GenomeNet

Database: UniProt
Entry: B3LZC7_DROAN
LinkDB: B3LZC7_DROAN
Original site: B3LZC7_DROAN 
ID   B3LZC7_DROAN            Unreviewed;      1153 AA.
AC   B3LZC7;
DT   02-SEP-2008, integrated into UniProtKB/TrEMBL.
DT   02-SEP-2008, sequence version 1.
DT   24-JAN-2024, entry version 69.
DE   RecName: Full=superoxide dismutase {ECO:0000256|ARBA:ARBA00012682};
DE            EC=1.15.1.1 {ECO:0000256|ARBA:ARBA00012682};
GN   Name=Dana\GF16197 {ECO:0000313|EMBL:EDV44106.1};
GN   Synonyms=dana_GLEANR_17468 {ECO:0000313|EMBL:EDV44106.1};
GN   ORFNames=GF16197 {ECO:0000313|EMBL:EDV44106.1};
OS   Drosophila ananassae (Fruit fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC   Drosophilidae; Drosophila; Sophophora.
OX   NCBI_TaxID=7217 {ECO:0000313|EMBL:EDV44106.1, ECO:0000313|Proteomes:UP000007801};
RN   [1] {ECO:0000313|EMBL:EDV44106.1, 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., Markow T.A.,
RA   Kaufman T.C., Kellis M., Gelbart W., Iyer V.N., Pollard D.A., Sackton T.B.,
RA   Larracuente A.M., Singh N.D., Abad J.P., Abt D.N., Adryan B., Aguade M.,
RA   Akashi H., Anderson W.W., Aquadro C.F., Ardell D.H., Arguello R.,
RA   Artieri C.G., Barbash D.A., Barker D., Barsanti P., Batterham P.,
RA   Batzoglou S., Begun D., Bhutkar A., Blanco E., Bosak S.A., Bradley R.K.,
RA   Brand A.D., 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., Daub J.,
RA   David R.G., Delcher A.L., Delehaunty K., Do C.B., Ebling H., Edwards K.,
RA   Eickbush T., Evans J.D., Filipski A., Findeiss S., Freyhult E., Fulton L.,
RA   Fulton R., Garcia A.C., Gardiner A., Garfield D.A., Garvin B.E., Gibson G.,
RA   Gilbert D., Gnerre S., Godfrey J., Good R., Gotea V., Gravely B.,
RA   Greenberg A.J., Griffiths-Jones S., Gross S., Guigo R., Gustafson E.A.,
RA   Haerty W., 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., Hubisz M.J.,
RA   Hultmark D., Huntley M.A., Jaffe D.B., Jagadeeshan S., Jeck W.R.,
RA   Johnson J., Jones C.D., Jordan W.C., Karpen G.H., Kataoka E.,
RA   Keightley P.D., Kheradpour P., Kirkness E.F., Koerich L.B., Kristiansen K.,
RA   Kudrna D., Kulathinal R.J., Kumar S., Kwok R., Lander E., Langley C.H.,
RA   Lapoint R., Lazzaro B.P., Lee S.J., Levesque L., Li R., Lin C.F., Lin M.F.,
RA   Lindblad-Toh K., Llopart A., Long M., Low L., Lozovsky E., Lu J., Luo M.,
RA   Machado C.A., Makalowski W., Marzo M., Matsuda M., Matzkin L.,
RA   McAllister B., McBride C.S., McKernan B., McKernan K., Mendez-Lago M.,
RA   Minx P., Mollenhauer M.U., Montooth K., Mount S.M., Mu X., Myers E.,
RA   Negre B., 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., Pesole G.,
RA   Phillippy A.M., Ponting C.P., Pop M., Porcelli D., Powell J.R.,
RA   Prohaska S., Pruitt K., Puig M., Quesneville H., Ram K.R., Rand D.,
RA   Rasmussen M.D., Reed L.K., Reenan R., Reily A., Remington K.A.,
RA   Rieger T.T., Ritchie M.G., Robin C., Rogers Y.H., Rohde C., Rozas J.,
RA   Rubenfield M.J., Ruiz A., Russo S., Salzberg S.L., Sanchez-Gracia A.,
