ID B4KRA2_DROMO Unreviewed; 630 AA.
AC B4KRA2;
DT 23-SEP-2008, integrated into UniProtKB/TrEMBL.
DT 23-SEP-2008, sequence version 1.
DT 27-MAR-2024, entry version 94.
DE SubName: Full=Uncharacterized protein, isoform A {ECO:0000313|EMBL:EDW09318.1};
DE SubName: Full=Uncharacterized protein, isoform C {ECO:0000313|EMBL:KRG04586.1};
GN Name=Dmoj\GI19106 {ECO:0000313|EMBL:EDW09318.1};
GN ORFNames=Dmoj_GI19106 {ECO:0000313|EMBL:EDW09318.1};
OS Drosophila mojavensis (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila.
OX NCBI_TaxID=7230 {ECO:0000313|EMBL:EDW09318.1, ECO:0000313|Proteomes:UP000009192};
RN [1] {ECO:0000313|EMBL:EDW09318.1, ECO:0000313|Proteomes:UP000009192}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TSC#15081-1352.22 {ECO:0000313|EMBL:EDW09318.1}, and Tucson
RC 15081-1352.22 {ECO:0000313|Proteomes:UP000009192};
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:EDW09318.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=TSC#15081-1352.22 {ECO:0000313|EMBL:EDW09318.1};
RX PubMed=18057021; DOI=10.1093/bioinformatics/btm542;
RA Zimin A.V., Smith D.R., Sutton G., Yorke J.A.;
RT "Assembly reconciliation.";
RL Bioinformatics 24:42-45(2008).
RN [3] {ECO:0000313|EMBL:EDW09318.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=TSC#15081-1352.22 {ECO:0000313|EMBL:EDW09318.1};
RG FlyBase;
RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; CH933808; EDW09318.1; -; Genomic_DNA.
DR EMBL; CH933808; KRG04586.1; -; Genomic_DNA.
DR RefSeq; XP_002005383.1; XM_002005347.2.
DR RefSeq; XP_015019190.1; XM_015163704.1.
DR AlphaFoldDB; B4KRA2; -.
DR SMR; B4KRA2; -.
DR EnsemblMetazoa; FBtr0169831; FBpp0168323; FBgn0141845.
DR EnsemblMetazoa; FBtr0424905; FBpp0382710; FBgn0141845.
DR GeneID; 6579488; -.
DR KEGG; dmo:Dmoj_GI19106; -.
DR eggNOG; KOG2101; Eukaryota.
DR HOGENOM; CLU_036868_0_0_1; -.
DR InParanoid; B4KRA2; -.
DR OMA; FTQYAST; -.
DR OrthoDB; 50529at2759; -.
DR Proteomes; UP000009192; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0003779; F:actin binding; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0035091; F:phosphatidylinositol binding; IEA:InterPro.
DR GO; GO:0004672; F:protein kinase activity; IEA:InterPro.
DR CDD; cd06871; PX_MONaKA; 1.
DR Gene3D; 3.30.1520.10; Phox-like domain; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR037903; MONaKA_PX.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR001683; PX_dom.
DR InterPro; IPR036871; PX_dom_sf.
DR InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR InterPro; IPR003124; WH2_dom.
DR PANTHER; PTHR22999:SF40; PX DOMAIN-CONTAINING PROTEIN KINASE-LIKE PROTEIN; 1.
DR PANTHER; PTHR22999; PX SERINE/THREONINE KINASE PXK; 1.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR Pfam; PF00787; PX; 1.
DR SMART; SM00312; PX; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR SUPFAM; SSF64268; PX domain; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS50195; PX; 1.
DR PROSITE; PS51082; WH2; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000009192}.
FT DOMAIN 14..122
FT /note="PX"
FT /evidence="ECO:0000259|PROSITE:PS50195"
FT DOMAIN 182..481
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 607..626
FT /note="WH2"
FT /evidence="ECO:0000259|PROSITE:PS51082"
FT REGION 167..202
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 486..519
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 534..607
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 174..191
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 534..554
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 565..596
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 630 AA; 70059 MW; 5AA98EB460476BC5 CRC64;
MAIFASRYER KLPIDDTEAI SCEITTVEQV DGHTEYLLRV QRGDKSWNVL RRYNEFNNLH
KCLRISGIEL PLPGKRIFGN MRPDFIAERK EALQVYINTI LMNPILASSL PAKRFVDPES
YSQSFHDHAV QNAMLCLRND TVWALGPTMG AIGWRLRKHY FKVTTKPPEK GSNKLVKSGS
QNQQSKHFAA GSNGGAHSVS IDAGSVDPNA EMVAEWLEYG PDKYVDEKEM HGVLKSLMGL
QHPHIEPVVF AAHTENGCLV IRKFHKHGTL KDVLCMATPK NPFLSKYGNP KGRTALSMKQ
VATYGKQILE ALIFLHSKGY ACGHLHSGNI VIVDDCVKLL DIENHLLGVP AFYRPFFVQH
SKIHTIETID VYCFGHVLFE MAMGYPLQES VVRQITECPE ALKSLLESIL SKEACKAGLP
TLDQLLGHRF FTQYATESAV TSEKPHFKLS LNAKELLRQA AVKSETRLRD EQKSVKNQKR
IVRVQELMSS EEEKRKSKQK AKLEHKQSKL KQQGSLQTSN GRLSLAAVTA ASTSAVASGG
GLSTTDSFNR SDSTPEEPAL AGIKSLTPAS QSPRQEIPAS SNLVVERQTS TPNIASEDVD
AGEDEPTRSA LLESICKFNR GSLRKVRSND
//
