ID B4GZD1_DROPE Unreviewed; 1929 AA.
AC B4GZD1;
DT 23-SEP-2008, integrated into UniProtKB/TrEMBL.
DT 23-SEP-2008, sequence version 1.
DT 27-MAR-2024, entry version 101.
DE RecName: Full=non-specific serine/threonine protein kinase {ECO:0000256|ARBA:ARBA00012513};
DE EC=2.7.11.1 {ECO:0000256|ARBA:ARBA00012513};
GN Name=Dper\GL27344 {ECO:0000313|EMBL:EDW28149.1};
GN ORFNames=Dper_GL27344 {ECO:0000313|EMBL:EDW28149.1};
OS Drosophila persimilis (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7234 {ECO:0000313|Proteomes:UP000008744};
RN [1] {ECO:0000313|EMBL:EDW28149.1, ECO:0000313|Proteomes:UP000008744}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MSH-3 / Tucson 14011-0111.49
RC {ECO:0000313|Proteomes:UP000008744};
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 -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
CC [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1;
CC Evidence={ECO:0000256|ARBA:ARBA00001433};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
CC threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
CC Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC EC=2.7.11.1; Evidence={ECO:0000256|ARBA:ARBA00000775};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
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DR EMBL; CH479198; EDW28149.1; -; Genomic_DNA.
DR RefSeq; XP_002023946.1; XM_002023910.1.
DR STRING; 7234.B4GZD1; -.
DR EnsemblMetazoa; FBtr0192959; FBpp0191451; FBgn0164925.
DR eggNOG; KOG0192; Eukaryota.
DR eggNOG; KOG0504; Eukaryota.
DR eggNOG; KOG0619; Eukaryota.
DR HOGENOM; CLU_000987_0_0_1; -.
DR OMA; GEEVIWC; -.
DR PhylomeDB; B4GZD1; -.
DR Proteomes; UP000008744; Unassembled WGS sequence.
DR GO; GO:0044297; C:cell body; IEA:EnsemblMetazoa.
DR GO; GO:0005829; C:cytosol; IEA:GOC.
DR GO; GO:1990033; C:dendritic branch point; IEA:EnsemblMetazoa.
DR GO; GO:0043198; C:dendritic shaft; IEA:EnsemblMetazoa.
DR GO; GO:0005795; C:Golgi stack; IEA:EnsemblMetazoa.
DR GO; GO:0031902; C:late endosome membrane; IEA:EnsemblMetazoa.
DR GO; GO:0005765; C:lysosomal membrane; IEA:EnsemblMetazoa.
DR GO; GO:0071212; C:subsynaptic reticulum; IEA:EnsemblMetazoa.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0031267; F:small GTPase binding; IEA:EnsemblMetazoa.
DR GO; GO:0006914; P:autophagy; IEA:EnsemblMetazoa.
DR GO; GO:0008088; P:axo-dendritic transport; IEA:EnsemblMetazoa.
DR GO; GO:0051683; P:establishment of Golgi localization; IEA:EnsemblMetazoa.
DR GO; GO:0040011; P:locomotion; IEA:EnsemblMetazoa.
DR GO; GO:0032418; P:lysosome localization; IEA:EnsemblMetazoa.
DR GO; GO:0050774; P:negative regulation of dendrite morphogenesis; IEA:EnsemblMetazoa.
DR GO; GO:0018105; P:peptidyl-serine phosphorylation; IEA:EnsemblMetazoa.
DR GO; GO:0009966; P:regulation of signal transduction; IEA:UniProt.
DR GO; GO:1900242; P:regulation of synaptic vesicle endocytosis; IEA:EnsemblMetazoa.
DR GO; GO:0042147; P:retrograde transport, endosome to Golgi; IEA:EnsemblMetazoa.
DR GO; GO:0050808; P:synapse organization; IEA:EnsemblMetazoa.
DR GO; GO:0048488; P:synaptic vesicle endocytosis; IEA:EnsemblMetazoa.
DR Gene3D; 1.25.40.20; Ankyrin repeat-containing domain; 2.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR Gene3D; 3.80.10.10; Ribonuclease Inhibitor; 3.
DR Gene3D; 3.30.70.1390; ROC domain from the Parkinson's disease-associated leucine-rich repeat kinase 2; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR002110; Ankyrin_rpt.
DR InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR InterPro; IPR032171; COR.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR001611; Leu-rich_rpt.
DR InterPro; IPR003591; Leu-rich_rpt_typical-subtyp.
DR InterPro; IPR032675; LRR_dom_sf.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR020859; ROC_dom.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR PANTHER; PTHR24198; ANKYRIN REPEAT AND PROTEIN KINASE DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR24198:SF169; NON-SPECIFIC SERINE_THREONINE PROTEIN KINASE; 1.
DR Pfam; PF00023; Ank; 1.
DR Pfam; PF12796; Ank_2; 1.
DR Pfam; PF16095; COR; 1.
DR Pfam; PF13855; LRR_8; 1.
DR Pfam; PF00069; Pkinase; 1.
DR Pfam; PF08477; Roc; 1.
DR PRINTS; PR00449; RASTRNSFRMNG.
DR SMART; SM00248; ANK; 5.
DR SMART; SM00364; LRR_BAC; 7.
DR SMART; SM00369; LRR_TYP; 8.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF48403; Ankyrin repeat; 2.
DR SUPFAM; SSF52058; L domain-like; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS50297; ANK_REP_REGION; 1.
DR PROSITE; PS50088; ANK_REPEAT; 1.
