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Database: UniProt
Entry: A0A0J8RZ39_COCIT
LinkDB: A0A0J8RZ39_COCIT
Original site: A0A0J8RZ39_COCIT 
ID   A0A0J8RZ39_COCIT        Unreviewed;       496 AA.
AC   A0A0J8RZ39;
DT   14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT   14-OCT-2015, sequence version 1.
DT   27-MAR-2024, entry version 29.
DE   SubName: Full=FAD binding domain-containing protein {ECO:0000313|EMBL:KMU89434.1};
GN   ORFNames=CIHG_07241 {ECO:0000313|EMBL:KMU89434.1};
OS   Coccidioides immitis H538.4.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Onygenaceae; Coccidioides.
OX   NCBI_TaxID=396776 {ECO:0000313|EMBL:KMU89434.1, ECO:0000313|Proteomes:UP000054563};
RN   [1] {ECO:0000313|Proteomes:UP000054563}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=H538.4 {ECO:0000313|Proteomes:UP000054563};
RX   PubMed=20516208; DOI=10.1101/gr.103911.109;
RA   Neafsey D.E., Barker B.M., Sharpton T.J., Stajich J.E., Park D.J.,
RA   Whiston E., Hung C.-Y., McMahan C., White J., Sykes S., Heiman D.,
RA   Young S., Zeng Q., Abouelleil A., Aftuck L., Bessette D., Brown A.,
RA   FitzGerald M., Lui A., Macdonald J.P., Priest M., Orbach M.J.,
RA   Galgiani J.N., Kirkland T.N., Cole G.T., Birren B.W., Henn M.R.,
RA   Taylor J.W., Rounsley S.D.;
RT   "Population genomic sequencing of Coccidioides fungi reveals recent
RT   hybridization and transposon control.";
RL   Genome Res. 20:938-946(2010).
CC   -!- SIMILARITY: Belongs to the oxygen-dependent FAD-linked oxidoreductase
CC       family. {ECO:0000256|ARBA:ARBA00005466}.
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DR   EMBL; DS017012; KMU89434.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0J8RZ39; -.
DR   STRING; 396776.A0A0J8RZ39; -.
DR   VEuPathDB; FungiDB:CIHG_07241; -.
DR   eggNOG; KOG1231; Eukaryota.
DR   Proteomes; UP000054563; Unassembled WGS sequence.
DR   GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR   Gene3D; 3.30.465.10; -; 1.
DR   InterPro; IPR016166; FAD-bd_PCMH.
DR   InterPro; IPR036318; FAD-bd_PCMH-like_sf.
DR   InterPro; IPR016169; FAD-bd_PCMH_sub2.
DR   InterPro; IPR006094; Oxid_FAD_bind_N.
DR   PANTHER; PTHR42973; BINDING OXIDOREDUCTASE, PUTATIVE (AFU_ORTHOLOGUE AFUA_1G17690)-RELATED; 1.
DR   PANTHER; PTHR42973:SF54; FAD-BINDING PCMH-TYPE DOMAIN-CONTAINING PROTEIN-RELATED; 1.
DR   Pfam; PF01565; FAD_binding_4; 1.
DR   SUPFAM; SSF56176; FAD-binding/transporter-associated domain-like; 1.
DR   PROSITE; PS51387; FAD_PCMH; 1.
PE   3: Inferred from homology;
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000054563};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           22..496
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5005308397"
FT   DOMAIN          59..229
FT                   /note="FAD-binding PCMH-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51387"
SQ   SEQUENCE   496 AA;  54239 MW;  1AB1800146FD253A CRC64;
     MISSTLIATV ACGAFASLVR AAPPQECCSI LSKALPMNVF ASGSSTWEFE NKDYWSSTAV
     LDPNCVFLPD TTARVSEAVT LLGENECKFA VKGAGHSAIP GAANIHDGIM MSLAWLNSSD
     VHLEDNYIRV GAGQPLGNVF EALDPHNVGA VIGRFSKVGL GMGVGAGVSF FSNREGLMID
     NILNYEVVIA SGEVVNANAT SNPDLFWALK GGNNNFGVVT HYDLSIFKTT GLYGGQVTYP
     ETSLDQLADV IYDYHVHQAV DDVNTHALPQ YAFDGNSNET SATILVAYND AVDELPEIMQ
     PWLKVPHSKS TLKRRTYGDL ATELNDGFPN GLVQEQRVFT VYADEQFYKD VWFKYRQWLQ
     KYKDVPGFFG SHAKMPITPR QIEEGVKKGG NALGLEKGPQ DKTLGIIYFG VTFNNPEDAP
     DVFPAHKEFV ESMIEFAKSR KVLHPLIMLT FSAYDQPAIA SYGDENVAKL HEVAKKYDPK
     GVFQRLVPGG QKLPAQ
//
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