RA   Saranga D.J., Sato H., Schaeffer S.W., Schatz M.C., Schlenke T.,
RA   Schwartz R., Segarra C., Singh R.S., Sirot L., Sirota M., Sisneros N.B.,
RA   Smith C.D., Smith T.F., Spieth J., Stage D.E., Stark A., Stephan W.,
RA   Strausberg R.L., Strempel S., Sturgill D., Sutton G., Sutton G.G., Tao W.,
RA   Teichmann S., Tobari Y.N., Tomimura Y., Tsolas J.M., Valente V.L.,
RA   Venter E., Venter J.C., Vicario S., Vieira F.G., Vilella A.J.,
RA   Villasante A., Walenz B., Wang J., Wasserman M., Watts T., Wilson D.,
RA   Wilson R.K., Wing R.A., Wolfner M.F., Wong A., Wong G.K., Wu C.I., Wu G.,
RA   Yamamoto D., Yang H.P., Yang S.P., Yorke J.A., Yoshida K., Zdobnov E.,
RA   Zhang P., 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., An P.,
RA   Anderson E., Anderson S., Arachi H., Azer M., Bachantsang P., Barry A.,
RA   Bayul T., Berlin A., Bessette D., Bloom T., Blye J., Boguslavskiy L.,
RA   Bonnet C., Boukhgalter B., Bourzgui I., Brown A., Cahill P., Channer S.,
RA   Cheshatsang Y., Chuda L., Citroen M., Collymore A., Cooke P., Costello M.,
RA   D'Aco K., Daza R., De Haan G., DeGray S., DeMaso C., Dhargay N., Dooley K.,
RA   Dooley E., Doricent M., Dorje P., Dorjee K., Dupes A., Elong R., Falk J.,
RA   Farina A., Faro S., Ferguson D., Fisher S., Foley C.D., Franke A.,
RA   Friedrich D., 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., LeVine R.,
RA   Lipovsky A., Liu X., Liu J., Liu S., Lokyitsang T., Lokyitsang Y.,
RA   Lubonja R., Lui A., MacDonald P., Magnisalis V., Maru K., Matthews C.,
RA   McCusker W., McDonough S., Mehta T., Meldrim J., Meneus L., Mihai O.,
RA   Mihalev A., Mihova T., Mittelman R., Mlenga V., Montmayeur A., Mulrain L.,
RA   Navidi A., Naylor J., Negash T., Nguyen T., Nguyen N., Nicol R., Norbu C.,
RA   Norbu N., Novod N., O'Neill B., Osman S., Markiewicz E., Oyono O.L.,
RA   Patti C., Phunkhang P., Pierre F., Priest M., Raghuraman S., Rege F.,
RA   Reyes R., Rise C., Rogov P., Ross K., Ryan E., Settipalli S., Shea T.,
RA   Sherpa N., Shi L., Shih D., Sparrow T., Spaulding J., Stalker J.,
RA   Stange-Thomann N., Stavropoulos S., Stone C., Strader C., Tesfaye S.,
RA   Thomson T., Thoulutsang Y., Thoulutsang D., Topham K., Topping I.,
RA   Tsamla T., Vassiliev H., Vo A., Wangchuk T., Wangdi T., Weiand M.,
RA   Wilkinson J., Wilson A., Yadav S., Young G., Yu Q., Zembek L., Zhong D.,
RA   Zimmer A., Zwirko Z., Jaffe D.B., Alvarez P., Brockman W., Butler J.,
RA   Chin C., 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   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CH902617; EDV44106.1; -; Genomic_DNA.
DR   RefSeq; XP_001955545.1; XM_001955509.2.
DR   AlphaFoldDB; B3LZC7; -.
DR   STRING; 7217.B3LZC7; -.
DR   EnsemblMetazoa; FBtr0120897; FBpp0119389; FBgn0093219.
DR   GeneID; 6498994; -.
DR   KEGG; dan:6498994; -.
DR   eggNOG; ENOG502QW6R; Eukaryota.
DR   HOGENOM; CLU_004514_0_0_1; -.
DR   InParanoid; B3LZC7; -.
DR   OMA; VWSWAVR; -.
DR   OrthoDB; 2912800at2759; -.
DR   PhylomeDB; B3LZC7; -.
