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Database: UniProt/TrEMBL
Entry: B3MKG0_DROAN
LinkDB: B3MKG0_DROAN
Original site: B3MKG0_DROAN 
ID   B3MKG0_DROAN            Unreviewed;       678 AA.
AC   B3MKG0;
DT   02-SEP-2008, integrated into UniProtKB/TrEMBL.
DT   02-SEP-2008, sequence version 1.
DT   06-JUL-2016, entry version 50.
DE   RecName: Full=NADPH--cytochrome P450 reductase {ECO:0000256|HAMAP-Rule:MF_03212, ECO:0000256|PIRNR:PIRNR000208};
DE            Short=CPR {ECO:0000256|HAMAP-Rule:MF_03212};
DE            Short=P450R {ECO:0000256|HAMAP-Rule:MF_03212};
DE            EC=1.6.2.4 {ECO:0000256|HAMAP-Rule:MF_03212, ECO:0000256|PIRNR:PIRNR000208};
GN   Name=Dana\GF14516 {ECO:0000313|EMBL:EDV31513.1};
GN   ORFNames=Dana_GF14516 {ECO:0000313|EMBL:EDV31513.1}, GF14516
GN   {ECO:0000313|FlyBase:FBgn0091543};
OS   Drosophila ananassae (Fruit fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta;
OC   Pterygota; Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha;
OC   Ephydroidea; Drosophilidae; Drosophila; Sophophora.
OX   NCBI_TaxID=7217 {ECO:0000313|EMBL:EDV31513.1, ECO:0000313|Proteomes:UP000007801};
RN   [1] {ECO:0000313|EMBL:EDV31513.1, ECO:0000313|Proteomes:UP000007801}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Tucson 14024-0371.13 {ECO:0000313|Proteomes:UP000007801};
RX   PubMed=17994087; DOI=10.1038/nature06341;
RG   Drosophila 12 Genomes Consortium;
RA   Clark A.G., Eisen M.B., Smith D.R., Bergman C.M., Oliver B.,
RA   Markow T.A., Kaufman T.C., Kellis M., Gelbart W., Iyer V.N.,
RA   Pollard D.A., Sackton T.B., Larracuente A.M., Singh N.D., Abad J.P.,
RA   Abt D.N., Adryan B., Aguade M., Akashi H., Anderson W.W.,
RA   Aquadro C.F., Ardell D.H., Arguello R., Artieri C.G., Barbash D.A.,
RA   Barker D., Barsanti P., Batterham P., Batzoglou S., Begun D.,
RA   Bhutkar A., Blanco E., Bosak S.A., Bradley R.K., Brand A.D.,
RA   Brent M.R., Brooks A.N., Brown R.H., Butlin R.K., Caggese C.,
RA   Calvi B.R., Bernardo de Carvalho A., Caspi A., Castrezana S.,
RA   Celniker S.E., Chang J.L., Chapple C., Chatterji S., Chinwalla A.,
RA   Civetta A., Clifton S.W., Comeron J.M., Costello J.C., Coyne J.A.,
RA   Daub J., David R.G., Delcher A.L., Delehaunty K., Do C.B., Ebling H.,
RA   Edwards K., Eickbush T., Evans J.D., Filipski A., Findeiss S.,
RA   Freyhult E., Fulton L., Fulton R., Garcia A.C., Gardiner A.,
RA   Garfield D.A., Garvin B.E., Gibson G., Gilbert D., Gnerre S.,
RA   Godfrey J., Good R., Gotea V., Gravely B., Greenberg A.J.,
RA   Griffiths-Jones S., Gross S., Guigo R., Gustafson E.A., Haerty W.,
RA   Hahn M.W., Halligan D.L., Halpern A.L., Halter G.M., Han M.V.,
RA   Heger A., Hillier L., Hinrichs A.S., Holmes I., Hoskins R.A.,
