ID A0A1Q9E6J7_SYMMI Unreviewed; 1179 AA.
AC A0A1Q9E6J7;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 22-FEB-2023, entry version 18.
DE SubName: Full=Dual oxidase 1 {ECO:0000313|EMBL:OLQ03043.1};
GN Name=Duox1 {ECO:0000313|EMBL:OLQ03043.1};
GN ORFNames=AK812_SmicGene14063 {ECO:0000313|EMBL:OLQ03043.1};
OS Symbiodinium microadriaticum (Dinoflagellate) (Zooxanthella
OS microadriatica).
OC Eukaryota; Sar; Alveolata; Dinophyceae; Suessiales; Symbiodiniaceae;
OC Symbiodinium.
OX NCBI_TaxID=2951 {ECO:0000313|EMBL:OLQ03043.1, ECO:0000313|Proteomes:UP000186817};
RN [1] {ECO:0000313|EMBL:OLQ03043.1, ECO:0000313|Proteomes:UP000186817}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCMP2467 {ECO:0000313|EMBL:OLQ03043.1,
RC ECO:0000313|Proteomes:UP000186817};
RA Aranda M., Li Y., Liew Y.J., Baumgarten S., Simakov O., Wilson M., Piel J.,
RA Ashoor H., Bougouffa S., Bajic V.B., Ryu T., Ravasi T., Bayer T.,
RA Micklem G., Kim H., Bhak J., Lajeunesse T.C., Voolstra C.R.;
RT "Genome analysis of coral dinoflagellate symbionts highlights evolutionary
RT adaptations to a symbiotic lifestyle.";
RL Submitted (FEB-2016) to the EMBL/GenBank/DDBJ databases.
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:OLQ03043.1}.
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DR EMBL; LSRX01000248; OLQ03043.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Q9E6J7; -.
DR OrthoDB; 2671609at2759; -.
DR Proteomes; UP000186817; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
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; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR Gene3D; 1.10.720.30; SAP domain; 1.
DR InterPro; IPR013112; FAD-bd_8.
DR InterPro; IPR017927; FAD-bd_FR_type.
DR InterPro; IPR039261; FNR_nucleotide-bd.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR017938; Riboflavin_synthase-like_b-brl.
DR InterPro; IPR003034; SAP_dom.
DR InterPro; IPR036361; SAP_dom_sf.
DR PANTHER; PTHR11972; NADPH OXIDASE; 1.
DR Pfam; PF08022; FAD_binding_8; 1.
DR Pfam; PF02037; SAP; 1.
DR PRINTS; PR00410; PHEHYDRXLASE.
DR SMART; SM00513; SAP; 1.
DR SUPFAM; SSF52343; Ferredoxin reductase-like, C-terminal NADP-linked domain; 1.
DR SUPFAM; SSF63380; Riboflavin synthase domain-like; 1.
DR SUPFAM; SSF68906; SAP domain; 1.
DR PROSITE; PS51384; FAD_FR; 1.
DR PROSITE; PS50800; SAP; 1.
PE 4: Predicted;
KW Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000186817};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 296..317
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 338..364
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 685..706
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 727..745
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 757..777
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 784..801
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 807..828
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 539..573
FT /note="SAP"
FT /evidence="ECO:0000259|PROSITE:PS50800"
FT DOMAIN 837..938
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000259|PROSITE:PS51384"
FT REGION 70..90
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 438..466
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1093..1112
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 438..453
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1093..1107
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1179 AA; 125083 MW; DF1182D0FAF34B55 CRC64;
MPRDLASVLM HSQGMGDHIE PAVSPSASMK MPVWSLLSSG QKLRRGPTRE GLLFFQILMK
LNVAPPGAGK TTAVSSERIG ESKVRGGPSG RIVVTEPRRV AARVEAVVVA LQRQVFSGFW
EAEMSERAAA VAALLGAVLV QVPLIHSPAR AAWCWPSEPP VCAVPTVANG KCVDDNNATL
TTLAPEGVCT PMCDDGYVLV GSCTQLQCPR SGPEPGCLQD LEDETWWAPC GFGTVCIENG
GSLGQPAWER FGNFRCLAEG SAELVGVARC DGVATATPPP EPEGLTDAEV LDYGTLGILG
GLIVVGLLGA AISYTAGGGV ARCMFMPGPM QWSPSNNFGI LAVLIALVGA CLLPQLPVSI
LILVPLDGLR PPLAEPAPEG VREVCGMCRK EVVRDPDASC VLGFVTDELE SEEDQRFALS
ALFGLRLGLS AAAQKARAAQ PSRQVSPVQD VTTSAAEDPL PGEKAGPGSF KDLLSVHRVL
AGSQPAPALG VSILILLPLA GLRPPLAEPA DMERKILDEI PATPPKDAED RGKASEEELG
SLKVPHLKAR LRELGQPVSG NKDTLQQRLR SALSLPPVEP PVLPPAPEPV AFQCTKCQMQ
KMEKPVAGAG RSICHSCWAL DKQLMSWNVN LADMMLQESI GEFYRKISEM RTGTRLKWRL
VKEKLLRHPL LSGAKRDAEP EPVKAMRSTG IAAGIAAMLT IMWSYFKGGV HDLVGMTREA
AWRIHTTIGT LTLILGVVHG AVAIAEKGSD IQQNAFWVVG MPAAVLMILG VVPAPFVSYD
KFKLLHFISL WGYIAALIHM FDHAISFQTI ASISVAVGNG VAMLAFIVQK VYTKAAHGKV
TVKTAELVNE SGGQHLFLTM SVPNFKFKAG QWAHLAVGKA SPVPHPFTLV PGETSDEVRI
FMKINRSGFT SKMAKLCSPD ATPPPMKLEG PYGRPSVPAP GMERTVFVLG GVGITPGLSL
AKAAAEAASG TKVAMYWALR SLELLNKSAP LLEPHLDADL SAIRLNGAGT QEGGSGMPLN
AKYGSEDIGA WLESVGGEYV KAGVKHAMVF ICGPPGLAEA AKAAAKRSAG GLAWHVHVEE
FLFLPSLGPC AGKTSQTAPT PGTDAENDGA NSIFIDPGWP HRKFIDSRKG LMIVVFVQAA
AKPQSEPTPT TAAENPARLA SLQWFGESSF VAYVRSVHW
//
