ID T0QAP9_SAPDV Unreviewed; 745 AA.
AC T0QAP9;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 27-MAR-2024, entry version 39.
DE RecName: Full=FAD-binding FR-type domain-containing protein {ECO:0000259|PROSITE:PS51384};
GN ORFNames=SDRG_10545 {ECO:0000313|EMBL:EQC31756.1};
OS Saprolegnia diclina (strain VS20).
OC Eukaryota; Sar; Stramenopiles; Oomycota; Saprolegniales; Saprolegniaceae;
OC Saprolegnia.
OX NCBI_TaxID=1156394 {ECO:0000313|EMBL:EQC31756.1, ECO:0000313|Proteomes:UP000030762};
RN [1] {ECO:0000313|EMBL:EQC31756.1, ECO:0000313|Proteomes:UP000030762}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VS20 {ECO:0000313|EMBL:EQC31756.1,
RC ECO:0000313|Proteomes:UP000030762};
RG The Broad Institute Genome Sequencing Platform;
RA Russ C., Nusbaum C., Tyler B., van West P., Dieguez-Uribeondo J.,
RA de Bruijn I., Tripathy S., Jiang R., Young S.K., Zeng Q., Gargeya S.,
RA Fitzgerald M., Haas B., Abouelleil A., Alvarado L., Arachchi H.M.,
RA Berlin A., Chapman S.B., Goldberg J., Griggs A., Gujja S., Hansen M.,
RA Howarth C., Imamovic A., Larimer J., McCowen C., Montmayeur A., Murphy C.,
RA Neiman D., Pearson M., Priest M., Roberts A., Saif S., Shea T., Sisk P.,
RA Sykes S., Wortman J., Nusbaum C., Birren B.;
RT "The Genome Sequence of Saprolegnia declina VS20.";
RL Submitted (APR-2012) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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DR EMBL; JH767167; EQC31756.1; -; Genomic_DNA.
DR RefSeq; XP_008614763.1; XM_008616541.1.
DR AlphaFoldDB; T0QAP9; -.
DR STRING; 1156394.T0QAP9; -.
DR EnsemblProtists; EQC31756; EQC31756; SDRG_10545.
DR GeneID; 19951272; -.
DR VEuPathDB; FungiDB:SDRG_10545; -.
DR eggNOG; KOG0039; Eukaryota.
DR InParanoid; T0QAP9; -.
DR OMA; IHVGVAY; -.
DR OrthoDB; 63659at2759; -.
DR Proteomes; UP000030762; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016491; F:oxidoreductase activity; 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 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:SF69; METALLOREDUCTASE AIM14-RELATED; 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 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 Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000030762};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 27..51
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 99..120
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 163..182
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 203..226
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 294..313
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 325..344
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 592..611
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 631..649
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 369..472
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000259|PROSITE:PS51384"
SQ SEQUENCE 745 AA; 81810 MW; FD21D1A49E66E94D CRC64;
MADFAVVKTP QFDNETPTPT RTSSTALLLR LLVLLCLGIY IFGNIATWAP LFELQLINTM
TEWWNGYPNN GGSVVAGHHS KIIDTGIGRN ITISGHTEFV RPTFLFLFCI LPFFVGLLLI
EALGHPALAP RRATSSAFWR VAQWMRRKPS LFGSVSRYSL GEWLFGVVFV IGGNVLCFYY
EWDRRVDLAK AAAVSGKIST TKYWNMVGIS AAYLCIYNMA FLLLPVSRNS AWMEFMNISY
ANGARLHRWV GYMTVLTGVL HTGGYWGKWV RDGTWIANQS PCIECDFTNE TTGYFAWFNF
FGLVSIVAML LMIPTSIPIV RRKAYEWFYI SHWVLFVIAL FFAILHWTQI LWWILPSGLV
FLIGRACSSY NARSPVPATM RVIGGNIVQV VLAVQSDYLV GHFVYLNVPA ISKLQWHALT
VASSAKTSGA TTMTLLVKPV GDWSTKLLTY ANECGDAPVV FVDGFCGAAL DHVGDFPMAL
LVGGGIGVTP ILAVLEEMAH NVHATGTWAQ RVTLVFSARD LALFELLAPV LTKLRELDPQ
QTHFTSHLFL STLADDKALD APLTTSSSVA KPQGAMTGRP FRAPLQSRTT RAILYVVLFA
VAILALGAAH WGNGPIQGAN HYALWPLQRA FELAVFTATI LVVYVFLWAE ARDATQNATA
PVPSDDALPA TIATIRDLLL HLGVTVGTRP DVHALVANTV AKDCAENGVV GVIVSGPESL
KCAVNDAAVA LGAHRFDIHE EEFEL
//
