESPRMPW HDMHMTLTGP VVLDLVQHFV ERWNEIKRRK YRHETRYDWL
ALPHDIQSSP DEAVARHPYR EQWHKIGRHF KQRFHRHFGH VVDYENPDYN EEGYPGPPHG
TCRVQAIRSV SDWSHGVLTE HSIQNAYIQL IQEAQHYIYI ENQFFISSTR SDDVVKNQIA
KALTERIIRA AQEGRKFQVV IVIPEVPGFA GPVKDDSAVK TIMAAQYRTM NRGGHSIYEE
VRKQGYEPLD YIRFYHLRAY DRINAPFPSF ISKIEEKSGV KFHEAMTALA RLWIGRSEGP
EDPTDVAVAI PTGKFLAQRT PAGANTELKT ETYKLPRTLE EARDLIQQFE RGSESLRDDE
AVSDNVVQHM LHDKTNLLDE KWLGTEEEER AAYVSELLYI HSKVMIVDDQ RVIMGSANIN
DRSQKGDGDS EIALVIEDDD MIDSQMDGKP WLASRFAATL RRKLYREHLG LIPPQLCEPN
SEPTSFMRPA PYPNEDETGE QEDAWVADPL ADATLDLWNS TAKRNRDIFT EIFRPVPTNL
VRTWEQYDNY VPKVMTGHVV PEVPLARVKD RLSGVRGALV ECPIDFLIDQ KDFVEGIDWM
GLNPTLPIYI
//
