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Database: UniProt
Entry: A0A0P1AFY1_PLAHL
LinkDB: A0A0P1AFY1_PLAHL
Original site: A0A0P1AFY1_PLAHL 
ID   A0A0P1AFY1_PLAHL        Unreviewed;       715 AA.
AC   A0A0P1AFY1;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   27-MAR-2024, entry version 31.
DE   SubName: Full=Transmembrane protein {ECO:0000313|EMBL:CEG39551.1};
OS   Plasmopara halstedii (Downy mildew of sunflower).
OC   Eukaryota; Sar; Stramenopiles; Oomycota; Peronosporales; Peronosporaceae;
OC   Plasmopara.
OX   NCBI_TaxID=4781 {ECO:0000313|EMBL:CEG39551.1, ECO:0000313|Proteomes:UP000054928};
RN   [1] {ECO:0000313|Proteomes:UP000054928}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Sharma Rahul, Thines Marco;
RL   Submitted (SEP-2014) 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; CCYD01000428; CEG39551.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0P1AFY1; -.
DR   STRING; 4781.A0A0P1AFY1; -.
DR   EnsemblProtists; CEG39551; CEG39551; CEG39551.
DR   OMA; MSFSFQR; -.
DR   OrthoDB; 5489970at2759; -.
DR   Proteomes; UP000054928; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   CDD; cd09631; DOMON_DOH; 1.
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; IPR045266; DOH_DOMON.
DR   InterPro; IPR005018; DOMON_domain.
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:SF210; DOMON 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   SUPFAM; SSF52343; Ferredoxin reductase-like, C-terminal NADP-linked domain; 1.
DR   SUPFAM; SSF63380; Riboflavin synthase domain-like; 1.
DR   PROSITE; PS50836; DOMON; 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:UP000054928};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        196..217
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        260..280
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        292..312
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        324..341
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        361..381
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        388..405
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        411..429
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          25..145
FT                   /note="DOMON"
FT                   /evidence="ECO:0000259|PROSITE:PS50836"
FT   DOMAIN          432..541
FT                   /note="FAD-binding FR-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51384"
SQ   SEQUENCE   715 AA;  77191 MW;  C56AB3628822019B CRC64;
     MAVSNASICS SAAFQALSGT RLGDSPIFMR ALIQGDEVCI EYQLDASIAS SAAWFAVGPS
     RDSRMVSSPA SNVMMFFRNT GTPTSYLLGG YTNSDVTEES VASYVAGTAS TTDMSFSFQR
     TLAAASSSDV AISPTAATTY IWAYGTSWPI SSHRSGTNGA ATFNIAAAAT AGSSAASTSI
     SSSANAPWCD DKNCPAIVGG IAFAIMALCG LLLTAGLKSS PVGKLLLHRT IVHPPVKLTT
     NKPLAMPHTM IWQTLADLHL GELLVMLIFV AALVVLIVML DDENNYVVSG QVSLLILMFL
     ILPVARIPVW SVLFGSSFER IVKFHRWLGL AMTIAVVIHV IQANDVVSLT LDEKYGEVTP
     LYGFIAFICF VAMFFLSIEY IRRMFFEVFY YAHRVLSIVG FVFAILHAPK FIGRALIVPL
     GLYALGLLYR WMSALTGSYN ASVSVHSGSN STTLVLTSSP KTGKLAMKIN PGSYFFVRLP
     AVSAIQWHPF SAVVTPDGNS IGFTIKAMGN GSFTRKLLEK AGTQYELKAN LCGPFGKMSL
     DLEHYDVVVL VAGGVGITPM MSLINQTRLF PKATNPSNKA SKTTDWFVLW SVREAEDILM
     MEQFLPSNAQ LDYAAAVSIQ DPNTAILGNN VPTPFNVNWM FHVSNARSNG FVTRGNGETV
     SYRGGQPILD ELINTSRFNG RRVTVVACGP PTMTVEAQGL ARNCGFDFHK EVFNW
//
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