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Database: UniProt
Entry: D8RJR0_SELML
LinkDB: D8RJR0_SELML
Original site: D8RJR0_SELML 
ID   D8RJR0_SELML            Unreviewed;       913 AA.
AC   D8RJR0;
DT   05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2010, sequence version 1.
DT   27-MAR-2024, entry version 76.
DE   SubName: Full=Uncharacterized protein RHD2L5-2 {ECO:0000313|EMBL:EFJ27951.1};
GN   Name=RHD2L5-2 {ECO:0000313|EMBL:EFJ27951.1};
GN   ORFNames=SELMODRAFT_451606 {ECO:0000313|EMBL:EFJ27951.1};
OS   Selaginella moellendorffii (Spikemoss).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Lycopodiopsida; Selaginellales; Selaginellaceae; Selaginella.
OX   NCBI_TaxID=88036 {ECO:0000313|Proteomes:UP000001514};
RN   [1] {ECO:0000313|EMBL:EFJ27951.1, ECO:0000313|Proteomes:UP000001514}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=21551031; DOI=10.1126/science.1203810;
RA   Banks J.A., Nishiyama T., Hasebe M., Bowman J.L., Gribskov M.,
RA   dePamphilis C., Albert V.A., Aono N., Aoyama T., Ambrose B.A., Ashton N.W.,
RA   Axtell M.J., Barker E., Barker M.S., Bennetzen J.L., Bonawitz N.D.,
RA   Chapple C., Cheng C., Correa L.G., Dacre M., DeBarry J., Dreyer I.,
RA   Elias M., Engstrom E.M., Estelle M., Feng L., Finet C., Floyd S.K.,
RA   Frommer W.B., Fujita T., Gramzow L., Gutensohn M., Harholt J., Hattori M.,
RA   Heyl A., Hirai T., Hiwatashi Y., Ishikawa M., Iwata M., Karol K.G.,
RA   Koehler B., Kolukisaoglu U., Kubo M., Kurata T., Lalonde S., Li K., Li Y.,
RA   Litt A., Lyons E., Manning G., Maruyama T., Michael T.P., Mikami K.,
RA   Miyazaki S., Morinaga S., Murata T., Mueller-Roeber B., Nelson D.R.,
RA   Obara M., Oguri Y., Olmstead R.G., Onodera N., Petersen B.L., Pils B.,
RA   Prigge M., Rensing S.A., Riano-Pachon D.M., Roberts A.W., Sato Y.,
RA   Scheller H.V., Schulz B., Schulz C., Shakirov E.V., Shibagaki N.,
RA   Shinohara N., Shippen D.E., Soerensen I., Sotooka R., Sugimoto N.,
RA   Sugita M., Sumikawa N., Tanurdzic M., Theissen G., Ulvskov P., Wakazuki S.,
RA   Weng J.K., Willats W.W., Wipf D., Wolf P.G., Yang L., Zimmer A.D., Zhu Q.,
RA   Mitros T., Hellsten U., Loque D., Otillar R., Salamov A., Schmutz J.,
RA   Shapiro H., Lindquist E., Lucas S., Rokhsar D., Grigoriev I.V.;
RT   "The Selaginella genome identifies genetic changes associated with the
RT   evolution of vascular plants.";
RL   Science 332:960-963(2011).
CC   -!- SIMILARITY: Belongs to the RBOH (TC 5.B.1.3) family.
CC       {ECO:0000256|ARBA:ARBA00007975}.
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DR   EMBL; GL377581; EFJ27951.1; -; Genomic_DNA.
DR   RefSeq; XP_002971353.1; XM_002971307.1.
DR   AlphaFoldDB; D8RJR0; -.
DR   EnsemblPlants; EFJ27951; EFJ27951; SELMODRAFT_451606.
DR   Gramene; EFJ27951; EFJ27951; SELMODRAFT_451606.
DR   KEGG; smo:SELMODRAFT_451606; -.
DR   eggNOG; KOG0039; Eukaryota.
DR   HOGENOM; CLU_005646_6_0_1; -.
DR   InParanoid; D8RJR0; -.
DR   OMA; RCSHIND; -.
DR   Proteomes; UP000001514; Unassembled WGS sequence.
DR   GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   GO; GO:0016174; F:NAD(P)H oxidase H2O2-forming activity; IBA:GO_Central.
DR   GO; GO:0004601; F:peroxidase activity; IEA:UniProtKB-KW.
DR   CDD; cd00051; EFh; 1.
DR   CDD; cd06186; NOX_Duox_like_FAD_NADP; 1.
