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Database: UniProt
Entry: X0ILF3_FUSOX
LinkDB: X0ILF3_FUSOX
Original site: X0ILF3_FUSOX 
ID   X0ILF3_FUSOX            Unreviewed;      1063 AA.
AC   X0ILF3;
DT   14-MAY-2014, integrated into UniProtKB/TrEMBL.
DT   14-MAY-2014, sequence version 1.
DT   27-MAR-2024, entry version 37.
DE   RecName: Full=phosphatidylserine decarboxylase {ECO:0000256|ARBA:ARBA00012243};
DE            EC=4.1.1.65 {ECO:0000256|ARBA:ARBA00012243};
GN   ORFNames=FOPG_03239 {ECO:0000313|EMBL:EXL84770.1};
OS   Fusarium oxysporum f. sp. conglutinans race 2 54008.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC   Fusarium oxysporum species complex.
OX   NCBI_TaxID=1089457 {ECO:0000313|EMBL:EXL84770.1};
RN   [1] {ECO:0000313|EMBL:EXL84770.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=54008 {ECO:0000313|EMBL:EXL84770.1};
RG   The Broad Institute Genome Sequencing Platform;
RA   Ma L.-J., Gale L.R., Schwartz D.C., Zhou S., Corby-Kistler H., Young S.K.,
RA   Zeng Q., Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Alvarado L.,
RA   Arachchi H.M., Berlin A., Brown A., Chapman S.B., Chen Z., Dunbar C.,
RA   Freedman E., Gearin G., Goldberg J., Griggs A., Gujja S., Heiman D.,
RA   Howarth C., Larson L., Lui A., MacDonald P.J.P., Montmayeur A., Murphy C.,
RA   Neiman D., Pearson M., Priest M., Roberts A., Saif S., Shea T., Shenoy N.,
RA   Sisk P., Stolte C., Sykes S., Wortman J., Nusbaum C., Birren B.;
RT   "The Genome Sequence of Fusarium oxysporum PHW808.";
RL   Submitted (NOV-2011) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:EXL84770.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=54008 {ECO:0000313|EMBL:EXL84770.1};
RG   The Broad Institute Genomics Platform;
RA   Ma L.-J., Corby-Kistler H., Broz K., Gale L.R., Jonkers W., O'Donnell K.,
RA   Ploetz R., Steinberg C., Schwartz D.C., VanEtten H., Zhou S., Young S.K.,
RA   Zeng Q., Gargeya S., Fitzgerald M., Abouelleil A., Alvarado L.,
RA   Chapman S.B., Gainer-Dewar J., Goldberg J., Griggs A., Gujja S., Hansen M.,
RA   Howarth C., Imamovic A., Ireland A., Larimer J., McCowan C., Murphy C.,
RA   Pearson M., Poon T.W., Priest M., Roberts A., Saif S., Shea T., Sykes S.,
RA   Wortman J., Nusbaum C., Birren B.;
RT   "The Genome Annotation of Fusarium oxysporum PHW808.";
RL   Submitted (MAY-2012) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=pyruvate; Xref=ChEBI:CHEBI:15361;
CC         Evidence={ECO:0000256|ARBA:ARBA00001928};
CC   -!- PATHWAY: Lipid metabolism. {ECO:0000256|ARBA:ARBA00005189}.
CC   -!- PATHWAY: Phospholipid metabolism; phosphatidylethanolamine
CC       biosynthesis. {ECO:0000256|ARBA:ARBA00024326}.
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DR   EMBL; JH658811; EXL84770.1; -; Genomic_DNA.
DR   AlphaFoldDB; X0ILF3; -.
DR   UniPathway; UPA00558; -.
DR   Proteomes; UP000030676; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   GO; GO:0004609; F:phosphatidylserine decarboxylase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006646; P:phosphatidylethanolamine biosynthetic process; IEA:UniProtKB-UniPathway.
DR   CDD; cd04024; C2A_Synaptotagmin-like; 1.
DR   CDD; cd00051; EFh; 1.
DR   Gene3D; 2.60.40.150; C2 domain; 2.
DR   Gene3D; 1.10.238.10; EF-hand; 1.
DR   InterPro; IPR000008; C2_dom.
DR   InterPro; IPR035892; C2_domain_sf.
DR   InterPro; IPR011992; EF-hand-dom_pair.
DR   InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR   InterPro; IPR002048; EF_hand_dom.
DR   InterPro; IPR003817; PS_Dcarbxylase.
DR   InterPro; IPR033177; PSD-B.
DR   NCBIfam; TIGR00163; PS_decarb; 1.
DR   PANTHER; PTHR10067; PHOSPHATIDYLSERINE DECARBOXYLASE; 1.
