ID B4P9U9_DROYA Unreviewed; 1394 AA.
AC B4P9U9;
DT 23-SEP-2008, integrated into UniProtKB/TrEMBL.
DT 23-SEP-2008, sequence version 1.
DT 27-MAR-2024, entry version 72.
DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:EDW90290.1};
DE EC=1.11.1.7 {ECO:0000313|EMBL:EDW90290.1};
GN Name=Dyak\GE13192 {ECO:0000313|EMBL:EDW90290.1};
GN ORFNames=Dyak_GE13192 {ECO:0000313|EMBL:EDW90290.1};
OS Drosophila yakuba (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7245 {ECO:0000313|EMBL:EDW90290.1, ECO:0000313|Proteomes:UP000002282};
RN [1] {ECO:0000313|EMBL:EDW90290.1, ECO:0000313|Proteomes:UP000002282}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tai18E2 / Tucson 14021-0261.01
RC {ECO:0000313|Proteomes:UP000002282};
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).
RN [2] {ECO:0000313|EMBL:EDW90290.1, ECO:0000313|Proteomes:UP000002282}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tai18E2 / Tucson 14021-0261.01
RC {ECO:0000313|Proteomes:UP000002282};
RX PubMed=17550304; DOI=10.1371/journal.pbio.0050152;
RA Ranz J.M., Maurin D., Chan Y.S., von Grotthuss M., Hillier L.W., Roote J.,
RA Ashburner M., Bergman C.M.;
RT "Principles of genome evolution in the Drosophila melanogaster species
RT group.";
RL PLoS Biol. 5:E152-E152(2007).
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DR EMBL; CM000158; EDW90290.1; -; Genomic_DNA.
DR RefSeq; XP_002090578.1; XM_002090542.2.
DR EnsemblMetazoa; FBtr0259710; FBpp0258202; FBgn0230887.
DR GeneID; 6529584; -.
DR KEGG; dya:Dyak_GE13192; -.
DR eggNOG; KOG2408; Eukaryota.
DR HOGENOM; CLU_005243_0_0_1; -.
DR OMA; WCLCAPS; -.
DR OrthoDB; 4560at2759; -.
DR PhylomeDB; B4P9U9; -.
DR Proteomes; UP000002282; Chromosome 2R.
DR GO; GO:0020037; F:heme binding; IEA:InterPro.
DR GO; GO:0140825; F:lactoperoxidase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006979; P:response to oxidative stress; IEA:InterPro.
DR CDD; cd09823; peroxinectin_like; 1.
DR Gene3D; 1.10.640.10; Haem peroxidase domain superfamily, animal type; 3.
DR InterPro; IPR019791; Haem_peroxidase_animal.
DR InterPro; IPR010255; Haem_peroxidase_sf.
DR InterPro; IPR037120; Haem_peroxidase_sf_animal.
DR PANTHER; PTHR11475:SF4; LD42267P; 1.
DR PANTHER; PTHR11475; OXIDASE/PEROXIDASE; 1.
DR Pfam; PF03098; An_peroxidase; 4.
DR PRINTS; PR00457; ANPEROXIDASE.
DR SUPFAM; SSF48113; Heme-dependent peroxidases; 2.
DR PROSITE; PS50292; PEROXIDASE_3; 2.
PE 4: Predicted;
KW Heme {ECO:0000256|PIRSR:PIRSR619791-2};
KW Iron {ECO:0000256|PIRSR:PIRSR619791-2};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR619791-2};
KW Oxidoreductase {ECO:0000313|EMBL:EDW90290.1};
KW Peroxidase {ECO:0000313|EMBL:EDW90290.1}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..21
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 22..1394
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002817733"
FT BINDING 1041
FT /ligand="heme b"
FT /ligand_id="ChEBI:CHEBI:60344"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000256|PIRSR:PIRSR619791-2"
SQ SEQUENCE 1394 AA; 155455 MW; 1D1C5A0E0EC194C7 CRC64;
MTKPEMLISL ILWCLCAPSL TLRIPEDLEN AAINALSSER ARSLTPCGSS AEAEGSVAGD
YDVCPPSKYR QPTAECNNVS HRKWGARGDI FQRLLAADYA DGVSQPRTSK GTHALPDAEL
VIEQLQRHVE GELRHAHITA MLPAWGQLLA NDLVEVGQLP IFGKCCERDS AVKDPSELQH
CFVRAGPDCK EYKRSAPGFD SDACQRHTRQ QMNIASAYID GSGLYGSTRH EFDQLRTYIS
GGVKVESCKY CQVAGATGAL HRALLQQHNN IGEQLSHINP DWSEEDVFLE ARRIITATIQ
HITYNEFLPL VLGQETTAKE GLRLTAEKHS SNYSSSVRGG IYNEFATAAM PAFWSMYPPE
MLAKKMSAHE LLSIAALQKS LVPSQTNAEG WSELALAVHR GRDHGVASYV HALDLCERRF
ADQSAANVSF DTLAQVSNIP EEYITNLRDI YQNANDIDLL VGALLEEPVV GALFGPTISC
LLTLQFEQLK QTDRFWYENE IPPSSFTLDQ LKSIRQTTLS GLLCGSHQVS TAQSKAFILE
DNYLNSILDC DQLPKFDLKP WQVNPEDEVH VDHVEVEPAT KEAIAELSPE LIEAAVERAK
QELEERRRFE YEVWRTKGGI SARSPDGTAA SFSKANLAAL NLANSSLIFE LTSNEIVKTL
NHITRRKRQI FNPNQNAFNR NELTDTLQTV DISGLLGGAQ NSLDTCPEPS QQCDANSPFR
TLSGRCNNLR NPNWGKSLTT FSRLLPAQYE DGISAPRLTG VTGTALPNPR TISTTIHPDI
SNLHTRYSLM VMQFAQFVDH DLTLTPIHKG FHESIPSCRP CNSRQTVHPE CNPFPVPAGD
FYYPEVNVTS GERFCFPSMR SLPGQQSLGP RDQINQNTHF LDGSMVYGET TCLSNKLRGF
SGRMNSTQVR GKELLPLGPH PECKSRNGLC FLGGDDRASE QPGLTAIHTA FLREHNRIVE
GLRGVNPHWN GEQLFHHARK IVSAQVQHIV FNEFLPRILS WNAVNLYGLK LLPQGYYKDY
NPSCSPIVFN EFAAAAFRIG HSLLRPHIPR LSVQHQPVEP PLLLRDGFFR MDALLQPGII
DEILRGLVAT PMETLDQFIT GEVTNHLFED RKIPFSGIDL IALNIQRARD HGIPSYNNYR
ALCNLKRATN WNDLSREIPT EVINRFQKVY ASVDDIDLFP GAMTERPLQG GLVGPTLACI
IGIQFRQLRK CDRFWYENQN PEVKFTEAQL AEIRKVTLAK IVCENLEISG DMQRAAFDLP
SNFLNPRVPC SSMPQIDLNA WRENVQGCQI GNRNVRVGES AFPSPCTSCV CSAEGAQCAS
LRITDCGQLI RQWPKEAILR DEVCNSQCGI YLTGQQASGF NAQQRQGQAQ PRVTRSRNQN
LFKFPDLTPF IASL
//