RA   Hubisz M.J., Hultmark D., Huntley M.A., Jaffe D.B., Jagadeeshan S.,
RA   Jeck W.R., Johnson J., Jones C.D., Jordan W.C., Karpen G.H.,
RA   Kataoka E., Keightley P.D., Kheradpour P., Kirkness E.F.,
RA   Koerich L.B., Kristiansen K., Kudrna D., Kulathinal R.J., Kumar S.,
RA   Kwok R., Lander E., Langley C.H., Lapoint R., Lazzaro B.P., Lee S.J.,
RA   Levesque L., Li R., Lin C.F., Lin M.F., Lindblad-Toh K., Llopart A.,
RA   Long M., Low L., Lozovsky E., Lu J., Luo M., Machado C.A.,
RA   Makalowski W., Marzo M., Matsuda M., Matzkin L., McAllister B.,
RA   McBride C.S., McKernan B., McKernan K., Mendez-Lago M., Minx P.,
RA   Mollenhauer M.U., Montooth K., Mount S.M., Mu X., Myers E., Negre B.,
RA   Newfeld S., Nielsen R., Noor M.A., O'Grady P., Pachter L.,
RA   Papaceit M., Parisi M.J., Parisi M., Parts L., Pedersen J.S.,
RA   Pesole G., Phillippy A.M., Ponting C.P., Pop M., Porcelli D.,
RA   Powell J.R., Prohaska S., Pruitt K., Puig M., Quesneville H.,
RA   Ram K.R., Rand D., Rasmussen M.D., Reed L.K., Reenan R., Reily A.,
RA   Remington K.A., Rieger T.T., Ritchie M.G., Robin C., Rogers Y.H.,
RA   Rohde C., Rozas J., Rubenfield M.J., Ruiz A., Russo S., Salzberg S.L.,
RA   Sanchez-Gracia A., Saranga D.J., Sato H., Schaeffer S.W., Schatz M.C.,
RA   Schlenke T., Schwartz R., Segarra C., Singh R.S., Sirot L., Sirota M.,
RA   Sisneros N.B., Smith C.D., Smith T.F., Spieth J., Stage D.E.,
RA   Stark A., Stephan W., Strausberg R.L., Strempel S., Sturgill D.,
RA   Sutton G., Sutton G.G., Tao W., Teichmann S., Tobari Y.N.,
RA   Tomimura Y., Tsolas J.M., Valente V.L., Venter E., Venter J.C.,
RA   Vicario S., Vieira F.G., Vilella A.J., Villasante A., Walenz B.,
RA   Wang J., Wasserman M., Watts T., Wilson D., Wilson R.K., Wing R.A.,
RA   Wolfner M.F., Wong A., Wong G.K., Wu C.I., Wu G., Yamamoto D.,
RA   Yang H.P., Yang S.P., Yorke J.A., Yoshida K., Zdobnov E., Zhang P.,
RA   Zhang Y., Zimin A.V., Baldwin J., Abdouelleil A., Abdulkadir J.,
RA   Abebe A., Abera B., Abreu J., Acer S.C., Aftuck L., Alexander A.,
RA   An P., Anderson E., Anderson S., Arachi H., Azer M., Bachantsang P.,
RA   Barry A., Bayul T., Berlin A., Bessette D., Bloom T., Blye J.,
RA   Boguslavskiy L., Bonnet C., Boukhgalter B., Bourzgui I., Brown A.,
RA   Cahill P., Channer S., Cheshatsang Y., Chuda L., Citroen M.,
RA   Collymore A., Cooke P., Costello M., D'Aco K., Daza R., De Haan G.,
RA   DeGray S., DeMaso C., Dhargay N., Dooley K., Dooley E., Doricent M.,
RA   Dorje P., Dorjee K., Dupes A., Elong R., Falk J., Farina A., Faro S.,
RA   Ferguson D., Fisher S., Foley C.D., Franke A., Friedrich D.,
RA   Gadbois L., Gearin G., Gearin C.R., Giannoukos G., Goode T.,
RA   Graham J., Grandbois E., Grewal S., Gyaltsen K., Hafez N., Hagos B.,