DR   PANTHER; PTHR10067:SF17; PHOSPHATIDYLSERINE DECARBOXYLASE PROENZYME 2; 1.
DR   Pfam; PF00168; C2; 2.
DR   Pfam; PF02666; PS_Dcarbxylase; 1.
DR   SMART; SM00239; C2; 2.
DR   SUPFAM; SSF49562; C2 domain (Calcium/lipid-binding domain, CaLB); 2.
DR   SUPFAM; SSF47473; EF-hand; 1.
DR   PROSITE; PS50004; C2; 2.
DR   PROSITE; PS00018; EF_HAND_1; 1.
DR   PROSITE; PS50222; EF_HAND_2; 1.
PE   4: Predicted;
KW   Calcium {ECO:0000256|ARBA:ARBA00022837};
KW   Decarboxylase {ECO:0000256|ARBA:ARBA00022793};
KW   Lipid biosynthesis {ECO:0000256|ARBA:ARBA00022516};
KW   Lipid metabolism {ECO:0000256|ARBA:ARBA00023098};
KW   Lyase {ECO:0000256|ARBA:ARBA00023239};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136};
KW   Phospholipid biosynthesis {ECO:0000256|ARBA:ARBA00023209};
KW   Phospholipid metabolism {ECO:0000256|ARBA:ARBA00023264};
KW   Pyruvate {ECO:0000256|ARBA:ARBA00023317};
KW   Zymogen {ECO:0000256|ARBA:ARBA00023145}.
FT   DOMAIN          42..161
FT                   /note="C2"
FT                   /evidence="ECO:0000259|PROSITE:PS50004"
FT   DOMAIN          279..400
FT                   /note="C2"
FT                   /evidence="ECO:0000259|PROSITE:PS50004"
FT   DOMAIN          530..565
FT                   /note="EF-hand"
FT                   /evidence="ECO:0000259|PROSITE:PS50222"
FT   REGION          1..56
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          213..270
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          424..493
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          631..688
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        8..56
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        213..237
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        238..260
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        424..458
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        638..664
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        670..688
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1063 AA;  118906 MW;  A2DC694F10EDA2BB CRC64;
     MVRIIPTRLK STSRSSSSSS TTIHSVSNTN GRTKNNRSNS PPMRSKNDST SPSRDAGNGL
     ALRVYIIKGK DLAAKDRSGT SDPYLVLSSG DSRIVTNDVP KTLNPEWNVT EEIPLTSVQN
     LVLDVICWDK DRFGKDYMGE FDLALEEIFN NDKVEQEPTW YRLKSKRPGK KTSVVSGEVQ
     LQFSLFDSTN PSATPQQILE KFQALVGTAP AGSRNVTPSM TPNLAPTGSQ SAPNPQDSPS
     DDDEDDFDED DSDEGDEDEG EQDATKRKRR LRIRGLKKRR RNNPYAFASS GSDVVGIIYL
     EVIKITDLPP ESNLTRTSFD MDPFVVASLG KKTYRTRRIR HDLNPVYNEK MLFHIQSHEQ
     QYSFAFTVID HDKYSGNDFI ASCDLPIHQL IERAPKANPE TGLYDLQAPA QAEPLPSRSR
     FKKLAMSRSN SSSSISKMIR PPLSKHASNT SMASATPAPA PTSAPDPNKL APADVLANTG
     SDPDSANQDS GDADFYEYNV PLKMKNTEKW EKKHNPVLYL RAKYMPYDAL RQQFWRAMLR
     QYDADESGRI SRIELTTMLE SLGSTLTENT IDGFFKRFPH RDADNDENWE LTMDECVICL
     EDQLEGRRRS SGTAADKLKG LVPEMKNLLH VPGHGHNNGG SETPSVLELD STSGTQTPIS
     NVPTLKTPAD EEGDPLDKSD SSDDRSEEHV VEIRECPICH QPRLNKRKDA DIITHIATCA
     SQDWRQVNSV LVGGFVTASQ AQRKWYSKVI TKISYGGYKL GANSANILVQ DRLTGQINEE
     KMSVYVRLGI RLLYKGLKSR DMENKRIRKL LKNLSIKQGK KFDDPASKDE IEKFIAFHGL
     DMSEVLLPLD EFNNFNEFFY RALKPGARPC SAPDNPHIIV SPADCRSVVF NSITVATKIW
     VKGREFNMKR LLGDAYPEDV SRFEGGALGI FRLAPQDYHR FHIPVDGVMG KPKTIEGEYY
     TVNPMAIRSA LDVYGENVRV LVPIDSEHHG RVMVICVGAM MVGSTVITRK EGDRVHRAEE
     LGYFKFGGST ILLLFEPGRM VFDDDLVDNS KDALETLVSN LHW
//
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