ID C6H909_AJECH Unreviewed; 1812 AA.
AC C6H909;
DT 01-SEP-2009, integrated into UniProtKB/TrEMBL.
DT 01-SEP-2009, sequence version 1.
DT 27-MAR-2024, entry version 58.
DE RecName: Full=phospholipase D {ECO:0000256|ARBA:ARBA00012027};
DE EC=3.1.4.4 {ECO:0000256|ARBA:ARBA00012027};
GN ORFNames=HCDG_02690 {ECO:0000313|EMBL:EER42792.1};
OS Ajellomyces capsulatus (strain H143) (Darling's disease fungus)
OS (Histoplasma capsulatum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Ajellomycetaceae; Histoplasma.
OX NCBI_TaxID=544712 {ECO:0000313|EMBL:EER42792.1, ECO:0000313|Proteomes:UP000002624};
RN [1] {ECO:0000313|Proteomes:UP000002624}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=H143 {ECO:0000313|Proteomes:UP000002624};
RA Champion M., Cuomo C.A., Ma L.-J., Henn M.R., Sil A., Goldman B.,
RA Young S.K., Kodira C.D., Zeng Q., Koehrsen M., Alvarado L., Berlin A.M.,
RA Borenstein D., Chen Z., Engels R., Freedman E., Gellesch M., Goldberg J.,
RA Griggs A., Gujja S., Heiman D.I., Hepburn T.A., Howarth C., Jen D.,
RA Larson L., Lewis B., Mehta T., Park D., Pearson M., Roberts A., Saif S.,
RA Shea T.D., Shenoy N., Sisk P., Stolte C., Sykes S., Walk T., White J.,
RA Yandava C., Klein B., McEwen J.G., Puccia R., Goldman G.H., Felipe M.S.,
RA Nino-Vega G., San-Blas G., Taylor J.W., Mendoza L., Galagan J.E.,
RA Nusbaum C., Birren B.W.;
RT "The genome sequence of Ajellomyces capsulatus strain H143.";
RL Submitted (MAY-2009) to the EMBL/GenBank/DDBJ databases.
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};
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DR EMBL; GG692421; EER42792.1; -; Genomic_DNA.
DR STRING; 544712.C6H909; -.
DR VEuPathDB; FungiDB:HCDG_02690; -.
DR eggNOG; KOG1329; Eukaryota.
DR HOGENOM; CLU_000690_0_1_1; -.
DR OMA; DSLWTKH; -.
DR Proteomes; UP000002624; Unassembled WGS sequence.
DR GO; GO:0070290; F:N-acylphosphatidylethanolamine-specific phospholipase D activity; IEA:UniProtKB-EC.
DR GO; GO:0035091; F:phosphatidylinositol binding; IEA:InterPro.
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 Gene3D; 3.30.1520.10; Phox-like domain; 1.
DR InterPro; IPR025202; PLD-like_dom.
DR InterPro; IPR001736; PLipase_D/transphosphatidylase.
DR InterPro; IPR015679; PLipase_D_fam.
DR InterPro; IPR036871; PX_dom_sf.
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};
KW Reference proteome {ECO:0000313|Proteomes:UP000002624}.
