ID F2SFK3_TRIRC Unreviewed; 551 AA.
AC F2SFK3;
DT 31-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 31-MAY-2011, sequence version 1.
DT 27-MAR-2024, entry version 53.
DE RecName: Full=FAD-binding FR-type domain-containing protein {ECO:0000259|PROSITE:PS51384};
GN ORFNames=TERG_01191 {ECO:0000313|EMBL:EGD84918.1};
OS Trichophyton rubrum (strain ATCC MYA-4607 / CBS 118892) (Athlete's foot
OS fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Arthrodermataceae; Trichophyton.
OX NCBI_TaxID=559305 {ECO:0000313|EMBL:EGD84918.1, ECO:0000313|Proteomes:UP000008864};
RN [1] {ECO:0000313|Proteomes:UP000008864}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4607 / CBS 118892 {ECO:0000313|Proteomes:UP000008864};
RX PubMed=22951933; DOI=10.1128/mbio.00259-12;
RA Martinez D.A., Oliver B.G., Graeser Y., Goldberg J.M., Li W.,
RA Martinez-Rossi N.M., Monod M., Shelest E., Barton R.C., Birch E.,
RA Brakhage A.A., Chen Z., Gurr S.J., Heiman D., Heitman J., Kosti I.,
RA Rossi A., Saif S., Samalova M., Saunders C.W., Shea T., Summerbell R.C.,
RA Xu J., Young S., Zeng Q., Birren B.W., Cuomo C.A., White T.C.;
RT "Comparative genome analysis of Trichophyton rubrum and related
RT dermatophytes reveals candidate genes involved in infection.";
RL MBio 3:E259-E259(2012).
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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DR EMBL; GG700648; EGD84918.1; -; Genomic_DNA.
DR RefSeq; XP_003239209.1; XM_003239161.1.
DR AlphaFoldDB; F2SFK3; -.
DR STRING; 559305.F2SFK3; -.
DR GeneID; 10374114; -.
DR VEuPathDB; FungiDB:TERG_01191; -.
DR eggNOG; KOG0039; Eukaryota.
DR HOGENOM; CLU_005646_3_0_1; -.
DR InParanoid; F2SFK3; -.
DR OMA; FTFAKEH; -.
DR OrthoDB; 367877at2759; -.
DR Proteomes; UP000008864; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR GO; GO:0006811; P:monoatomic ion transport; IEA:UniProtKB-KW.
DR CDD; cd06186; NOX_Duox_like_FAD_NADP; 1.
DR Gene3D; 3.40.50.80; Nucleotide-binding domain of ferredoxin-NADP reductase (FNR) module; 1.
DR Gene3D; 2.40.30.10; Translation factors; 1.
DR InterPro; IPR013112; FAD-bd_8.
DR InterPro; IPR017927; FAD-bd_FR_type.
DR InterPro; IPR013130; Fe3_Rdtase_TM_dom.
DR InterPro; IPR013121; Fe_red_NAD-bd_6.
DR InterPro; IPR039261; FNR_nucleotide-bd.
DR InterPro; IPR017938; Riboflavin_synthase-like_b-brl.
DR PANTHER; PTHR11972:SF39; FAD-BINDING FR-TYPE DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR11972; NADPH OXIDASE; 1.
DR Pfam; PF08022; FAD_binding_8; 1.
DR Pfam; PF01794; Ferric_reduct; 1.
DR Pfam; PF08030; NAD_binding_6; 1.
DR SFLD; SFLDS00052; Ferric_Reductase_Domain; 1.
DR SFLD; SFLDG01168; Ferric_reductase_subgroup_(FRE; 1.
DR SFLD; SFLDG01169; NADPH_oxidase_subgroup_(NOX); 1.
DR SUPFAM; SSF52343; Ferredoxin reductase-like, C-terminal NADP-linked domain; 1.
DR SUPFAM; SSF63380; Riboflavin synthase domain-like; 1.
DR PROSITE; PS51384; FAD_FR; 1.
PE 4: Predicted;
KW Electron transport {ECO:0000256|ARBA:ARBA00022982};
KW Ion transport {ECO:0000256|ARBA:ARBA00023065};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000008864};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}; Transport {ECO:0000256|ARBA:ARBA00023065}.
FT TRANSMEM 18..37
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 57..81
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 102..120
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 140..161
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 173..192
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 242..365
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000259|PROSITE:PS51384"
SQ SEQUENCE 551 AA; 64060 MW; 6025015E3647F95D CRC64;
MTKKTSSKWK SHFNPSKLFF YFIFYGIQIG FFAYGWWKQA TDQRLAALNT LTFSVWMSRG
AGFVLSIDTA LILFPMCRTL LRYVRPKVKW LPLDEAQWFH RQIAYSLLIF SVIHVVAHYV
NFFNIERYQK RPEAAVQIHY TQAGGITGHV MLLCMLLMYT TSHHRIRQQS YETFWYTHHL
FIPFLLALYT HATGCFVRDT PDPISPFAGK KFWDHCIGYE GWRWELWGGG LYLIERLYRE
IRAARDTEIV KVVRHPYDAM EIQFRKPSLR YKPGQWLFLQ VPDVSRTQWH PFTITSCPHD
PYISIHIRQV GDFTRELGNR LGCGPEQAKD IDGLDPLGMY EIAMQNGQTM PQIRIDGPYG
APAEDVFSND VAILIGTGIG VTPWASILKD IWHYRAGPNP PTRLRRVEFI WICKDTSSFE
WFQALLSSLE AQSAEEARSG QEFLRIHTYL TQRFDQDTAA NIYLNSVGQE LDPLTELRTG
TKFGRPDFAR FFGALRSSIM DRTYMSNLEA TRRADVGVYF CGPNQAAKQV KKAAKECTSK
EVKFKFWKEH F
//