DR   Proteomes; UP000007801; Unassembled WGS sequence.
DR   GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR   GO; GO:0006801; P:superoxide metabolic process; IEA:InterPro.
DR   Gene3D; 2.60.40.200; Superoxide dismutase, copper/zinc binding domain; 4.
DR   InterPro; IPR036423; SOD-like_Cu/Zn_dom_sf.
DR   InterPro; IPR001424; SOD_Cu_Zn_dom.
DR   PANTHER; PTHR20910; AGAP001623-PA; 1.
DR   PANTHER; PTHR20910:SF1; SOD_CU DOMAIN-CONTAINING PROTEIN; 1.
DR   Pfam; PF00080; Sod_Cu; 1.
DR   SUPFAM; SSF49329; Cu,Zn superoxide dismutase-like; 5.
PE   4: Predicted;
KW   Reference proteome {ECO:0000313|Proteomes:UP000007801};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..25
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           26..1153
FT                   /note="superoxide dismutase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5002789344"
FT   DOMAIN          696..819
FT                   /note="Superoxide dismutase copper/zinc binding"
FT                   /evidence="ECO:0000259|Pfam:PF00080"
SQ   SEQUENCE   1153 AA;  129179 MW;  A73095B1DF7CB491 CRC64;
     MVRVGHLFRF AVLCWIASAF SGADAQHLIA YISQRGLHGE ITFRQVNATT VEIKASLEAT
     LQYPDQVWSW AVRRFPVDYS NTDPDERCEL SRLGSQVLSF DEDLEYLVLP GNETATWERN
     MQLIGDRGIW GKSLVLTEVN SNARICATIT TVQSSVEHMA EARFNTPIAG SVHFRWLAPT
     EGSSGDTLIY SDLYHIREQP AGLEGGNGRS TPFTQHHWKI FVTDIFKLDH HRTEDNCNFL
     QLVFDPQGGG AGQGIGDLDS RLGRIGVAKN ALRSPQRSVF RDAQLALLPS DLTIPHRTLY
     LVLFDNQHPD TYLACTKIRH VQPLTYKTFI NSGGVKGEVT FTQRSKFDPT FLNFTLGAPL
     SQHVSRKFAE DVAAFRIHSL PPVPQRMGHE DYCWTTGEMH NPRELNDNIP PPGYGTQEQY
     AVGDLSGKLQ GRNKGYFHQY VLPGTSSELS GLYWDVFLPL QGRHSIVQRS LVIYTYNRTD
     VGNITQSIWG CSSLGQYQKN GIYQQNMVTA QVLFRYPVVG RVIFRQAAEE PWQDTTMLFE
     YLIQADGSTQ NTTFDHRWAI HSAPPGKDFY DWQQRCISAG PVFNPYRVDW GNRSADDFCQ
     PHLPAMCRLG ALDARLGRLT IAGGKRVAQK ISRKMFVDGN LPLSGRHSIL GKSLVLYEDN
     GPKARGERLA CSAVIGHFRR KVVAKEWYAN GDPLTVSGRV EITQQSEYDI SNVEVQLKGL
     KDNTGYHIHR TPVEANLAFP CEASTLYGHW NPFEVNPKSA PPTKRGTTDQ YEMGDLSGKF
     GGLEGVTQFE DSYNDTNLPL FGYNSIIGRS VVIQKRQKNA RWACSTLERG YSPSEARELR
     AIASFHHPTG YAYGYIKMTQ LIHSDGSQSE TVIEVKLRHP GKNDRNSTRN HNWQIYVNPV
     GVDAAVKPTI TRCVAGGYVW NPYYTQLADP LNLDLYEQEC GPDNPLRCYV GDVGARLGTI
     DLGGERVVLT DSNFPLESPV GAIGRSIVIF GPDNSHERFA CANIEADHNV IKYINLQKPP
     RFVVAQFLEE LRSVMGIPEW MLDVDARKTK ELHGGACIQM IIHFKGPLAH RLELDMSRLI
     AAGRLDAPSL FIPGYVNTKR KATISYRTCG VRDTNEKRTK NFKGGFYSSS SNLIQPKAFS
     LSIVVISLAF SFL
//
DBGET integrated database retrieval system