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Database: UniProt
Entry: J3KFZ3_COCIM
LinkDB: J3KFZ3_COCIM
Original site: J3KFZ3_COCIM 
ID   J3KFZ3_COCIM            Unreviewed;       456 AA.
AC   J3KFZ3;
DT   03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT   27-MAY-2015, sequence version 2.
DT   27-MAR-2024, entry version 48.
DE   RecName: Full=FAD-binding PCMH-type domain-containing protein {ECO:0000259|PROSITE:PS51387};
GN   ORFNames=CIMG_11581 {ECO:0000313|EMBL:EAS34594.3};
OS   Coccidioides immitis (strain RS) (Valley fever fungus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Onygenaceae; Coccidioides.
OX   NCBI_TaxID=246410 {ECO:0000313|EMBL:EAS34594.3, ECO:0000313|Proteomes:UP000001261};
RN   [1] {ECO:0000313|Proteomes:UP000001261}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RS {ECO:0000313|Proteomes:UP000001261};
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).
RN   [2] {ECO:0000313|Proteomes:UP000001261}
RP   GENOME REANNOTATION.
RC   STRAIN=RS {ECO:0000313|Proteomes:UP000001261};
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; GG704914; EAS34594.3; -; Genomic_DNA.
DR   RefSeq; XP_001246177.2; XM_001246176.2.
DR   AlphaFoldDB; J3KFZ3; -.
DR   GeneID; 24163784; -.
DR   KEGG; cim:CIMG_11581; -.
DR   VEuPathDB; FungiDB:CIMG_11581; -.
DR   InParanoid; J3KFZ3; -.
DR   OMA; VMPLAWY; -.
DR   OrthoDB; 1608525at2759; -.
DR   Proteomes; UP000001261; Unassembled WGS sequence.
DR   GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR   Gene3D; 3.30.465.10; -; 1.
DR   Gene3D; 3.40.462.20; -; 1.
DR   Gene3D; 3.30.43.10; Uridine Diphospho-n-acetylenolpyruvylglucosamine Reductase, domain 2; 1.
DR   InterPro; IPR016166; FAD-bd_PCMH.
DR   InterPro; IPR036318; FAD-bd_PCMH-like_sf.
DR   InterPro; IPR016167; FAD-bd_PCMH_sub1.
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:SF7; FAD-BINDING PCMH-TYPE DOMAIN-CONTAINING PROTEIN; 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:UP000001261}.
FT   DOMAIN          38..207
FT                   /note="FAD-binding PCMH-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51387"
SQ   SEQUENCE   456 AA;  50802 MW;  BE5F49974D3F9B9B CRC64;
     MTLDTFLSVI KTRLSERAEV LTGAFDSTFW EKRWSDDGFQ VPGAIVRPGC EDDVIQIVKY
     AKITSTPFAV ATGCHSPWSS IKKHGFIIDM SSYSTIDVDP TARTVKVRGG VLHKEFQAAL
     ARQGQCTVVG DAQNIGVIPY FIGGGISIFS GRFGFGSDNI LSGRIVTADG SLLHVSDNLN
     SDLFWALRGA GQFFGIVTEL TIRTYPLSLI GSEIGTHYFS RFFFPISKVR EVGAVMENII
     RNRSQPTAGH LMIMAQPPKF EQIIVVNAHY IGNPAAGAFS FKPLYDLGPM KLSCRKISFE
     NNGDEPLCKD SIRRFRRLNL SALDEFTTEK FVALASLHRE LITQCPDAEL TQVIIGWRAS
     GSSAPVTDTA FGNAGRLLWL NLLTWYGDVS SRAMVANFVA EATRIGRKGS AEDKYISYTN
     SNREDPLEWR YKGVERVRRL RELKQRWDPE SRFPKL
//
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