ID A0A1V9Z6R1_9STRA Unreviewed; 764 AA.
AC A0A1V9Z6R1;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE SubName: Full=Ferric reductase {ECO:0000313|EMBL:OQR93685.1};
GN ORFNames=ACHHYP_02351 {ECO:0000313|EMBL:OQR93685.1};
OS Achlya hypogyna.
OC Eukaryota; Sar; Stramenopiles; Oomycota; Saprolegniales; Saprolegniaceae;
OC Achlya.
OX NCBI_TaxID=1202772 {ECO:0000313|EMBL:OQR93685.1, ECO:0000313|Proteomes:UP000243579};
RN [1] {ECO:0000313|EMBL:OQR93685.1, ECO:0000313|Proteomes:UP000243579}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 48635 {ECO:0000313|EMBL:OQR93685.1,
RC ECO:0000313|Proteomes:UP000243579};
RX PubMed=25527045; DOI=10.1093/gbe/evu276;
RA Misner I., Blouin N., Leonard G., Richards T.A., Lane C.E.;
RT "The secreted proteins of Achlya hypogyna and Thraustotheca clavata
RT identify the ancestral oomycete secretome and reveal gene acquisitions by
RT horizontal gene transfer.";
RL Genome Biol. Evol. 7:120-135(2014).
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OQR93685.1}.
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DR EMBL; JNBR01000399; OQR93685.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1V9Z6R1; -.
DR STRING; 1202772.A0A1V9Z6R1; -.
DR OrthoDB; 367877at2759; -.
DR Proteomes; UP000243579; 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 Gene3D; 2.40.30.10; Translation factors; 1.
DR InterPro; IPR000778; Cyt_b245_heavy_chain.
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 PRINTS; PR00466; GP91PHOX.
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 Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000243579};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 397..418
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 430..449
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 479..583
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000259|PROSITE:PS51384"
SQ SEQUENCE 764 AA; 84753 MW; E60F7555C151A4E6 CRC64;
MRTGSRGALN NTSFLSNSSF VKNASFASVN SFGNNTSFVS TTSDVVMLQP DEADDSDVDD
EGAKKAEEGC VAINRPDDPI EQFEALKRVV ASVADAKGNI NRATFVTTFE MDLPVSSIRG
CSVLLSAAME LPVADDTKLK ILFDTMDAVG SGMIERSHIA DLFKTKFQAE KLQCVGSDFN
AMADMLFAKA GARSQEFMTF AQFALVFRGY LHEATATVET TPEPRQELKS SPLPARWSLA
RARRFYHHHA LRIWWLTAYV IFIGYEGISK AAQYPVDSAT GWALRIARGA AQVAMPNFLL
ALLPMCRSIV EVLKQSKILW RIVPFDDLLA FHRIAGTVAL VAGLVHTGAH VANEAAVYLI
ATPDEIARSF LVAHVSPLRA ADGTPLMLPF SHMLCTLPIV TGVVMLAIAL VVLPTALLPR
FRQGRFNLFW FSHMLLGPFL LLGCIHGATS WLSKAQSYLW IAPPLAIYLI ERRFRFAKSW
TTPLRIERVE FLDGVVALFM EKPTRFEYTP GMYTFLNVPA LSQHEWHPFT ISSAPDDAHV
SLHIRNAGDW TGALHTLLAQ CNSEGKPFPV VHLDGPVGAP TQAYHRYSTV VMIGGGIGVT
PFASILKDTV HKWNAMRCPN CAHCRAPPGT KLRKMYFHWV TRQQEALQWF RNTMDEIHAM
DRDGVIETHH HLTSVKANET LKLFQAFVHD TTGKDVVSGL KQLTHFGRPD WDHWFGAMAA
AHPGERIGVF FCGPHPLDAV LSAMCRKYST AQATTFEYHS EKFA
//
