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Database: UniProt
Entry: A0A395S1Y1_FUSSP
LinkDB: A0A395S1Y1_FUSSP
Original site: A0A395S1Y1_FUSSP 
ID   A0A395S1Y1_FUSSP        Unreviewed;      1264 AA.
AC   A0A395S1Y1;
DT   05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 1.
DT   27-MAR-2024, entry version 19.
DE   SubName: Full=Pyoverdine dityrosine biosynthesis {ECO:0000313|EMBL:RGP66049.1};
GN   ORFNames=FSPOR_6875 {ECO:0000313|EMBL:RGP66049.1};
OS   Fusarium sporotrichioides.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium.
OX   NCBI_TaxID=5514 {ECO:0000313|EMBL:RGP66049.1, ECO:0000313|Proteomes:UP000266152};
RN   [1] {ECO:0000313|EMBL:RGP66049.1, ECO:0000313|Proteomes:UP000266152}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NRRL 3299 {ECO:0000313|EMBL:RGP66049.1,
RC   ECO:0000313|Proteomes:UP000266152};
RX   PubMed=29649280; DOI=10.1371/journal.ppat.1006946;
RA   Proctor R.H., McCormick S.P., Kim H.S., Cardoza R.E., Stanley A.M.,
RA   Lindo L., Kelly A., Brown D.W., Lee T., Vaughan M.M., Alexander N.J.,
RA   Busman M., Gutierrez S.;
RT   "Evolution of structural diversity of trichothecenes, a family of toxins
RT   produced by plant pathogenic and entomopathogenic fungi.";
RL   PLoS Pathog. 14:e1006946-e1006946(2018).
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:RGP66049.1}.
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DR   EMBL; PXOF01000097; RGP66049.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A395S1Y1; -.
DR   STRING; 5514.A0A395S1Y1; -.
DR   Proteomes; UP000266152; Unassembled WGS sequence.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   CDD; cd02440; AdoMet_MTases; 1.
DR   Gene3D; 3.60.130.10; Clavaminate synthase-like; 1.
DR   Gene3D; 3.20.20.60; Phosphoenolpyruvate-binding domains; 1.
DR   Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR   InterPro; IPR005000; Aldolase/citrate-lyase_domain.
DR   InterPro; IPR007817; Isocyanide_synthase_DIT1.
DR   InterPro; IPR013217; Methyltransf_12.
DR   InterPro; IPR015813; Pyrv/PenolPyrv_Kinase-like_dom.
DR   InterPro; IPR040442; Pyrv_Kinase-like_dom_sf.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   InterPro; IPR042098; TauD-like_sf.
DR   InterPro; IPR003819; TauD/TfdA-like.
DR   PANTHER; PTHR37285:SF6; BIOSYNTHESIS PROTEIN, PUTATIVE (AFU_ORTHOLOGUE AFUA_5G02660)-RELATED; 1.
DR   PANTHER; PTHR37285; SPORE WALL MATURATION PROTEIN DIT1; 1.
DR   Pfam; PF05141; DIT1_PvcA; 1.
DR   Pfam; PF03328; HpcH_HpaI; 1.
DR   Pfam; PF08242; Methyltransf_12; 1.
DR   Pfam; PF02668; TauD; 1.
DR   SUPFAM; SSF51197; Clavaminate synthase-like; 1.
DR   SUPFAM; SSF51621; Phosphoenolpyruvate/pyruvate domain; 1.
DR   SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
PE   4: Predicted;
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000266152}.
FT   DOMAIN          44..221
FT                   /note="HpcH/HpaI aldolase/citrate lyase"
FT                   /evidence="ECO:0000259|Pfam:PF03328"
FT   DOMAIN          358..459
FT                   /note="Methyltransferase type 12"
FT                   /evidence="ECO:0000259|Pfam:PF08242"
FT   DOMAIN          1008..1261
FT                   /note="TauD/TfdA-like"
FT                   /evidence="ECO:0000259|Pfam:PF02668"
FT   REGION          629..648
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        629..647
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1264 AA;  141054 MW;  41A5A7436322DB83 CRC64;
     MAVQSKHLND EGMAAYRGPS LQQPHRARQA LKDAYAGLIP PLLGFYCGIT STSVAQYVAT
     LGYDVVWVDW EHSSCGIETM TSIVQTISFF SEGKSMPFVR LPGHDHKDVA YALDAGASVV
     FPQVDTVEQA KECVSATKYG LKNRGSRSAP PFRLIPGVTD HKLDHSHTLH ENLNRQAAVL
     IQIESEKGIN NLDAILTEVS DIDAVWLGAM DLRVSMGFEG MWGNEPEFLT AVGKYNSILA
     KHDMPGAGIV QGPPDVMTQL SKGRAFMIVA SDVQAIMGQK QAFVEARTLM PKVNNYDGSP
     PILQPQESEQ IENDLYLLPR DEQETKRLDE QHRYIVELCD GFILSPIIQT DRLKMVADVG
     TGSGAWLIDL DTRLRAQGES NNTAFHGFDI SDLQFPTLSK DQEPRFKFSV HDVRKPFPKE
     HIGKYDLVHV RLLVWALPAD DVDAVVANLS SLLKPGGYLA WDEAAYLDSV DSAGTPEGIR
     IHDIVVDFMK KRNLCVDLPS VLRKSYQKAG LDMQHSIRYS SLQHPKLHLT TNKIIGDGAI
     SVLRNLTQET PVTPEQVKLN NEMKSLIASY PATQQLMRWQ CCLQSVVGRY PQQLPLRAPS
     VAITNGVTTN GTATNGVAEN GTIVNGTHTD GIKANGTHES STKSGQLAAK KLERGKSFSN
     PSSPESMALK AMVNLNRYRM SYKNDWDLPK AISTLRPFLE NAIRNKEPIR LVLPAFPFKS
     SNRTAKVLGA DPDEAERISL LHLDGLCKAL EEATKLKVEL LITSDGVMYN DLLGISDEEV
     WRYGEGIRRI AKEQGCSHIS FNRLGALISH EVDSTASLDD YMRDAPGYRR QLEALLPPGF
     DPAQEIKTNH DVKLTYLGYK RFLDLEMQNA APNDSNLSLR DRKAITAKNM IKRGKAYAEA
     IRNAYPNAIR LSIHESDDVN KISIAILPLA SGNPMTPWHG ALIRAVNGDL TISHALNVSA
     LKYDLVYEYG KPSYFRERSP LFSWTGMDLS FTYMYPTGII VRPAHKDLKY SLQDIDMGKL
     RALSEQCSPV VLRGFRDTKE KSVFGSKAKE MGTILPWKEG DIMVVKDQMN DASDSNVTTT
     NEAMPMHYDG MFKLVKVMDE QGRESVTSDP PLLQYFVCQA TTGNNQGFTL FASSRLFCHY
     LPDKYPIEEL RKVRWTCHSG GYFDHHVPSL PLVVSHPVDA RPCIRWHEPW PKTETKYGDA
     SITIDNGDQS LVGLVDSLLY DERVCLRFAW EEGDVLVNDN MEMLHTRTAF ERGAERELWR
     IHVS
//
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