DR PROSITE; PS51450; LRR; 3.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
DR PROSITE; PS51424; ROC; 1.
PE 4: Predicted;
KW ANK repeat {ECO:0000256|ARBA:ARBA00023043, ECO:0000256|PROSITE-
KW ProRule:PRU00023}; GTP-binding {ECO:0000256|ARBA:ARBA00023134};
KW Kinase {ECO:0000256|ARBA:ARBA00022777};
KW Leucine-rich repeat {ECO:0000256|ARBA:ARBA00022614};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000008744};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW Transferase {ECO:0000256|ARBA:ARBA00022777}.
FT REPEAT 301..333
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT DOMAIN 927..1157
FT /note="Roc"
FT /evidence="ECO:0000259|PROSITE:PS51424"
FT DOMAIN 1288..1630
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 959..1001
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1693..1712
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1929 AA; 214480 MW; 654382EA0A18668B CRC64;
MSWKFVEEPK PGTETALEAC DYFVDEVTYG SGGPGGPRLD AREEVRQIKH GELRAAVSEG
DERTVRVLLS ALGTERQIIV NMAPSGANTL LFTACQSGYE SITQRLLDAG ADGRSHAVTK
YSPLYAAVHS GHMGIARLML DRFPELIQQP TVERWLPLHA ACINGHIKLL ELLIGYKYPD
YLYQTYRDEE GQWEWRLPFD ANAHDVTGQT SLYIASILGN KQLVGVLLKW QLHCRRTLGD
SASSVSTPIT PTRKRISFGI QAIMSKLHIS GESEALEEQP PAESTESQRC PINVNLLCGA
ARETALLAAV RGGHLDVVQS LLQHGANPNI VAKPVEDQND PKCSEEIYGL SNVPIAEACK
QRSLAMLDLL LKHGARDDNG SAISMALAGG DEAILSRLLA RRVHPDSDYK INKKGLPTPV
EVNVFLPSTS NISYSAMFPN VPTIIDWHSL SSNVQLTVVR IPWLVSGVLL LNPKLQTHPR
LTEVSLTAIT RIDFSHNLLT TIPQELLHLV SLKYLNVAQN KITELPPPMG KTYSCPVLDE
LFLQDNQLTS LPAAIFHLPA LTILDISNNK LQELPFDLWR APKLRELNVA FNLLKDLPVP
PMQTSSSVWS LDKLQLQSYD EPSSNKPRNL THQELTHRNI WSGSLEIADN DMKWHQDPEL
GDGKAPGAGA SQLSSLNIAN NLFNSIPAAL PCLAVNLTRL NMSYNSLRSM GHVTSYPATL
KQLDLSHNEI SCWPSLPRIT ESDPHLLCYS YVQVPEGQEE PTYKSSASKG NASSFRASVL
KSVCRHRRHL RLEALRTLIL ADNLLTRIQL STDDATTLFN ESEDADWSVV GVSKSKVIFP
NLSMLDMTNN CLKEIPPSLH ELSSLSVLNI SGNVNITELP PHLGLLSRLW NLNTRGCLLQ
EPLRSMIESK KHKTMDIVGY LKSIYEDAQP YARMKLMVVG VAGIGKSTLL DLLRQGVGPG
SSSSSSSHRS RANENHWAKR MGHARSSSRS QRHSSTSNSN ISTVGVDIGT WICEKRKRSP
GSHGPVVFRT WDFGGQKEYY ATHQYFLSKR SLYLVLWRIS DGHKGLAELL QWLANIQARA
PNSPVIIVGT HFDAVGESIS AQQAEHLQQL IREKFIAIPD AEKIGLPRVI DSIEISCRTL
HNIHLLANII YDTSMQLRSP GSKEPMLLQK IPASYIALED IVHVIACNLR AAGRDPVLDA
EQYRRLITEQ MRLHNYKSFR DAAELQQATT WCHENGVLLH YDDATLRDYY FLDPQWLCDM
LAHVVTVREI NPFAPTGVMK LDDLQLLFRS VQVQGNGNRS YIVSLLNKFE VALTWDSRTL
LIPSLLPLQE GATPNTGTTV KLSQRSPTQG LRRILLMTYF PSGFWSRLIT RILADEQIVE
AIRNVYVAAQ DSALMAYKVA LGKWDRDPLQ HSCKAYCTAR QELAVLLTLK HPNIVPLVGI
CIKPLALVLE LAPLGGLDAL LRQYRRSGAH MGPHTFQTLV LQAARAIEYL HRRRIIYRDL
KSENVLVWEL PQPHTEDSPR NHVHIKIADY GISRQTAPSG AKGFGGTEGF MAPEIIRYNG
EEEYTEKGHE SIKECILEGS RPALTQRETQ FPTCCLDLMV LCWHEQPRRR PTASQIVSIL
SAPECIHLLD VVALPHSEKI VCGVFQSTIG MGDEERSGLE LWLPAYGSRI DILDCTPSGC
LVQCNSISCA PQPQVGPPKT PENGAQSRSR SAQRLPKMNM LCCCLVGEAI WMGDVSGNLH
AYSTSTYAHL FSYMLDPAIN NESHVFSCLY PGCMVYQWGA TSKRIENKLD CSKLLPCSES
LQSIAIDEHV SLIKCQISAL AAHNTELYIG TTWGCLIVAE LQTLRPISVF RPYENEIKAI
ITLSNDKVPL IATIGRRYRS LISRYVDSAE SSNACSAVST PTHGAAKSLP PVDVDNHIHC
LLWRAKHWT
//