DR   Gene3D; 1.10.238.10; EF-hand; 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; IPR011992; EF-hand-dom_pair.
DR   InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR   InterPro; IPR002048; EF_hand_dom.
DR   InterPro; IPR013112; FAD-bd_8.
DR   InterPro; IPR017927; FAD-bd_FR_type.
DR   InterPro; IPR013121; Fe_red_NAD-bd_6.
DR   InterPro; IPR039261; FNR_nucleotide-bd.
DR   InterPro; IPR013623; NADPH_Ox.
DR   InterPro; IPR017938; Riboflavin_synthase-like_b-brl.
DR   PANTHER; PTHR11972; NADPH OXIDASE; 1.
DR   PANTHER; PTHR11972:SF153; RESPIRATORY BURST OXIDASE HOMOLOG PROTEIN F; 1.
DR   Pfam; PF08022; FAD_binding_8; 1.
DR   Pfam; PF08030; NAD_binding_6; 1.
DR   Pfam; PF08414; NADPH_Ox; 1.
DR   PRINTS; PR00466; GP91PHOX.
DR   SFLD; SFLDG01169; NADPH_oxidase_subgroup_(NOX); 1.
DR   SUPFAM; SSF47473; EF-hand; 1.
DR   SUPFAM; SSF52343; Ferredoxin reductase-like, C-terminal NADP-linked domain; 1.
DR   SUPFAM; SSF63380; Riboflavin synthase domain-like; 1.
DR   PROSITE; PS00018; EF_HAND_1; 1.
DR   PROSITE; PS50222; EF_HAND_2; 1.
DR   PROSITE; PS51384; FAD_FR; 1.
PE   3: Inferred from homology;
KW   Calcium {ECO:0000256|ARBA:ARBA00022837};
KW   Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW   Membrane {ECO:0000256|SAM:Phobius}; NADP {ECO:0000256|ARBA:ARBA00022857};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00022559};
KW   Peroxidase {ECO:0000256|ARBA:ARBA00022559};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001514};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        360..379
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        492..522
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        542..566
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          238..273
FT                   /note="EF-hand"
FT                   /evidence="ECO:0000259|PROSITE:PS50222"
FT   DOMAIN          596..719
FT                   /note="FAD-binding FR-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51384"
FT   REGION          114..134
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        114..132
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   913 AA;  104278 MW;  842DBA956BEA0A03 CRC64;
     MEVCPKSPGD EDNVDESRML ELTIDVRDDN VRVRSVSALD DRCDDPQPSG RITLASLLRH
     TTQSGRFISK QISQELELIR NWAASTPRSR SRSRPSSPDR DRLVKILALS RSNSAVSSRS
     SASQQQPRIR KQQSGDLFLA RSRSGAETAL QGLRYISRAI ESADQKAVWE AVEMRFQQLA
     KPDGMLDRGD FGLCIGMPDS REFTGELFDA LARRKHQNLQ CINKEELYEF WLQLSDQSFD
     SRIQIFFDMC DKDADGRITE EEVKEIIILS ASANKLSKLN EQAEEYAALI MEELDPSGIG
     YIELWQLESL MLGQFASLAQ DGYLNYSQTW SQTLAFEQSG KIILCARKIK YFVIENWQRV
     WVVGLWIFAM CGLFLWKFFA YKQTSAFKLL GYCLCSAKGA AETLKLNMAL VLLPVCRNTI
     TWLRSTIVGS VVPFDDSLNF HKASIIAGAI VAGVGIHATV HLACDFPRII RASEEEFMIY
     LGRGFHYKQP TYVGILVSIE GVTGISMVIM MSIAFVLATR WFRRNLVRLP WPLHRLTGFN
     AFWYSHHLFM VVYVLLLLHS IFLFFTNDWV AKSTWMYLSV PVLLYSVERI LSAFRARHFT
     VQVVKAAIHP GNVLALKMTK PPTFKYKSGM YLFIKCISIS PFEWHPFSIT SAPSDRHLSV
     HIRTVGDWTE ELRRIFSKAL GGLAEKENVL ESESSDISII RHRFPKLQID GPYGAPAQDY
     QKYDVLLLVG IGIGATPFIS VLKDMLNQIK LADQQQFLSM KQIRSPRKRN ERKLQCPTNA
     YFYWVTREQG SFEWFRGVLN EVAEIDNKAV IEMHNYLTSV YEEGDARSAL ITMMQAFHHA
     KNGVDIVSGT RVRTHFARPK WYKVFSRLAN IHTNSRIGVF YCGPMVLARE LDALSSEFNQ
     ISNSKFEFHK ENF
//
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