FT DOMAIN 934..961
FT /note="PLD phosphodiesterase"
FT /evidence="ECO:0000259|PROSITE:PS50035"
FT DOMAIN 1240..1267
FT /note="PLD phosphodiesterase"
FT /evidence="ECO:0000259|PROSITE:PS50035"
FT REGION 1..329
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 343..364
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 558..607
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 753..774
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1389..1428
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1450..1530
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1685..1761
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 10..48
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 107..143
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 163..178
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 181..205
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 208..234
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 268..308
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 315..329
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1389..1405
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1406..1425
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1460..1475
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1498..1530
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1812 AA; 205967 MW; 89B681F987B008CB CRC64;
MGEDPAPSMA EGLQQSSSPQ RSSVPQNLKL TMPHTLSTNG ASFTTRLEDE TLHSSDLKKD
PVNGINGTYG APGTLVELGT GFEPPSSEQP ARDIDASGHQ GNIPYRTKPA SIPSRNPSTK
SGKGKQQRQH GFSTPQGRRS VQFARTASDV EGGGSHSRAS SIGPEDGDQK DRRFHSSLFS
KLKTFAASPS FPTHARTSSG LTTGDESAEH RPPGDTATPR SERGEFRFPN TLEEEGSEMD
ADAESSSGEQ AVGIPKRKRK IRRQRGSVSH TAPATPKSSA RPSFHPSGSY THGDNFFGSH
FSRRTEPHTI SPPTRDGVSE DEGRERLKRD NMWRRRNGWL HSARGLSYSG PSRTEGRGSQ
DEKRLSNFRR LTGFGGQPDH GEGLTATWRR HKAERGSSLS AQRWRQIKAG LKMIGHRKKV
ETTVDHVKSA ELLAELISGI PAALLLASMF QRDEHGSRRI PILLEQLKVH ITDSKFDPHS
SDRHLTFRIE LEYGSGMTRM KWVINRTLRD FANLHIKYKL QIGTMRYIQL KAHDSAHPLP
RFPRSAFPYL RGVRGLESEG EEEADEGGFE TAGDGTSGNE KANRKKKRRS SLGLSRRRSS
LTAPVESGAS GVLESGITRA ASIGGIKKES YPERQRKKLE IYLQQMIRFL IFRPDSNRLC
KFLELSALGV RLASEGSYHG KEGFLVIQSS KGLDFRRALN PAMIKSRHSP KWFLVRHSYV
VCVDSPEEMN IYDVFLVDPF FQIQHQKVRL RDQKPKQLAR SAKESAAHPQ HHTLKLQNSE
RKLRLLARNE RQLHQFEDSI RFMMDTTPWS KPNRFDSFAP VRPNCFAQWL VDGRDYMWVV
SRAINQAKDV VYIHDWWLSP ELYMRRPAAI SQKWRLDRLL QKKAQEGVKV FVIMYRNINS
AIPIDSEYSK FSLLDLHPNI FVQRSPNQFR QNTFFWAHHE KLCLVDHTLA FIGGIDLCFG
RWDTPQHLLT DDKLTGFELT DVPKDADHCQ LWPGKDYSNP RIQDFYDLDK PYEEMYDREV
VPRMPWHDIA MHVVGQPARD LTRHFVQRWN YILRQRKPTR PTPFLLPPPD FNPADLESLG
LDGTCEVQIL RSSSTWSTGT PDVTEHSIMN AYVKMIEQSE HFVYIENQFF ITSCEIEGKK
IENLIGDALV ERIIRASRSD EEWRAVILIP LMPGFQNQVD TEGGTSVRLI MQCQYRSICR
GETSIFGRLR AAGIEPEDYI QFFSLRSWGK IGPRKHLVTE QLYIHAKCMI VDDRVAIIGS
ANINERSMLG SRDSECAAIV RDTDLLWSTM GGKPYLVGRF PHTLRMRLMR EHIGLDVDEI
MEQAEAESDQ MNARGEPNTP YNYSDDMLDR EFDEATERQD ERELLERRHR IQDEFLARSE
EMHSFNHDVD WEQANNPNLK SNKKLTQDSR VMRNEDHKKD LEGYGVDQMK SIQEAGHGDG
RDSFIVDDRI EFLGPGSPGD PNSRSRQSNV PKELPSQTGD HGEQEDFPPA AAKNFDPSVP
SSRPSTQPTA YDLSSNAGNP SLQTSQDIPN RTHIVSSEIN LPVVDKDCMR DPLNDSFYLD
VWQAIAENNT KLYRSVFRCM PDNEVKTWKE YKEYTAYAER FADMQGQSHY EAKAHEAKNN
PEAAKVTGPP GTAVIPNQLA KAEKMGHDMK DKVLNPVKCD TLAAEEDLRH WASEANKAQI
ERKRFELSHQ EPSTSQGEKD ALKATETKSS HSSQNLDGVM ASFPEVERSP QKWADGSLRP
TAQSQRRRRR ATTRSSRREF HASDDIISKA EAEDLMNLIQ GHLIVWPYEW LEREEQGGNW
LYTLDQISPL EI
//
