ID A0A369GYZ1_9HYPO Unreviewed; 888 AA.
AC A0A369GYZ1;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE RecName: Full=FAD-binding domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=CP533_6838 {ECO:0000313|EMBL:RDA90638.1};
OS Ophiocordyceps camponoti-saundersi (nom. inval.).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Ophiocordycipitaceae; Ophiocordyceps.
OX NCBI_TaxID=2039874 {ECO:0000313|EMBL:RDA90638.1, ECO:0000313|Proteomes:UP000253071};
RN [1] {ECO:0000313|EMBL:RDA90638.1, ECO:0000313|Proteomes:UP000253071}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BCC 79314 {ECO:0000313|EMBL:RDA90638.1,
RC ECO:0000313|Proteomes:UP000253071};
RA Kobmoo N., Wichadakul D., Arnamnart N., Rodriguez De La Vega R.C.,
RA Luangsa-Ard J.-J., Giraud T.;
RT "A genome scan of diversifying selection in the zombie-ant fungus
RT Ophiocordyceps unilateralis complex supports a role of enterotoxins in
RT coevolution and host-specificity.";
RL Submitted (OCT-2017) to the EMBL/GenBank/DDBJ databases.
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:RDA90638.1}.
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DR EMBL; PDHQ01000115; RDA90638.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A369GYZ1; -.
DR STRING; 2039874.A0A369GYZ1; -.
DR Proteomes; UP000253071; Unassembled WGS sequence.
DR GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR GO; GO:0046983; F:protein dimerization activity; IEA:InterPro.
DR CDD; cd17742; BRCT_CHS5_like; 1.
DR CDD; cd13945; Chs5_N; 1.
DR CDD; cd00063; FN3; 1.
DR Gene3D; 3.40.30.120; -; 1.
DR Gene3D; 3.40.50.10190; BRCT domain; 1.
DR Gene3D; 3.30.9.10; D-Amino Acid Oxidase, subunit A, domain 2; 1.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR InterPro; IPR001357; BRCT_dom.
DR InterPro; IPR036420; BRCT_dom_sf.
DR InterPro; IPR031673; Chs5_N.
DR InterPro; IPR002938; FAD-bd.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR031669; Fn3_2.
DR InterPro; IPR003961; FN3_dom.
DR InterPro; IPR036116; FN3_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR PANTHER; PTHR47351; CHITIN BIOSYNTHESIS PROTEIN CHS5; 1.
DR PANTHER; PTHR47351:SF1; CHITIN BIOSYNTHESIS PROTEIN CHS5; 1.
DR Pfam; PF16892; CHS5_N; 1.
DR Pfam; PF01494; FAD_binding_3; 1.
DR Pfam; PF16893; fn3_2; 1.
DR Pfam; PF12738; PTCB-BRCT; 1.
DR Pfam; PF21274; Rng_hyd_C; 1.
DR PRINTS; PR00420; RNGMNOXGNASE.
DR SMART; SM00292; BRCT; 1.
DR SUPFAM; SSF52113; BRCT domain; 1.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
DR SUPFAM; SSF49265; Fibronectin type III; 1.
DR PROSITE; PS50172; BRCT; 1.
DR PROSITE; PS50853; FN3; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 4: Predicted;
KW FAD {ECO:0000256|ARBA:ARBA00022827};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000253071}.
FT DOMAIN 638..732
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 726..814
FT /note="BRCT"
FT /evidence="ECO:0000259|PROSITE:PS50172"
FT REGION 822..888
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 825..839
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 856..877
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 888 AA; 97474 MW; D14780862BC52F61 CRC64;
MKHLDTEFLI VGCGPAGASL ACFLGSYGLT GIAISADSGT ADTPRAHITN MAAMECLRDI
GLDRDVDRVA SRHGCMEHTR WCQSMAGAEL ARVYSWGHDP QRMGDYERAS PCKPADVPQT
LLEPVLVQYA VHNGFRIRFD TKLLSLTVDD DDDNDIITAT VRDELSHTEY KIRTRYLFGA
DGARSLVVRE LGFPLRRKPG QGPAYNVLVK ADMSHLIGSR MGNLHWVIRP GDDDAVFTPM
AIVRMVRLWD EWLFILFARD NDAPAPSAEQ YRDRVRKLIG DDTPAEIVGT SKWQINDVVA
ETYSKGNVFC LGDAVHRHPP MNGLGSNTCI QDAYNLAWKL ALVHRGKADR SLLDTYQVER
QPVGSAVVAR ANRAFQDHFT LWDALGTNTS PDSKRAFEEL TEVSPAGQKR RQDFRRGVEQ
TTAEFHGLGI EMGQHYRSKA VYDADEPEPW KPTGRAAEDP VLYYEPSTYP GSRLPHVWLN
KACPTQPVST IDVAGHGRFV LLTGIGGEAW KEAARRVSAS LEVKIDAYSI GFRQDWEDVY
FDWERLRGVS ESGAVLVRPD RPVMLISLTV GKVDAGVTVL LTPDKRLIEF PSILLPPNIS
SGSIVDITVS QNTSKESAEE DKFRALQDRI YNSFGASEPA TPALRCRNAT QTSVVLEWDP
VQLATADLIS LSLYRNGQKA GNIPRPLAMH STKISGLAVD TGYTFHLVLR TSAGTRISEK
VSVRTHKMTD LSGITITTGI LPAAAREKLA LAVDRIGAKM ADSVRIDTTH FVTTEGRGPA
WEKAVESNIP VVRPEWVAAC ETNGRILGVT KFYLDAMRAG PPTEEHVVPP APPPKAPPVV
PPKDEEHEVA LRPKDGATNG TTTTTTGSGT GETASKLPDA ASFQEVEL
//
