ID   C5P1T9_COCP7            Unreviewed;       470 AA.
AC   C5P1T9;
DT   01-SEP-2009, integrated into UniProtKB/TrEMBL.
DT   01-SEP-2009, sequence version 1.
DT   27-MAR-2024, entry version 55.
DE   SubName: Full=FAD binding domain containing protein {ECO:0000313|EMBL:EER29647.1};
GN   ORFNames=CPC735_073290 {ECO:0000313|EMBL:EER29647.1};
OS   Coccidioides posadasii (strain C735) (Valley fever fungus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Onygenaceae; Coccidioides.
OX   NCBI_TaxID=222929 {ECO:0000313|EMBL:EER29647.1, ECO:0000313|Proteomes:UP000009084};
RN   [1] {ECO:0000313|EMBL:EER29647.1, ECO:0000313|Proteomes:UP000009084}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C735 {ECO:0000313|Proteomes:UP000009084};
RX   PubMed=19717792; DOI=10.1101/gr.087551.108;
RA   Sharpton T.J., Stajich J.E., Rounsley S.D., Gardner M.J., Wortman J.R.,
RA   Jordar V.S., Maiti R., Kodira C.D., Neafsey D.E., Zeng Q., Hung C.-Y.,
RA   McMahan C., Muszewska A., Grynberg M., Mandel M.A., Kellner E.M.,
RA   Barker B.M., Galgiani J.N., Orbach M.J., Kirkland T.N., Cole G.T.,
RA   Henn M.R., Birren B.W., Taylor J.W.;
RT   "Comparative genomic analyses of the human fungal pathogens Coccidioides
RT   and their relatives.";
RL   Genome Res. 19:1722-1731(2009).
CC   -!- SIMILARITY: Belongs to the paxM FAD-dependent monooxygenase family.
CC       {ECO:0000256|ARBA:ARBA00007992}.
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:EER29647.1}.
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DR   EMBL; ACFW01000009; EER29647.1; -; Genomic_DNA.
DR   RefSeq; XP_003071792.1; XM_003071746.1.
DR   AlphaFoldDB; C5P1T9; -.
DR   GeneID; 9697286; -.
DR   KEGG; cpw:CPC735_073290; -.
DR   VEuPathDB; FungiDB:CPC735_073290; -.
DR   HOGENOM; CLU_009665_18_0_1; -.
DR   OrthoDB; 2163350at2759; -.
DR   Proteomes; UP000009084; Unassembled WGS sequence.
DR   GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 1.
DR   InterPro; IPR002938; FAD-bd.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   PANTHER; PTHR13789; MONOOXYGENASE; 1.
DR   PANTHER; PTHR13789:SF261; SALICYLATE HYDROXYLASE_MONOOXYGENASE, PUTATIVE (AFU_ORTHOLOGUE AFUA_4G13860)-RELATED; 1.
DR   Pfam; PF01494; FAD_binding_3; 1.
DR   PRINTS; PR00420; RNGMNOXGNASE.
DR   SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
PE   3: Inferred from homology;
KW   FAD {ECO:0000256|ARBA:ARBA00022827};
KW   Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002}.
FT   DOMAIN          169..369
FT                   /note="FAD-binding"
FT                   /evidence="ECO:0000259|Pfam:PF01494"
SQ   SEQUENCE   470 AA;  52187 MW;  84C432F67C3C6CAE CRC64;
     MKIAIVGGGI SGCAIYLALK KRLPQPPASM AEHEFVIFES YDTTRNLASQ HAPGDTHSAS
     LIVGGGIGLH PNGVRSLERL NEDLARDVKL AGHCFNVQKF MSSYGRELAR LPCSSEDTYS
     ISLSRHALWS CLRNYVPDDL IVTKRVTQVI ANSNGRSVIQ FADGSPDEEA DLVIGADGLK
     SPTRRALFPE AKEDPYPPEF AGLVGVGGVV QGEEFKSLVE PCTINFVFGR NGFFGYSFVQ
     SLTNPSEYIS STSQSKTTPS DTVMWWSTYE MESCPDPRAV DKEAILRDLH NRLDTWKDPI
     IQKILGTVNI QTIFPVNTTP ELPTWTRDGV IVIGDAAHTL TPTSGQGTCQ ALEDVECFSM
     LLSHFLNKTY DSLSDPSAAA LARIERETIA QVMQKHMEIR KPRVHAIQEK GKQFDQKKKN
     LGRVAEFMMY FGLFIMGKLP MPSWMTGLWT YDIANEVNYE ISKMEAENHH
//