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Database: UniProt
Entry: A0A395RG42_FUSSP
LinkDB: A0A395RG42_FUSSP
Original site: A0A395RG42_FUSSP 
ID   A0A395RG42_FUSSP        Unreviewed;      1155 AA.
AC   A0A395RG42;
DT   05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 1.
DT   27-MAR-2024, entry version 22.
DE   RecName: Full=Lustrin a {ECO:0008006|Google:ProtNLM};
GN   ORFNames=FSPOR_11570 {ECO:0000313|EMBL:RGP59100.1};
OS   Fusarium sporotrichioides.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium.
OX   NCBI_TaxID=5514 {ECO:0000313|EMBL:RGP59100.1, ECO:0000313|Proteomes:UP000266152};
RN   [1] {ECO:0000313|EMBL:RGP59100.1, ECO:0000313|Proteomes:UP000266152}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NRRL 3299 {ECO:0000313|EMBL:RGP59100.1,
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:RGP59100.1}.
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DR   EMBL; PXOF01000236; RGP59100.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A395RG42; -.
DR   Proteomes; UP000266152; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProt.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   CDD; cd00029; C1; 1.
DR   Gene3D; 3.40.50.11500; -; 1.
DR   InterPro; IPR046349; C1-like_sf.
DR   InterPro; IPR001194; cDENN_dom.
DR   InterPro; IPR005112; dDENN_dom.
DR   InterPro; IPR043153; DENN_C.
DR   InterPro; IPR002219; PE/DAG-bd.
DR   InterPro; IPR037516; Tripartite_DENN.
DR   InterPro; IPR005113; uDENN_dom.
DR   PANTHER; PTHR12296:SF21; DENN DOMAIN-CONTAINING PROTEIN 3; 1.
DR   PANTHER; PTHR12296; DENN DOMAIN-CONTAINING PROTEIN 4; 1.
DR   Pfam; PF03455; dDENN; 1.
DR   Pfam; PF02141; DENN; 1.
DR   Pfam; PF03456; uDENN; 1.
DR   SMART; SM00801; dDENN; 1.
DR   SMART; SM00799; DENN; 1.
DR   SMART; SM00800; uDENN; 1.
DR   SUPFAM; SSF57889; Cysteine-rich domain; 1.
DR   PROSITE; PS50211; DENN; 1.
DR   PROSITE; PS50081; ZF_DAG_PE_2; 1.
PE   4: Predicted;
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000266152};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT   DOMAIN          243..1023
FT                   /note="UDENN"
FT                   /evidence="ECO:0000259|PROSITE:PS50211"
FT   DOMAIN          890..938
FT                   /note="Phorbol-ester/DAG-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50081"
FT   REGION          42..131
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          237..256
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          695..810
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        56..127
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        695..716
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        738..780
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        788..804
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1155 AA;  127796 MW;  A891907A630E502E CRC64;
     MESSSTPLAE YFWIAGVESV SYHDPSSQPA PVIVPVESTI IEDGEPEDEW TNGDQPKTNA
     RHSRQNSASR LSKMSLTERF SIQTLDDTDG NTKSNRSSAT IRAVNPPDFS NGSEDSNGNS
     QPSAPSGILG EGSMFMGDFD FDKALVKFAA EREVFLEDLT FSAGAKVQAR APMVNPRMER
     IRAEESDSGR LSPLRSIKGS IRRKMSFRDM NSVRKQPSNR ISTSRAASIR TTRRLSNYNS
     VIPPPEPLNT DPDMHPLKRR FEPVLLDRYP PQEAGDEISR RGRFPDYVPM FAFPNDIQIV
     SSDDRPRSTW HGFTMTSDDN SKLYGITIII WTALNADVAE DVEKKCEQWR QSHMSEEERE
     LAASLGVRLA GERTHLSQLL AKLPTIPSGS PARERLEDEI SAVEEKITLM TDMLRPLRHG
     AASKIEGLTA GESGLWVPRA YGILGRDAGN MSFWKEWLKA IVTPMTDGSV LRIPPSSPRV
     GRWQPLERYV VNLCTEAFNP LGSKTQVELG VRELRLYARK EADNEIPGSR TIDIYALFRC
     LSLENIVALF EYAMAESRII FLSSHTSMLH LACHALANLL YPLKWSSIFI PVLPARLLSA
     LEAPCPYIVG IERRYDNIEL PEDDYVLVDL DKDTIDATSQ PVRLPRQARR KLMSLLQVAA
     PHKLRYGVAT GPPPYAMESF PYDAFSTENG TLFRSSTPKS TLGKWVSQSS SGFGEPDPPN
     EIQPPIFNAF ASAHVENGKS DRPSTSKSGK TSPQSSVSPV SINFPPMPST PVSRSDSGFA
     LASTLREKRS GHFGEEKMRR SSSFGIDKHP PFQKPGMPFL NGHQANLSIS AISVESQNSV
     IGGANGGYGG GNGGYAPSTY AQSTLAASTI MPSMQIQPVR NTETTVWVEG HCFNYMPKDN
     TSMCTICNDL AEGDGVYRCT GCKIVSHGRC LGYCSLICPE AFHADRVRAA FVRCLASLLY
     TYRKYLGRPS KQQKSNGQLY AFDMDGFIKS LPHDQHDYAA MMRETQCFNE FIHDREMQPA
     NDASIRLFDE IIMAKKARGR SGLATGLSRL STLRASHGAS TYGGFGPPRG GSNSKIPAFL
     GDISDHIWRT ASVPLPKGNF PGEYRTIVTR TPARLDRSLM REPRSIQGMP RVEPRGTRGL
     IRKQVPNMFG TTPPT
//
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