RA   Hall J., Henson C., Hollinger A., Honan T., Huard M.D., Hughes L.,
RA   Hurhula B., Husby M.E., Kamat A., Kanga B., Kashin S., Khazanovich D.,
RA   Kisner P., Lance K., Lara M., Lee W., Lennon N., Letendre F.,
RA   LeVine R., Lipovsky A., Liu X., Liu J., Liu S., Lokyitsang T.,
RA   Lokyitsang Y., Lubonja R., Lui A., MacDonald P., Magnisalis V.,
RA   Maru K., Matthews C., McCusker W., McDonough S., Mehta T., Meldrim J.,
RA   Meneus L., Mihai O., Mihalev A., Mihova T., Mittelman R., Mlenga V.,
RA   Montmayeur A., Mulrain L., Navidi A., Naylor J., Negash T., Nguyen T.,
RA   Nguyen N., Nicol R., Norbu C., Norbu N., Novod N., O'Neill B.,
RA   Osman S., Markiewicz E., Oyono O.L., Patti C., Phunkhang P.,
RA   Pierre F., Priest M., Raghuraman S., Rege F., Reyes R., Rise C.,
RA   Rogov P., Ross K., Ryan E., Settipalli S., Shea T., Sherpa N., Shi L.,
RA   Shih D., Sparrow T., Spaulding J., Stalker J., Stange-Thomann N.,
RA   Stavropoulos S., Stone C., Strader C., Tesfaye S., Thomson T.,
RA   Thoulutsang Y., Thoulutsang D., Topham K., Topping I., Tsamla T.,
RA   Vassiliev H., Vo A., Wangchuk T., Wangdi T., Weiand M., Wilkinson J.,
RA   Wilson A., Yadav S., Young G., Yu Q., Zembek L., Zhong D., Zimmer A.,
RA   Zwirko Z., Jaffe D.B., Alvarez P., Brockman W., Butler J., Chin C.,
RA   Gnerre S., Grabherr M., Kleber M., Mauceli E., MacCallum I.;
RT   "Evolution of genes and genomes on the Drosophila phylogeny.";
RL   Nature 450:203-218(2007).
CC   -!- CATALYTIC ACTIVITY: NADPH + n oxidized hemoprotein = NADP(+) + n
CC       reduced hemoprotein. {ECO:0000256|HAMAP-Rule:MF_03212,
CC       ECO:0000256|PIRNR:PIRNR000208}.
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_03212};
CC       Note=Binds 1 FAD per monomer. {ECO:0000256|HAMAP-Rule:MF_03212};
CC   -!- COFACTOR:
CC       Name=FMN; Xref=ChEBI:CHEBI:58210; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_03212};
CC       Note=Binds 1 FMN per monomer. {ECO:0000256|HAMAP-Rule:MF_03212};
CC   -!- SIMILARITY: Belongs to the NADPH--cytochrome P450 reductase
CC       family. {ECO:0000256|HAMAP-Rule:MF_03212}.
CC   -!- SIMILARITY: Contains 1 FAD-binding FR-type domain.
CC       {ECO:0000256|HAMAP-Rule:MF_03212}.
CC   -!- SIMILARITY: Contains 1 flavodoxin-like domain. {ECO:0000256|HAMAP-
CC       Rule:MF_03212}.
CC   -!- SIMILARITY: In the C-terminal section; belongs to the flavoprotein
CC       pyridine nucleotide cytochrome reductase family.
CC       {ECO:0000256|HAMAP-Rule:MF_03212, ECO:0000256|PIRNR:PIRNR000208}.
CC   -!- SIMILARITY: In the N-terminal section; belongs to the flavodoxin
CC       family. {ECO:0000256|HAMAP-Rule:MF_03212}.
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DR   EMBL; CH902620; EDV31513.1; -; Genomic_DNA.
