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Database: UniProt
Entry: A0A367LLP9_9HYPO
LinkDB: A0A367LLP9_9HYPO
Original site: A0A367LLP9_9HYPO 
ID   A0A367LLP9_9HYPO        Unreviewed;       478 AA.
AC   A0A367LLP9;
DT   07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT   07-NOV-2018, sequence version 1.
DT   27-MAR-2024, entry version 19.
DE   SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:RCI15182.1};
GN   ORFNames=L249_6940 {ECO:0000313|EMBL:RCI15182.1};
OS   Ophiocordyceps polyrhachis-furcata BCC 54312.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Ophiocordycipitaceae; Ophiocordyceps.
OX   NCBI_TaxID=1330021 {ECO:0000313|EMBL:RCI15182.1, ECO:0000313|Proteomes:UP000253664};
RN   [1] {ECO:0000313|EMBL:RCI15182.1, ECO:0000313|Proteomes:UP000253664}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BCC 54312 {ECO:0000313|EMBL:RCI15182.1,
RC   ECO:0000313|Proteomes:UP000253664};
RX   PubMed=26511477; DOI=10.1186/s12864-015-2101-4;
RA   Wichadakul D., Kobmoo N., Ingsriswang S., Tangphatsornruang S.,
RA   Chantasingh D., Luangsa-ard J.J., Eurwilaichitr L.;
RT   "Insights from the genome of Ophiocordyceps polyrhachis-furcata to
RT   pathogenicity and host specificity in insect fungi.";
RL   BMC Genomics 16:881-881(2015).
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:RCI15182.1}.
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DR   EMBL; LKCN02000003; RCI15182.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A367LLP9; -.
DR   Proteomes; UP000253664; Unassembled WGS sequence.
DR   GO; GO:0005507; F:copper ion binding; IEA:InterPro.
DR   GO; GO:0006801; P:superoxide metabolic process; IEA:InterPro.
DR   Gene3D; 2.60.40.200; Superoxide dismutase, copper/zinc binding domain; 1.
DR   InterPro; IPR036423; SOD-like_Cu/Zn_dom_sf.
DR   InterPro; IPR024134; SOD_Cu/Zn_/chaperone.
DR   PANTHER; PTHR10003:SF37; CELL SURFACE SUPEROXIDE DISMUTASE [CU-ZN] 4; 1.
DR   PANTHER; PTHR10003; SUPEROXIDE DISMUTASE CU-ZN -RELATED; 1.
DR   SUPFAM; SSF49329; Cu,Zn superoxide dismutase-like; 1.
PE   4: Predicted;
KW   Reference proteome {ECO:0000313|Proteomes:UP000253664};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           19..478
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5016569981"
FT   REGION          115..144
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          191..230
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          394..429
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        191..217
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        402..429
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   478 AA;  49779 MW;  1A3AC93BAC6942A5 CRC64;
     MRAAVLATAS LSAGLVAAQG TQNAPVIKSN PSGATFEAQL PAQAFTAGSL DGNVRGSIVA
     STPADGVGVE FKVRFDNVPQ EGGPFLYHIH VNDVPSNGNC TSTLAHLDPY KRGEDVPCDS
     SRPETCQVGD LSGKHGKPNS TSSGSFSADY VDRFLSTSPE SNAFFGNRSF VFHFANKTRI
     TCANFKQVES GGSASNTGAA SSTASSPPNT PMGTGSVHGP SGSPVPFRGD ATMSTLSLPL
     TMLSVAGVMM TTENNAAEGE ARAGARGEWA GEAVVPDTVC PAYISSGVNA GQEVEVLERV
     KALVVPGEVR DAPCVLCLTG GLECWIQAGS TRAFLCAECA DDDDDYDAPG LSAVIRVFRG
     WEGRLAAVEA RVDAEAAAFR AELAAAAAKK KIKKNKKKKT TTKTPTTATP ATPTKNRRGA
     AATTTATPIT PTKTPQLFIY MRSEEISSEN IRWLVFCQDD YSEVGEAAQI AAEPVGLV
//
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