ID A0A369H3J6_9HYPO Unreviewed; 630 AA.
AC A0A369H3J6;
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:0000259|Pfam:PF01494};
GN ORFNames=CP533_1479 {ECO:0000313|EMBL:RDA89613.1};
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:RDA89613.1, ECO:0000313|Proteomes:UP000253071};
RN [1] {ECO:0000313|EMBL:RDA89613.1, ECO:0000313|Proteomes:UP000253071}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BCC 79314 {ECO:0000313|EMBL:RDA89613.1,
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 -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
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:RDA89613.1}.
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DR EMBL; PDHQ01000348; RDA89613.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A369H3J6; -.
DR STRING; 2039874.A0A369H3J6; -.
DR Proteomes; UP000253071; Unassembled WGS sequence.
DR GO; GO:0005751; C:mitochondrial respiratory chain complex IV; IEA:InterPro.
DR GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR GO; GO:0004497; F:monooxygenase activity; IEA:UniProtKB-KW.
DR GO; GO:0006123; P:mitochondrial electron transport, cytochrome c to oxygen; IEA:InterPro.
DR CDD; cd00922; Cyt_c_Oxidase_IV; 1.
DR Gene3D; 1.10.442.10; Cytochrome c oxidase subunit IV; 1.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 1.
DR InterPro; IPR004203; Cyt_c_oxidase_su4_fam.
DR InterPro; IPR036639; Cyt_c_oxidase_su4_sf.
DR InterPro; IPR002938; FAD-bd.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR PANTHER; PTHR46028; KYNURENINE 3-MONOOXYGENASE; 1.
DR PANTHER; PTHR46028:SF2; KYNURENINE 3-MONOOXYGENASE; 1.
DR Pfam; PF02936; COX4; 1.
DR Pfam; PF01494; FAD_binding_3; 1.
DR PRINTS; PR00420; RNGMNOXGNASE.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
DR SUPFAM; SSF81406; Mitochondrial cytochrome c oxidase subunit IV; 1.
PE 4: Predicted;
KW FAD {ECO:0000256|ARBA:ARBA00022827};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW Mitochondrion {ECO:0000256|ARBA:ARBA00023128};
KW Monooxygenase {ECO:0000256|ARBA:ARBA00023033};
KW NADP {ECO:0000256|ARBA:ARBA00022857};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000253071}.
FT DOMAIN 81..331
FT /note="FAD-binding"
FT /evidence="ECO:0000259|Pfam:PF01494"
FT REGION 588..630
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 588..602
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 630 AA; 71294 MW; FA751360ECFB5C92 CRC64;
MPLEEAIKLK YMSFGQRGTI PLNFTKSINL AVSERGINAM RLAGHPTLLE TVMDGTIPMR
GRMIHGKSPL GETYEHSQDY DVKGRVIYAI DRSGLNSRLL DVLDSLPNVR LFFNHKLTGA
DFGTCRAWIE ARDEGDSSNG RPREIEVSFD LMIGADGAHS AVRYHLMKFS RMDYRQEYID
TLWCEFRIEP KTSDQDDPNT SFQISPNHLH IWPGKQFMFI AIPSKDGSFT CTLFLSSKQF
ADLEADPSTL PAFFDAQFPG VTSLIPRESL ETSFRDNPHL PLISLKCRPY HHASSGVFIG
DAAHAMVPFY GQGMNAGMED VHILFSTFDK YTEYREGHPL AMSAHQRSQA LAEYSAKREP
DAHAINDLSL QNYIEMRSSV LSKRYRIRKF LEEFVSDNFP SIGWHTRYSR VSFSNEPYSE
IVRQSEHQGN LLMRSFVGFS FALAFAPIDI IRPAMDFPRC SKLLRTRLFS NSCKRLVVLS
SPISRASSSH AISKPTLANI EKRWEGMPLQ EQADLWMALR DRMKGDWNDL TIQEKKAAYW
IAFGPHGPRA VDPPGTNARI AWTVVKGLVA SFVIFAIIRS FAKPEPHTMS REYQEASNEM
LKRQKADPIT GISSEGYTGR GQIQSPPKGH
//