DR   RefSeq; XP_001962292.1; XM_001962256.2.
DR   ProteinModelPortal; B3MKG0; -.
DR   STRING; 7217.FBpp0117708; -.
DR   EnsemblMetazoa; FBtr0119216; FBpp0117708; FBgn0091543.
DR   GeneID; 6497339; -.
DR   KEGG; dan:Dana_GF14516; -.
DR   FlyBase; FBgn0091543; Dana\GF14516.
DR   eggNOG; KOG1158; Eukaryota.
DR   eggNOG; COG0369; LUCA.
DR   InParanoid; B3MKG0; -.
DR   KO; K00327; -.
DR   OMA; YEWITSG; -.
DR   OrthoDB; EOG7HQN7J; -.
DR   PhylomeDB; B3MKG0; -.
DR   Proteomes; UP000007801; Unassembled WGS sequence.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0010181; F:FMN binding; IEA:InterPro.
DR   GO; GO:0003958; F:NADPH-hemoprotein reductase activity; IEA:UniProtKB-EC.
DR   Gene3D; 1.20.990.10; -; 1.
DR   Gene3D; 3.40.50.360; -; 1.
DR   HAMAP; MF_03212; NCPR; 1.
DR   InterPro; IPR003097; FAD-binding_1.
DR   InterPro; IPR017927; Fd_Rdtase_FAD-bd.
DR   InterPro; IPR001094; Flavdoxin-like.
DR   InterPro; IPR008254; Flavodoxin/NO_synth.
DR   InterPro; IPR001709; Flavoprot_Pyr_Nucl_cyt_Rdtase.
DR   InterPro; IPR029039; Flavoprotein-like_dom.
DR   InterPro; IPR023173; NADPH_Cyt_P450_Rdtase_dom3.
DR   InterPro; IPR001433; OxRdtase_FAD/NAD-bd.
DR   InterPro; IPR023208; P450R.
DR   InterPro; IPR017938; Riboflavin_synthase-like_b-brl.
DR   Pfam; PF00667; FAD_binding_1; 1.
DR   Pfam; PF00258; Flavodoxin_1; 1.
DR   Pfam; PF00175; NAD_binding_1; 1.
DR   PIRSF; PIRSF000208; P450R; 1.
DR   PRINTS; PR00369; FLAVODOXIN.
DR   PRINTS; PR00371; FPNCR.
DR   SUPFAM; SSF52218; SSF52218; 1.
DR   SUPFAM; SSF63380; SSF63380; 1.
DR   PROSITE; PS51384; FAD_FR; 1.
DR   PROSITE; PS50902; FLAVODOXIN_LIKE; 1.
PE   3: Inferred from homology;
KW   Complete proteome {ECO:0000313|Proteomes:UP000007801};
KW   Endoplasmic reticulum {ECO:0000256|HAMAP-Rule:MF_03212,
KW   ECO:0000256|PIRNR:PIRNR000208};
KW   FAD {ECO:0000256|HAMAP-Rule:MF_03212};
KW   Flavoprotein {ECO:0000256|HAMAP-Rule:MF_03212};
KW   FMN {ECO:0000256|HAMAP-Rule:MF_03212};
KW   Membrane {ECO:0000256|HAMAP-Rule:MF_03212,
KW   ECO:0000256|PIRNR:PIRNR000208};
KW   NADP {ECO:0000256|HAMAP-Rule:MF_03212, ECO:0000256|PIRNR:PIRNR000208};
KW   Oxidoreductase {ECO:0000256|HAMAP-Rule:MF_03212,
KW   ECO:0000256|PIRNR:PIRNR000208, ECO:0000313|EMBL:EDV31513.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007801};
KW   Transmembrane {ECO:0000256|HAMAP-Rule:MF_03212};
KW   Transmembrane helix {ECO:0000256|HAMAP-Rule:MF_03212}.
