ID   B4LQZ8_DROVI            Unreviewed;       375 AA.
AC   B4LQZ8;
DT   23-SEP-2008, integrated into UniProtKB/TrEMBL.
DT   23-SEP-2008, sequence version 1.
DT   02-NOV-2016, entry version 67.
DE   RecName: Full=Mitogen-activated protein kinase {ECO:0000256|RuleBase:RU361165, ECO:0000256|SAAS:SAAS00574127};
DE            EC=2.7.11.24 {ECO:0000256|RuleBase:RU361165, ECO:0000256|SAAS:SAAS00574127};
GN   Name=Dvir\GJ17518 {ECO:0000313|EMBL:EDW64537.1};
GN   ORFNames=Dvir_GJ17518 {ECO:0000313|EMBL:EDW64537.1}, GJ17518
GN   {ECO:0000313|FlyBase:FBgn0204688};
OS   Drosophila virilis (Fruit fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta;
OC   Pterygota; Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha;
OC   Ephydroidea; Drosophilidae; Drosophila.
OX   NCBI_TaxID=7244 {ECO:0000313|EMBL:EDW64537.1, ECO:0000313|Proteomes:UP000008792};
RN   [1] {ECO:0000313|EMBL:EDW64537.1, ECO:0000313|Proteomes:UP000008792}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TSC#15010-1051.87 {ECO:0000313|EMBL:EDW64537.1}, and Tucson
RC   15010-1051.87 {ECO:0000313|Proteomes:UP000008792};
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).
RN   [2] {ECO:0000313|EMBL:EDW64537.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=TSC#15010-1051.87 {ECO:0000313|EMBL:EDW64537.1};
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:EDW64537.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=TSC#15010-1051.87 {ECO:0000313|EMBL:EDW64537.1};
RG   FlyBase;
RL   Submitted (JUN-2008) to the EMBL/GenBank/DDBJ databases.
RN   [4] {ECO:0000313|EMBL:KRF81685.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=TSC#15010-1051.87 {ECO:0000313|EMBL:KRF81685.1};
RG   FlyBase;
RL   Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
CC       {ECO:0000256|RuleBase:RU361165, ECO:0000256|SAAS:SAAS00574132}.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|RuleBase:RU361165};
CC   -!- ENZYME REGULATION: Activated by threonine and tyrosine
CC       phosphorylation. {ECO:0000256|RuleBase:RU361165}.
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr
CC       protein kinase family. MAP kinase subfamily.
CC       {ECO:0000256|RuleBase:RU361165}.
CC   -!- SIMILARITY: Contains 1 protein kinase domain.
CC       {ECO:0000256|RuleBase:RU361165}.
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DR   EMBL; CH940649; EDW64537.1; -; Genomic_DNA.
DR   EMBL; CH940649; KRF81685.1; -; Genomic_DNA.
DR   EMBL; CH940649; KRF81686.1; -; Genomic_DNA.
DR   RefSeq; XP_002052382.1; XM_002052346.2.
DR   RefSeq; XP_015028433.1; XM_015172947.1.
DR   RefSeq; XP_015028434.1; XM_015172948.1.
DR   ProteinModelPortal; B4LQZ8; -.
DR   STRING; 7244.FBpp0231935; -.
DR   EnsemblMetazoa; FBtr0233443; FBpp0231935; FBgn0204688.
DR   GeneID; 6629054; -.
DR   KEGG; dvi:Dvir_GJ17518; -.
DR   FlyBase; FBgn0204688; Dvir\GJ17518.
DR   eggNOG; KOG0660; Eukaryota.
DR   eggNOG; ENOG410XNY0; LUCA.
DR   InParanoid; B4LQZ8; -.
DR   KO; K04371; -.
DR   OMA; EEAESHH; -.
DR   OrthoDB; EOG091G08QL; -.
DR   PhylomeDB; B4LQZ8; -.
DR   Proteomes; UP000008792; Unassembled WGS sequence.
DR   GO; GO:0005622; C:intracellular; IEA:GOC.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004707; F:MAP kinase activity; IEA:UniProtKB-EC.
DR   InterPro; IPR011009; Kinase-like_dom.
DR   InterPro; IPR003527; MAP_kinase_CS.
DR   InterPro; IPR008349; MAPK_ERK1/2.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR008271; Ser/Thr_kinase_AS.
DR   Pfam; PF00069; Pkinase; 1.
DR   PRINTS; PR01770; ERK1ERK2MAPK.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF56112; SSF56112; 1.
DR   PROSITE; PS01351; MAPK; 1.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|RuleBase:RU000304,
KW   ECO:0000256|SAAS:SAAS00574094};
KW   Complete proteome {ECO:0000313|Proteomes:UP000008792};
KW   Kinase {ECO:0000256|RuleBase:RU361165, ECO:0000256|SAAS:SAAS00574086};
KW   Magnesium {ECO:0000256|RuleBase:RU361165};
KW   Nucleotide-binding {ECO:0000256|RuleBase:RU000304,
KW   ECO:0000256|SAAS:SAAS00574135};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008792};
KW   Serine/threonine-protein kinase {ECO:0000256|RuleBase:RU000304,
KW   ECO:0000256|SAAS:SAAS00574114};
KW   Transferase {ECO:0000256|RuleBase:RU361165,
KW   ECO:0000256|SAAS:SAAS00574095, ECO:0000313|EMBL:EDW64537.1}.
FT   DOMAIN       37    325       Protein kinase. {ECO:0000259|PROSITE:
FT                                PS50011}.
SQ   SEQUENCE   375 AA;  42993 MW;  E2B753B3ADABB61D CRC64;
     MAEGNTGTSA EGAAALAAPH PNAEVIRGQI FEVGPRYRKL TYIGEGAYGM VVSADDTLTN
     QRVAIKKISP FEHQTYCQRT LREITILTRF KHENIIDIRD ILRVDSIEQM RDVYIVQCLM
     ETDLYKLLKT QRLSNDHICY FLYQILRGLK YIHSANVLHR DLKPSNLLLN KTCDLKICDF
     GLARIADPEH DHTGFLTEYV ATRWYRAPEI MLNSKGYTKS IDIWSVGCIL AEMLSNRPIF
     PGKHYLDQLN HILGVLGSPS QEDLECIINE KARNYLESLP FKPNVPWSRL FPNADALALD
     LLGKMLTFNP HKRIPVEEAL AHPYLEQYYD PGDEPVAEVP FRINMENDDI SRDALKSLIF
     EETLKFKERQ PEQAL
//