ID A0A177DFC3_ALTAL Unreviewed; 1030 AA.
AC A0A177DFC3;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE RecName: Full=Phospholipase {ECO:0000256|PIRNR:PIRNR009376};
DE EC=3.1.4.4 {ECO:0000256|PIRNR:PIRNR009376};
GN ORFNames=AA0117_g7314 {ECO:0000313|EMBL:RYN73854.1}, CC77DRAFT_1042505
GN {ECO:0000313|EMBL:OAG17947.1};
OS Alternaria alternata (Alternaria rot fungus) (Torula alternata).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Pleosporineae; Pleosporaceae; Alternaria;
OC Alternaria sect. Alternaria; Alternaria alternata complex.
OX NCBI_TaxID=5599 {ECO:0000313|EMBL:OAG17947.1, ECO:0000313|Proteomes:UP000077248};
RN [1] {ECO:0000313|EMBL:OAG17947.1, ECO:0000313|Proteomes:UP000077248}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SRC1lrK2f {ECO:0000313|EMBL:OAG17947.1,
RC ECO:0000313|Proteomes:UP000077248};
RG DOE Joint Genome Institute;
RA Zeiner C.A., Purvine S.O., Zink E.M., Wu S., Pasa-Tolic L., Chaput D.L.,
RA Haridas S., Grigoriev I.V., Santelli C.M., Hansel C.M.;
RT "Comparative analysis of secretome profiles of manganese(II)-oxidizing
RT ascomycete fungi.";
RL Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000291422}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FERA 1177 {ECO:0000313|Proteomes:UP000291422};
RA Armitage A.D., Cockerton H.M., Sreenivasaprasad S., Woodhall J., Lane C.,
RA Harrison R.J., Clarkson J.P.;
RT "Genomics, evolutionary history and diagnostics of the Alternaria alternata
RT species group including apple and Asian pear pathotypes.";
RL bioRxiv 0:0-0(2019).
RN [3] {ECO:0000313|EMBL:RYN73854.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=FERA 1177 {ECO:0000313|EMBL:RYN73854.1};
RA Armitage A.D., Cockerton H.M., Sreenivasaprasad S., Woodhall J., Lane C.,
RA Harrison R.J., Clarkson J.P.;
RT "Genomics, evolutionary history and diagnostics of the Alternaria alternata
RT species group including apple and Asian pear pathotypes.";
RL J. ISSAAS 0:0-0(2019).
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; KV441485; OAG17947.1; -; Genomic_DNA.
DR EMBL; PDXD01000019; RYN73854.1; -; Genomic_DNA.
DR RefSeq; XP_018383368.1; XM_018527272.1.
DR STRING; 5599.A0A177DFC3; -.
DR GeneID; 29112866; -.
DR KEGG; aalt:CC77DRAFT_1042505; -.
DR VEuPathDB; FungiDB:CC77DRAFT_1042505; -.
DR OMA; ILYWAHH; -.
DR OrthoDB; 335467at2759; -.
DR Proteomes; UP000077248; Unassembled WGS sequence.
DR Proteomes; UP000291422; 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; 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; PF13091; PLDc_2; 1.
DR PIRSF; PIRSF009376; Phospholipase_D_euk; 4.
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:UP000077248}.
FT DOMAIN 321..348
FT /note="PLD phosphodiesterase"
FT /evidence="ECO:0000259|PROSITE:PS50035"
FT DOMAIN 799..826
FT /note="PLD phosphodiesterase"
FT /evidence="ECO:0000259|PROSITE:PS50035"
FT REGION 1..59
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 72..107
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 443..488
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 501..527
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 700..745
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..38
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 39..55
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 86..105
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 461..482
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1030 AA; 116635 MW; 165F323B538D418E CRC64;
MSRRDDDLAY GDYHGQGGEE GDRGFVGDMG RRFGFGRKEN NQHSSSSSNQ GSGGMSFFKK
IHDPLHGFVS DLKDAISGDD NAQKPPPGTY EQQGGQPQPG QEYHEQHRFS SFAPERHGND
IKWYVDGCSY MYAVSIALER ARESIWILDW WLSPELYLRR PPAKNQQYRV DRMLQAAAER
GVKVNIIVYK EVTQALTRKF LNPTLPDYLH SLLPSSTDRF TKGLTRVGLD VIFKSLEEWE
KTDPLIAPPI TVSSAHTKHH LEDLHPNIGV FRHPDHLPDA AVLQSSFFAA MKNMSFTPAK
LAQLPGDGLK AIYGAHEGTV MYWAHHEKLC LIDGHIAFMG GLDLCYGRWD TNQHAIADAH
PGNIDRIVFP GQDFNNARML DFQDVTNWEN NKLDRTQSSR MGWSDVALCI SGPVVQDLRT
HFAQRWNFIY DEKYSKKATR YARLPETSSG AQQAPMQQRG FEGEEEGERG FGREEEGERG
LFGHGAGGHL RQKMQSRFEQ YGQEHGSQYG QQQSHAEHSS QQGGVDCQIT RSSAKWSHNL
VTTEHSIQNA YCEVIRNSKH FIYIENQFFI TATGDQQKPI KNKIGAAMVE RIIRAARNGE
KYKMIVMIPA VPAFAGDLKL DEALGTRAIM EFQYDSINRG GHSIYEEIAK AGFNPMDYIR
FYNLRSYDRI NSSQIMKEAE QRSGVSYNQA SEGYDAAHDN ARGYEAYRPP PTQEYGVYEM
DGSGRPPSHG RPDAGPQSQG RPGDYDRYQQ EAAKIGGRQG LGDGRWDTVS ECYMLGGEDI
RSVPWEGSAA DEMDAFVSEE LYIHSKLLIA DDQIVICGSA NLNDRSQLGD HDSEIAVIIQ
DPRPVDSYMD GRPYRASEFA ASLRRELFRK HLGLLKPQDM ERPTANYQPI GVPNEYDWGS
NEDRQVVDPL SDDFQNLWNW RAHTNTQAFG KIFHPVPSDE VKNWKQYDEY YSRFFGQDEK
AKENKKPSMY KWGHVVAENF GQGEQGVREV KEVLSTIKGN LVEMPLLFLK EEDIAQEGVG
LNAVTEELYT
//