FT   TOPO_DOM      1     20       Lumenal. {ECO:0000256|HAMAP-Rule:
FT                                MF_03212}.
FT   TRANSMEM     21     41       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_03212}.
FT   TOPO_DOM     42    678       Cytoplasmic. {ECO:0000256|HAMAP-Rule:
FT                                MF_03212}.
FT   DOMAIN       83    227       Flavodoxin-like. {ECO:0000259|PROSITE:
FT                                PS50902}.
FT   DOMAIN      282    522       FAD-binding FR-type.
FT                                {ECO:0000259|PROSITE:PS51384}.
FT   NP_BIND      89     94       FMN. {ECO:0000256|HAMAP-Rule:MF_03212}.
FT   NP_BIND     141    144       FMN. {ECO:0000256|HAMAP-Rule:MF_03212}.
FT   NP_BIND     176    185       FMN. {ECO:0000256|HAMAP-Rule:MF_03212}.
FT   NP_BIND     457    460       FAD. {ECO:0000256|HAMAP-Rule:MF_03212}.
FT   NP_BIND     475    477       FAD. {ECO:0000256|HAMAP-Rule:MF_03212}.
FT   NP_BIND     491    494       FAD. {ECO:0000256|HAMAP-Rule:MF_03212}.
FT   NP_BIND     596    597       NADP. {ECO:0000256|HAMAP-Rule:MF_03212}.
FT   NP_BIND     602    606       NADP. {ECO:0000256|HAMAP-Rule:MF_03212}.
FT   BINDING     211    211       FMN. {ECO:0000256|HAMAP-Rule:MF_03212}.
FT   BINDING     301    301       NADP. {ECO:0000256|HAMAP-Rule:MF_03212}.
FT   BINDING     481    481       FAD. {ECO:0000256|HAMAP-Rule:MF_03212}.
FT   BINDING     536    536       NADP. {ECO:0000256|HAMAP-Rule:MF_03212}.
FT   BINDING     639    639       NADP. {ECO:0000256|HAMAP-Rule:MF_03212}.
FT   BINDING     677    677       FAD. {ECO:0000256|HAMAP-Rule:MF_03212}.
SQ   SEQUENCE   678 AA;  76417 MW;  1BA5DCABCA3C8CFF CRC64;
     MASEQIIEEA AEAVAGGNEP FLGLLDIALL AVLIGGAAFY FLRSRKKEEE PVRSYSIQPT
     TVSTTTATDN SFIKKLKASG RSLVVFYGSQ TGTGEEFAGR LAKEGIRYRL KGMVADPEEC
     DMEELLQLKD IDNSLAVFCL ATYGEGDPTD NAMEFYEWIT NGDVDLTGLN YAVFGLGNKT
     YEHYNKVAIY VDKRLEELGA NRVFELGLGD DDANIEDDFI TWKDRFWPAV CDHFGIEGGG
     EEVLIRQYRL LEQPDVQPDR IYTGEIARLH SVQNQRPPFD AKNPFLAPIK VNRELHKGGG
     RSCMHIELSI EGSKMRYDAG DHVAMYPIND KGLVEKLGQL CNADLDTIFS LINTDTDSSK
     KHPFPCPTTY RTALTHYLEI TAIPRTHILK ELAEYCTDEK EKELLRSMAS ISPEGKEKYQ
     SWIQDACRNI VHILEDIKSC RPPIDHVCEL LPRLQPRYYS ISSSGKLHPT DVHVTAVLVE
     YKTPTGRVNK GVATTYLKNK QPKDGEEVKV PVFIRKSQFR LPTKPETPII MVGPGTGLAP
     FRGFIQERQH LRDEGKTVGE SILYFGCRKR SEDYIYESEL EEWVKKGTLN LKAAFSRDQA
     SKVYVQHLLE QDADLIWNVI GENKGHFYIC GDAKNMAVDV RNILVKILST KGNMSEADAV
     QYIKKMEAQK RYSADVWS
//
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