GenomeNet

Database: UniProt
Entry: B4Q0G6_DROYA
LinkDB: B4Q0G6_DROYA
Original site: B4Q0G6_DROYA 
ID   B4Q0G6_DROYA            Unreviewed;       636 AA.
AC   B4Q0G6;
DT   23-SEP-2008, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 2.
DT   24-JAN-2024, entry version 89.
DE   RecName: Full=asparaginase {ECO:0000256|ARBA:ARBA00012920};
DE            EC=3.5.1.1 {ECO:0000256|ARBA:ARBA00012920};
GN   Name=Dyak\GE16877 {ECO:0000313|EMBL:EDX01250.2};
GN   ORFNames=Dyak_GE16877 {ECO:0000313|EMBL:EDX01250.2};
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:EDX01250.2, ECO:0000313|Proteomes:UP000002282};
RN   [1] {ECO:0000313|EMBL:EDX01250.2, 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:EDX01250.2, 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; CM000162; EDX01250.2; -; Genomic_DNA.
DR   RefSeq; XP_002100142.2; XM_002100106.2.
DR   AlphaFoldDB; B4Q0G6; -.
DR   SMR; B4Q0G6; -.
DR   EnsemblMetazoa; FBtr0263395; FBpp0261887; FBgn0234367.
DR   GeneID; 6524280; -.
DR   KEGG; dya:Dyak_GE16877; -.
DR   eggNOG; KOG0503; Eukaryota.
DR   HOGENOM; CLU_019134_3_0_1; -.
DR   OrthoDB; 1421816at2759; -.
DR   Proteomes; UP000002282; Chromosome X.
DR   GO; GO:0004067; F:asparaginase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0009066; P:aspartate family amino acid metabolic process; IEA:UniProt.
DR   CDD; cd08963; L-asparaginase_I; 1.
DR   Gene3D; 3.40.50.40; -; 1.
DR   Gene3D; 1.25.40.20; Ankyrin repeat-containing domain; 2.
DR   Gene3D; 3.40.50.1170; L-asparaginase, N-terminal domain; 1.
DR   InterPro; IPR002110; Ankyrin_rpt.
DR   InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR   InterPro; IPR006033; AsnA_fam.
DR   InterPro; IPR036152; Asp/glu_Ase-like_sf.
DR   InterPro; IPR006034; Asparaginase/glutaminase-like.
DR   InterPro; IPR027475; Asparaginase/glutaminase_AS2.
DR   InterPro; IPR040919; Asparaginase_C.
DR   InterPro; IPR027473; L-asparaginase_C.
DR   InterPro; IPR041725; L-asparaginase_I.
DR   InterPro; IPR027474; L-asparaginase_N.
DR   InterPro; IPR037152; L-asparaginase_N_sf.
DR   NCBIfam; TIGR00519; asnASE_I; 1.
DR   PANTHER; PTHR11707:SF28; 60 KDA LYSOPHOSPHOLIPASE; 1.
DR   PANTHER; PTHR11707; L-ASPARAGINASE; 1.
DR   Pfam; PF12796; Ank_2; 2.
DR   Pfam; PF00710; Asparaginase; 1.
DR   Pfam; PF17763; Asparaginase_C; 1.
DR   PIRSF; PIRSF001220; L-ASNase_gatD; 2.
DR   PIRSF; PIRSF500176; L_ASNase; 2.
DR   PRINTS; PR00139; ASNGLNASE.
DR   SFLD; SFLDS00057; Glutaminase/Asparaginase; 1.
DR   SMART; SM00248; ANK; 3.
DR   SMART; SM00870; Asparaginase; 1.
DR   SUPFAM; SSF48403; Ankyrin repeat; 1.
DR   SUPFAM; SSF53774; Glutaminase/Asparaginase; 1.
DR   PROSITE; PS50297; ANK_REP_REGION; 2.
DR   PROSITE; PS50088; ANK_REPEAT; 3.
DR   PROSITE; PS00917; ASN_GLN_ASE_2; 1.
DR   PROSITE; PS51732; ASN_GLN_ASE_3; 1.
PE   4: Predicted;
KW   ANK repeat {ECO:0000256|PROSITE-ProRule:PRU00023};
KW   Hydrolase {ECO:0000313|EMBL:EDX01250.2}.
FT   DOMAIN          57..269
FT                   /note="L-asparaginase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00710"
FT   DOMAIN          289..403
FT                   /note="Asparaginase/glutaminase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF17763"
FT   REPEAT          482..514
FT                   /note="ANK"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT   REPEAT          515..547
FT                   /note="ANK"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT   REPEAT          581..613
FT                   /note="ANK"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT   REGION          21..44
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        168
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10100"
FT   BINDING         137
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001220-2"
FT   BINDING         168..169
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001220-2"
SQ   SEQUENCE   636 AA;  69535 MW;  6714CCD4B8438603 CRC64;
     MSSNGMAIPV LKTNGHERLA SLDKSMPPAS PTLPSPTIRR NKSDGKLMAQ DVKEAMVKVI
     YTGGTIGMVR NERNALAPIP NALVRSIRKY PNIHDEEYAL RRFGTSASMA PLVLPIVQGV
     DRRVIYQITE YTPLLDSSNM TMNDWARIAS DIQQSYEFFD GFVVLHGTDT LSYTASALSF
     MLENLGKTVI ITGSQIPIFE TRTDGKDNFT SALIIAGNYI IPEVCVFFGH KLMRGNRTVK
     VSSNALDAFD SPNVPPLARI GIDVNVDYRL IFRPCSIERF RVHLNLDENV GLLRIFPSIS
     HSTFRAFLAP PIRGVVLQSF GSGNIPSNRT DLIDELRAAG ERGVIIINCT QCPNGTVAEI
     YDTGKVLCDV GVIPGFDMTP EAALSKLAYV IGKEEWSLEV KKQMMQANLR GELTSLKAAK
     MEDYDLVDAV ARSLHLSSPQ ELDQLGETLF PAMINAAVAE GDPKKINNLK AYGADLSGTN
     HDQRTALHLA CQLGNVEIVK YLLQNGVSVH VRDRYDRTPL LEAVSTDSHE IIQLLINCGA
     HLTGSSRAIG EQLCAAAARG SMVRLKSYQF AGADLAQPDP SGRTALHVAA LHGFPEVVQY
     VLPYFENPHE KDMLGLTALD YAERGGHAAA IEALKT
//
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