ID A0A166ZHE9_9HYPO Unreviewed; 1749 AA.
AC A0A166ZHE9;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE RecName: Full=phospholipase D {ECO:0000256|ARBA:ARBA00012027};
DE EC=3.1.4.4 {ECO:0000256|ARBA:ARBA00012027};
GN ORFNames=BBO_07301 {ECO:0000313|EMBL:OAA37921.1};
OS Beauveria brongniartii RCEF 3172.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Cordycipitaceae; Beauveria;
OC Beauveria brongniartii.
OX NCBI_TaxID=1081107 {ECO:0000313|EMBL:OAA37921.1, ECO:0000313|Proteomes:UP000076863};
RN [1] {ECO:0000313|EMBL:OAA37921.1, ECO:0000313|Proteomes:UP000076863}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RCEF 3172 {ECO:0000313|EMBL:OAA37921.1,
RC ECO:0000313|Proteomes:UP000076863};
RX PubMed=27071652; DOI=10.1093/gbe/evw082;
RA Shang Y., Xiao G., Zheng P., Cen K., Zhan S., Wang C.;
RT "Divergent and convergent evolution of fungal pathogenicity.";
RL Genome Biol. Evol. 8:1374-1387(2016).
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|ARBA:ARBA00000798};
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:OAA37921.1}.
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DR EMBL; AZHA01000028; OAA37921.1; -; Genomic_DNA.
DR OrthoDB; 335467at2759; -.
DR Proteomes; UP000076863; Unassembled WGS sequence.
DR GO; GO:0070290; F:N-acylphosphatidylethanolamine-specific phospholipase D activity; IEA:UniProtKB-EC.
DR GO; GO:0004630; F:phospholipase D activity; IEA:UniProtKB-EC.
DR GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-KW.
DR CDD; cd01254; PH_PLD; 1.
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; 2.
DR InterPro; IPR025202; PLD-like_dom.
DR InterPro; IPR001736; PLipase_D/transphosphatidylase.
DR InterPro; IPR015679; PLipase_D_fam.
DR PANTHER; PTHR18896:SF76; PHOSPHOLIPASE; 1.
DR PANTHER; PTHR18896; PHOSPHOLIPASE D; 1.
DR Pfam; PF00614; PLDc; 1.
DR Pfam; PF13091; PLDc_2; 1.
DR SMART; SM00155; PLDc; 2.
DR SUPFAM; SSF56024; Phospholipase D/nuclease; 2.
DR PROSITE; PS50035; PLD; 2.
PE 4: Predicted;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Lipid degradation {ECO:0000256|ARBA:ARBA00022963};
KW Lipid metabolism {ECO:0000256|ARBA:ARBA00022963}.
FT DOMAIN 892..919
FT /note="PLD phosphodiesterase"
FT /evidence="ECO:0000259|PROSITE:PS50035"
FT DOMAIN 1196..1223
FT /note="PLD phosphodiesterase"
FT /evidence="ECO:0000259|PROSITE:PS50035"
FT REGION 1..224
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 260..287
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 503..582
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1337..1365
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1412..1451
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1551..1575
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1606..1706
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 47..77
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 187..209
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 505..528
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1416..1436
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1614..1651
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1652..1680
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1749 AA; 196885 MW; 8DB72ADE91AE957A CRC64;
MARDDSVSPL SRSPQKSPTN DNPFKPPVVG GGLAATAPRR TPDGVASDDN VDNQQKEAPA
APSTRPSSLS AGLAPPKATE SNTAECFGAP GGRGSPDTPS TPGARVQFAR FDPPDFQPSH
SRHNSIENPD GVKSRGASLM SKLKSLTPGA LQSPKAPSLD LENMQAGAAS PTATRSPGRW
PDTLLEEEGE TDADMDGEAD ADVEEEADEA QPAGPPKKKK KRRMRRFVMG DGSVPGSPFR
FPNDGDAFGH RFLRRRASMP DTSTHNHVLS EGETPQPPKR RPFRRGHSWM HSGTAQAETD
IEALESSAVV GRRHGHARRS TVFGGGGVSD GDAIIQRRPF FTSERASNFG AQKWRQVKST
LRSLRQKKDD RIDYYKSTEL MAELRAGAPA VLMFASMIQR DEHGNKRIPV LLEQLKLKIT
DSTPDEGDDS DRHWDFTIQL EYGSGSSRMV WTVVRSVRDI YNLHFRYKFK LNNDMYLPGQ
IHLAARPKQP HFPYSAFPYL RAARGGRRDS SDAGEDAASD RERHAGQAGE ITAGDAAEAT
ASDGGGNRHP RRKRSRVNML GMRRRSTGLT DNGEGPSEGG PEALRQRFFE KQRRILEKYL
SELVRWLMFR ADSNRLCKFL ELSALGVRLA AEGSYHGKEG FLHIQSAKGL DFRRVLTPAK
MIARHSRKWF LVRSSYIVCV DSPENMNIYD VYLVDSSFSI ASKRSAIKQI AFKKKKKNDD
PTAEPSPSKH TLTLRTSERK VRLFTRFHSI NKQFHESITE MLLRTPWSKK KRFDSFAPVR
QGVFAQWLVD GRDYMWNVSR AINMAKDVIY IHDWWLSPEL YMRRPAAISQ KWRLDRLLQK
KAREGVKIFI IIYRNVEAAV PIDSEYTKFS LLNLHPNIFV QRSPNQFKKN QFFFAHHEKI
CIVDHDVAFT GGVDLCFGRW DCPQHPIVDD KATGFESSDV PRDAEHCQLF PGKDYSNPRV
QDFFRLAEPY EEMYDRSKVP RMPWHDIGMQ VVGQPARDLT RHFIQRWNYL RRGRKSTRPL
PFLLPPPEAN FEELEALGLT GTCEVQVLRS ASTWSLGLEE TEHSIQTAYI KMIEDSEHLV
YIENQFFISS TEVYNTRIVN RIGDALVHRI VRAHENGECW RCIILIPLMP GFQNTVDEQE
GTSVRLIIMC QLQSICRGEN SIFGRLRAAG IDPQEYIDFF SLRQWGIMST DALVTEQLYI
HAKTIIVDDR VALIGSANIN ERSMVGHRDS EVAVIVRDTD MIWSTMGGKP YQVGRFAHTL
RMRLMREHLG LDVDAIQEEE REDDPDLEGY EEQMDHIYEE KSGSSIGAPN GESSQPARVG
MQRLRSFNSD IDIEMAKAVD PDASQLDDES NRKDKGKKRE SNAAFQAERH IQDVAGHGPD
HWKAAELSGV DGGRDSVIID GREFLVSSVD SMGKGTLEEP QHKDVQESES RWQESGVENK
KPPPLPPFDE SAELDELRPA QLPTLPETGQ DDSPGDVLGA FRYMATEIKQ ATITKDCMTD
PIAPEFIDDI WNKVAQNNTK LYRKVFRCMP DSEVKTWAEY RDFVAYSKKF QERMEGRSTS
EEPDGTSEAG GNLRRTASSG AIGISVPDLE ALARLNGEDA EKLAANLNEQ HTNPDITGEK
REEDADEKAA AAADEEREMG ADVEKQPTNT ETLERKTTTF ANLEKPPTRD TTTTAAQAQF
GSVKRRRRAT TRGSRRWSNP EDMPSRTEGE GLLRMIQGNL VEFPYDWLIT EEHNGNWGYQ
VDGVAPLAI
//
