ID F1A617_DICPU Unreviewed; 711 AA.
AC F1A617;
DT 03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 03-MAY-2011, sequence version 1.
DT 24-JAN-2024, entry version 70.
DE RecName: Full=Superoxide-generating NADPH oxidase flavocytochrome {ECO:0008006|Google:ProtNLM};
GN ORFNames=DICPUDRAFT_51890 {ECO:0000313|EMBL:EGC28364.1};
OS Dictyostelium purpureum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=5786 {ECO:0000313|EMBL:EGC28364.1, ECO:0000313|Proteomes:UP000001064};
RN [1] {ECO:0000313|Proteomes:UP000001064}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=QSDP1 {ECO:0000313|Proteomes:UP000001064};
RX PubMed=21356102; DOI=10.1186/gb-2011-12-2-r20;
RG US DOE Joint Genome Institute (JGI-PGF);
RA Sucgang R., Kuo A., Tian X., Salerno W., Parikh A., Feasley C.L., Dalin E.,
RA Tu H., Huang E., Barry K., Lindquist E., Shapiro H., Bruce D., Schmutz J.,
RA Salamov A., Fey P., Gaudet P., Anjard C., Babu M.M., Basu S.,
RA Bushmanova Y., van der Wel H., Katoh-Kurasawa M., Dinh C., Coutinho P.M.,
RA Saito T., Elias M., Schaap P., Kay R.R., Henrissat B., Eichinger L.,
RA Rivero F., Putnam N.H., West C.M., Loomis W.F., Chisholm R.L., Shaulsky G.,
RA Strassmann J.E., Queller D.C., Kuspa A., Grigoriev I.V.;
RT "Comparative genomics of the social amoebae Dictyostelium discoideum and
RT Dictyostelium purpureum.";
RL Genome Biol. 12:R20.1-R20.23(2011).
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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DR EMBL; GL871663; EGC28364.1; -; Genomic_DNA.
DR RefSeq; XP_003295111.1; XM_003295063.1.
DR AlphaFoldDB; F1A617; -.
DR STRING; 5786.F1A617; -.
DR EnsemblProtists; EGC28364; EGC28364; DICPUDRAFT_51890.
DR GeneID; 10511140; -.
DR KEGG; dpp:DICPUDRAFT_51890; -.
DR eggNOG; KOG0039; Eukaryota.
DR InParanoid; F1A617; -.
DR OMA; ENETHEQ; -.
DR OrthoDB; 4186at2759; -.
DR Proteomes; UP000001064; Unassembled WGS sequence.
DR GO; GO:0043020; C:NADPH oxidase complex; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0016175; F:superoxide-generating NAD(P)H oxidase activity; IBA:GO_Central.
DR GO; GO:0006952; P:defense response; IBA:GO_Central.
DR GO; GO:0042742; P:defense response to bacterium; IEA:EnsemblProtists.
DR GO; GO:0030587; P:sorocarp development; IEA:EnsemblProtists.
DR GO; GO:0030435; P:sporulation resulting in formation of a cellular spore; IEA:EnsemblProtists.
DR GO; GO:0042554; P:superoxide anion generation; IBA:GO_Central.
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; 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; 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; NADPH OXIDASE; 1.
DR PANTHER; PTHR11972:SF201; SUPEROXIDE-GENERATING NADPH OXIDASE HEAVY CHAIN SUBUNIT C; 1.
DR Pfam; PF13499; EF-hand_7; 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 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; 2.
DR PROSITE; PS51384; FAD_FR; 1.
PE 4: Predicted;
KW Calcium {ECO:0000256|ARBA:ARBA00022837};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW NADP {ECO:0000256|ARBA:ARBA00022857};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000001064};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 163..184
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 204..228
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 248..273
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 293..319
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 331..354
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 32..67
FT /note="EF-hand"
FT /evidence="ECO:0000259|PROSITE:PS50222"
FT DOMAIN 76..111
FT /note="EF-hand"
FT /evidence="ECO:0000259|PROSITE:PS50222"
FT DOMAIN 375..506
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000259|PROSITE:PS51384"
FT REGION 109..144
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 109..130
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 711 AA; 83463 MW; 53CED989A8A1AFC2 CRC64;
MKKLKSVDFS IFKINLFDLI NQIYLNLSKI GTEDEKISSV FNLYDIYNKG FISRNDLKEV
LLYRTNQNGL KLSDFTLESL MDHIFEQFDK NADGFIDFNE FKQELKNNDN ENKSKYNKGD
IEMNKVEENE NENENENENE IEGEENSSKY NIKRYFKIEG SKLFFMALFL IVNITILIYS
FFLVHDKNQK AIQLFGPGLY ITRVAAQLIE FNAAMILITM CKQLFTMVRN TRFRGLFPVD
KYMTFHKLIG YTLLVASLLH TIGWIVGMAI ATGKPDALFY DCLYPHFEYR PTVWQMIFNS
LPGVTGVIMI LIIIIMCTLA IKTIRKSNFE LFYYSHHLFI GFYVLLILHG TMGWIRPPTF
WKWFIGPGFL YAVDRGFRLF KKTYKVNVVD FSLKNERVIN LTFSKPSSFN YKPGQYLLIN
IPQISRLQWH PFTMTSSPLE ENVHVHIRVT GGWTRKLFKW LSNIKQERER RINSGETTID
AIEIEMEKEK PIQIHIDGPF GSSSQYALNQ RQVILVGAGI GVAPMASLLQ DITMKKEKVY
NEDSITKQEN ETHEQHLERF NEIKRKHGLG ELEKVHFFWL NRDQKCFQWF EDLLIDISKN
SNDVPKISIN TFNTRCFPKN DVRVFMVWNG LDRIFKAQGL DPTTNLPFKT HWGRPNWDAI
FEYYSRKYSG ETISVFCCGP SELSKELYEK CRYNTSLKSN GTKFYFHKEN F
//
