ID A0A179A146_9EURO Unreviewed; 1287 AA.
AC A0A179A146;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 02-APR-2025, entry version 32.
DE RecName: Full=phospholipase D {ECO:0000256|ARBA:ARBA00012027};
DE EC=3.1.4.4 {ECO:0000256|ARBA:ARBA00012027};
GN ORFNames=AYL99_01731 {ECO:0000313|EMBL:OAP65759.1};
OS Fonsecaea erecta.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Fonsecaea.
OX NCBI_TaxID=1367422 {ECO:0000313|EMBL:OAP65759.1, ECO:0000313|Proteomes:UP000078343};
RN [1] {ECO:0000313|EMBL:OAP65759.1, ECO:0000313|Proteomes:UP000078343}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 125763 {ECO:0000313|EMBL:OAP65759.1,
RC ECO:0000313|Proteomes:UP000078343};
RA Weiss V.A., Vicente V.A., Raittz R.T., Moreno L.F., De Souza E.M.,
RA Pedrosa F.O., Steffens M.B., Faoro H., Tadra-Sfeir M.Z., Najafzadeh M.J.,
RA Felipe M.S., Teixeira M., Sun J., Xi L., Gomes R., De Azevedo C.M.,
RA Salgado C.G., Da Silva M.B., Nascimento M.F., Queiroz-Telles F.,
RA Attili D.S., Gorbushina A.;
RT "Draft genome of Fonsecaea erecta CBS 125763.";
RL Submitted (APR-2016) to the EMBL/GenBank/DDBJ databases.
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:OAP65759.1}.
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DR EMBL; LVYI01000001; OAP65759.1; -; Genomic_DNA.
DR RefSeq; XP_018699126.1; XM_018833247.1.
DR STRING; 1367422.A0A179A146; -.
DR GeneID; 30005901; -.
DR OrthoDB; 14911at2759; -.
DR Proteomes; UP000078343; Unassembled WGS sequence.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IEA:TreeGrafter.
DR GO; GO:0004630; F:phospholipase D activity; IEA:UniProtKB-EC.
DR GO; GO:0009395; P:phospholipid catabolic process; IEA:TreeGrafter.
DR CDD; cd09138; PLDc_vPLD1_2_yPLD_like_1; 1.
DR CDD; cd09141; PLDc_vPLD1_2_yPLD_like_2; 1.
DR FunFam; 3.30.870.10:FF:000032; Phospholipase; 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; 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 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:ARBA00023098};
KW Reference proteome {ECO:0000313|Proteomes:UP000078343}.
FT DOMAIN 325..352
FT /note="PLD phosphodiesterase"
FT /evidence="ECO:0000259|PROSITE:PS50035"
FT DOMAIN 1056..1083
FT /note="PLD phosphodiesterase"
FT /evidence="ECO:0000259|PROSITE:PS50035"
FT REGION 1..108
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 127..151
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 450..716
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 733..755
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 38..50
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 51..79
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 133..151
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 455..467
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 476..489
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 498..514
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 527..566
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 599..608
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 609..619
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 652..672
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 701..716
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1287 AA; 141615 MW; 59165BAACAAEBAD8 CRC64;
MSYHQRPEDD GLAYGDDYSQ SRGSGAQDGT DRSLLGDTFK KFRSELDKYK SSSSSSPNYG
YSGSGSGSNQ QYYGQQGPST GYPQIGQSAY PGGPPTQQPG GRPDLASKLF GGLQNTLQNI
GSDVTNLLGP GNRPSSQYGP PAPGQSTYAG YTNVPVPQSI PSGPNRYDSF ASEKPGNDVK
WYVDGCGYFW AVSQALEGAK HSIWILDWWL SPELYLRRPP SQNEQWRLDR TLQRAAQRGV
KVKVIVYKEV TQALTLSSAH TKHELEKLHP NIAVFRHPDH LPDAQTAQSS LISSFQALKL
DAAGLSKLGG DTLKGIYGVT DDVILYWAHH EKLCLIDDKI AFMGGLDLCF GRWDTNQHSI
ADAHPSNIND IVFPGQDYNN ARVMDFSDVA QPFQNKLDRT KNSRMGWSDI GICLQGACVL
DLRHHFVDRW NFIYDEKYNV RKDQRYYRLL DDFPHPPAGP GQRPQPRPQS QGHLQPPAPA
GGYAPPPGSQ PYSEPAWHTT SRPHTPNAGQ YQSQAGTDAG GYGATTPSAP GVQTLSQHPD
AQYGQTTASF GPGAQTQAPS QTSASAYGQF PPPPPQAPVQ TSAGAYGQPA PLMHPPHPSS
SDAYSQVYSP PPHATPPPAM STYGQVSSPP PPAAAVQQPV STGGSYQQPP AQSIPPNFPP
PPPGPPPQPS PGPTHVYPGY PPPPSANAPY APYHQEVSEL SSQQSPPQSY QHQPYQAYQP
ADAGQARGFD EYDQDASRGF DDYGQGSESE RGLRGRFDQY KTEGKLLGQQ FSSIGNAVSS
GLGDKAHQLQ GKYFGGTDSY GRPYGQPRPV MTCQLLRSCT TWSNGTPLEH SIQNAYIDVI
RNSQHFVYIE NQFFITATGD QQKPVKNLIG QAIVERILRA ARNNEKYKMI VVIPAVPAFA
GDLRDDSSLA TRAIMEFQYN SINRGGHSIM EKIAQAGFNP MDYIRFYNLR NYDRINCSNT
MQQVEQHSGV RYEDARKQHD DAVGAGYGQY GEKTGTTQLS QAPQYQQYQT TAQQTTTPGS
GRWDSVAECY MLGGQDIRTV PWDGAPEAEL DAFVSEELYI HSKCLIADDR IVIVGSANLN
DRSQVGSHDS EIALLINDST PVQSYMNGQP YQANGFAASL RRQLVRKHLG LVRPQHFFRP
DPNFDPVGVP NVYDWGSPED NVVADPLSDT FQALWNSRAR TNTEVFRRAF RAVPDDFVTT
WGDYKEFYEY FYRHADMEAQ GKPSKLPPRV EYGHVVRADF PGGVSELKEL LSQVKGTLVE
MPLCFLQNED IAKEGLTLNP LTEEVYT
//
