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Database: UniProt
Entry: M2TV30_COCH5
LinkDB: M2TV30_COCH5
Original site: M2TV30_COCH5 
ID   M2TV30_COCH5            Unreviewed;       973 AA.
AC   M2TV30;
DT   01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   01-MAY-2013, sequence version 1.
DT   27-MAR-2024, entry version 37.
DE   RecName: Full=Phospholipase {ECO:0000256|PIRNR:PIRNR009376};
DE            EC=3.1.4.4 {ECO:0000256|PIRNR:PIRNR009376};
GN   ORFNames=COCHEDRAFT_1139663 {ECO:0000313|EMBL:EMD90364.1};
OS   Cochliobolus heterostrophus (strain C5 / ATCC 48332 / race O) (Southern
OS   corn leaf blight fungus) (Bipolaris maydis).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Pleosporomycetidae; Pleosporales; Pleosporineae; Pleosporaceae; Bipolaris.
OX   NCBI_TaxID=701091 {ECO:0000313|EMBL:EMD90364.1, ECO:0000313|Proteomes:UP000016936};
RN   [1] {ECO:0000313|EMBL:EMD90364.1, ECO:0000313|Proteomes:UP000016936}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C5 / ATCC 48332 / race O {ECO:0000313|Proteomes:UP000016936};
RX   PubMed=23236275; DOI=10.1371/journal.ppat.1003037;
RA   Ohm R.A., Feau N., Henrissat B., Schoch C.L., Horwitz B.A., Barry K.W.,
RA   Condon B.J., Copeland A.C., Dhillon B., Glaser F., Hesse C.N., Kosti I.,
RA   LaButti K., Lindquist E.A., Lucas S., Salamov A.A., Bradshaw R.E.,
RA   Ciuffetti L., Hamelin R.C., Kema G.H.J., Lawrence C., Scott J.A.,
RA   Spatafora J.W., Turgeon B.G., de Wit P.J.G.M., Zhong S., Goodwin S.B.,
RA   Grigoriev I.V.;
RT   "Diverse lifestyles and strategies of plant pathogenesis encoded in the
RT   genomes of eighteen Dothideomycetes fungi.";
RL   PLoS Pathog. 8:E1003037-E1003037(2012).
RN   [2] {ECO:0000313|Proteomes:UP000016936}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C5 / ATCC 48332 / race O {ECO:0000313|Proteomes:UP000016936};
RX   PubMed=23357949; DOI=10.1371/journal.pgen.1003233;
RA   Condon B.J., Leng Y., Wu D., Bushley K.E., Ohm R.A., Otillar R., Martin J.,
RA   Schackwitz W., Grimwood J., MohdZainudin N., Xue C., Wang R., Manning V.A.,
RA   Dhillon B., Tu Z.J., Steffenson B.J., Salamov A., Sun H., Lowry S.,
RA   LaButti K., Han J., Copeland A., Lindquist E., Barry K., Schmutz J.,
RA   Baker S.E., Ciuffetti L.M., Grigoriev I.V., Zhong S., Turgeon B.G.;
RT   "Comparative genome structure, secondary metabolite, and effector coding
RT   capacity across Cochliobolus pathogens.";
RL   PLoS Genet. 9:E1003233-E1003233(2013).
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; KB445578; EMD90364.1; -; Genomic_DNA.
DR   AlphaFoldDB; M2TV30; -.
DR   STRING; 701091.M2TV30; -.
DR   eggNOG; KOG1329; Eukaryota.
DR   HOGENOM; CLU_000690_2_2_1; -.
DR   OMA; ILYWAHH; -.
DR   Proteomes; UP000016936; 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; PF13091; PLDc_2; 1.
DR   PIRSF; PIRSF009376; Phospholipase_D_euk; 3.
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:UP000016936}.
FT   DOMAIN          270..297
FT                   /note="PLD phosphodiesterase"
FT                   /evidence="ECO:0000259|PROSITE:PS50035"
FT   DOMAIN          742..769
FT                   /note="PLD phosphodiesterase"
FT                   /evidence="ECO:0000259|PROSITE:PS50035"
FT   REGION          1..58
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          74..105
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          394..472
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          646..689
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        38..54
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        78..105
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        410..439
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        444..472
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        667..681
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   973 AA;  110318 MW;  2FE8EF7F475EA034 CRC64;
     MSRRDDDLAY GEYNAQEGQE GDRGLIGDMG RRFGFGKKEN TQPQSSSSQQ GGGGGGMSFF
     KKLHDPLHDF VSDLKDAISG DDNNNQQKPP AGTYEQTGQP GATQEYHQQH RFSSFAPERH
     GNEIKWYVDG CSYMYAVSIA LERAKESIWI LDWWLSPELY LRRPPAKNQQ YRVDRMLLAA
     AERGVKVNII VYKEVTQALT LSSSHTKHHL EDLHQNIGVF RHPDHLPDAA VLQSNFFASM
     KNMSFTPAAL AQLPGDGLKA IYGAHEGTVM YWAHHEKLCL IDGHIAFMGG LDLCYGRWDT
     NQHAIADAHP GNIDRIVFPG QDFNNARMMD FQDVSNWENN KLDRTQSSRM GWSDVALCVS
     GPVVQDLRTH FTQRWNFIYD EKYSKKATRY ARLPDISSGA QQAPTQQRGF EGDEGERGFG
     GNEEGDRGIF GHGGLRQKMH SKFDQYGQGH SSYQPHQQSH AEHSSQKGGV DCQITRSSAK
     WSHNLITTEH SIQNAYCEII RNSKHFIYIE NQFFITATGD QQKPIKNMVG AAIVERIVRA
     ARNGEKYKMI VMIPAVPAFA GDLKLDEALG TRAIMEFQYD SINRGGHSIY EEIAKAGFNP
     MEYIRFYNLR SYDRINSSQV MQETEQRSGV SYTQAQEGFD AAHDNARGYQ AYRPPPTQEY
     GVYEMDGSSV PQQQYGGGPQ SQGRKSDYDR YQQEAMKVGG RQGLGDGRWD TVSECYMLGG
     EDIRNVPWEG SPDAEMDAFV SEELYIHSKL LIADDQVVIC GSANLNDRSQ LGDHDSEIAI
     IIHDPNTVES YMDGRPWRAS KFAASLRREI FRKHLGLLKP QDMERPNANY EPVGIPNQYD
     WGSHEDRQVV DPISDEFWNL WNWRAHTNTQ AFGKVFHPVP SDEVKNWKQY DEYYSRFFGQ
     DEKAKENKKP SLYKWGHVVA ENFAPGEQGV REVKEILSTI KGNLVEMPLL FLKEEDIAKE
     GVGLNALTEE IYT
//
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