ID A0A3B0JQ00_DROGU Unreviewed; 1641 AA.
AC A0A3B0JQ00;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE RecName: Full=non-specific serine/threonine protein kinase {ECO:0000256|ARBA:ARBA00012513};
DE EC=2.7.11.1 {ECO:0000256|ARBA:ARBA00012513};
GN ORFNames=DGUA_6G000681 {ECO:0000313|EMBL:SPP73238.1};
OS Drosophila guanche (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7266 {ECO:0000313|EMBL:SPP73238.1, ECO:0000313|Proteomes:UP000268350};
RN [1] {ECO:0000313|Proteomes:UP000268350}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Alioto T., Alioto T.;
RL Submitted (JAN-2018) to the EMBL/GenBank/DDBJ databases.
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 -!- SIMILARITY: Belongs to the protein kinase superfamily. AGC Ser/Thr
CC protein kinase family. DMPK subfamily. {ECO:0000256|ARBA:ARBA00005719}.
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DR EMBL; OUUW01000001; SPP73238.1; -; Genomic_DNA.
DR STRING; 7266.A0A3B0JQ00; -.
DR Proteomes; UP000268350; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0007010; P:cytoskeleton organization; IEA:UniProt.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd20809; C1_MRCK; 1.
DR CDD; cd00132; CRIB; 1.
DR CDD; cd01243; PH_MRCK; 1.
DR CDD; cd05597; STKc_DMPK_like; 1.
DR Gene3D; 3.30.60.20; -; 1.
DR Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR000961; AGC-kinase_C.
DR InterPro; IPR046349; C1-like_sf.
DR InterPro; IPR001180; CNH_dom.
DR InterPro; IPR000095; CRIB_dom.
DR InterPro; IPR031597; KELK.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR002219; PE/DAG-bd.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR001849; PH_domain.
DR InterPro; IPR017892; Pkinase_C.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR PANTHER; PTHR22988; MYOTONIC DYSTROPHY S/T KINASE-RELATED; 1.
DR PANTHER; PTHR22988:SF66; SERINE_THREONINE-PROTEIN KINASE GENGHIS KHAN; 1.
DR Pfam; PF00130; C1_1; 1.
DR Pfam; PF00780; CNH; 1.
DR Pfam; PF15796; KELK; 1.
DR Pfam; PF00069; Pkinase; 1.
DR Pfam; PF00433; Pkinase_C; 1.
DR SMART; SM00109; C1; 1.
DR SMART; SM00036; CNH; 1.
DR SMART; SM00285; PBD; 1.
DR SMART; SM00233; PH; 1.
DR SMART; SM00133; S_TK_X; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF57889; Cysteine-rich domain; 1.
DR SUPFAM; SSF50729; PH domain-like; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS51285; AGC_KINASE_CTER; 1.
DR PROSITE; PS50219; CNH; 1.
DR PROSITE; PS50108; CRIB; 1.
DR PROSITE; PS50003; PH_DOMAIN; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
DR PROSITE; PS00479; ZF_DAG_PE_1; 1.
DR PROSITE; PS50081; ZF_DAG_PE_2; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU10141};
KW Coiled coil {ECO:0000256|ARBA:ARBA00023054, ECO:0000256|SAM:Coils};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:SPP73238.1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT DOMAIN 100..369
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 370..440
FT /note="AGC-kinase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51285"
FT DOMAIN 996..1046
FT /note="Phorbol-ester/DAG-type"
FT /evidence="ECO:0000259|PROSITE:PS50081"
FT DOMAIN 1066..1184
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT DOMAIN 1210..1496
FT /note="CNH"
FT /evidence="ECO:0000259|PROSITE:PS50219"
FT DOMAIN 1553..1566
FT /note="CRIB"
FT /evidence="ECO:0000259|PROSITE:PS50108"
FT REGION 439..478
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 551..577
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1615..1641
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 646..684
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 439..474
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 129
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 1641 AA; 187238 MW; 08999E637392CD9A CRC64;
MEYESSEFSD ITTGSCKKRL NFLKYILSDT TVDQKWASDL GEDTEGHQFS LDYLLDTFIV
LYDECSNSSL RREKGVSDFL KLSKPFVHVV RKLRLGRDDF DILKIIGRGA FGEVCVVQMI
STEKVYAMKI LNKWEMLKRA ETACFREERD VLVFGDRQWI TNLHYAFQDN INLYLVMDYY
CGGDLLTLLS KFEDKLPEDM AKFYITEMIL AIHSIHQIKY VHRDIKPDNV LLDKRGHVRL
ADFGSCLRLD KDGTVQSNVA VGTPDYISPE ILRAMEDGKG RYGTECDWWS LGVCMYEMLY
GETPFYAESL VETYGKIMNH QNCFNLPTQE TLNYKVSEMS QDLLCKLICI PENRLGQNGI
QDFMDHPWFV GIDWKNIRCG LAPYVPEVSS PTDTSNFDVD DNDVRLTDSM PPSANPAFSG
FHLPFIGFTF SLNTSSPADS KANQSSGFED DNTSCSLQQS SNLPSNNSEA SVDSVQDKKQ
MKALTEQIAA FKQEKLELTK QHSEIFERLK TQEAELQDAI SQRNVAMVEY SEVTEKLSEL
RNQKQKLSRQ VRDKEEELDG AMQKNDSLRN ELRKSDKTRR ELELHIEDAV IEASKEKKLR
EHAEECCRQL QLELRKCNSS VETTMPMSIS SEMSSYEIER LEMQYSEKLN HQQTRHNLEM
EALREQLENS NLELSKELHQ TQDRLKYTQL ESITDSAETL LELKKQHDLE KSSWFEEKQR
LSTEVSLKAK NLKDLQAEDD EIFKELRMKR EAINQWERQM AEIIQWVSDE KDARGYLQAL
ATKMTEELEY LKHVGTFNNN GVDNKNWRNR RSQKLDKMEL LNLQSALQRE IQAKAIISEE
LSQTRSDLIS IQKEVRDYKK RYDSILHDFQ KKETELRDLQ KGGLEYSESF LNKSTHQGLS
SAFFRDISKS EMIDAADSFG NDSSDSFIGT PNFFQSGNSG MLFNYEPKYA GKSKDGGSLA
AMKDASVSDI SREDAELLMK ESQKKVASSN PSNTAIHQFL VRTFSSPTKC NHCTSLMVGL
TRQGVVCEIC GFACHTICCQ KVPTTCPVPM DQTKRPLGID PTRGIGTAYE GYVKVPKSGV
IKRGWIRQFV VVCDFKLFLY DISPDRCALP SVSVSQVLDM RDPEFSVGSV RESDVIHAAK
KDVPCIFKIK TALIESGLSL NTLMLADNES EKSKWVIALG ELHRILKRNS LPNTAIFKVY
EILDNTLSLI RNALCSVIIY PNQILLGTED GLFYINLDQY EIARIGESKK ILQLWYIEEE
QILVILCGKQ RNLRLLPIRA LEASDVEWIK VVESKNCISA CTGIIRRFPN IVYSFIIALK
RPNNHTQIVV YEINRTRTRH QKTCEFTIGY LAQHLQILSD MRLVVAHQSG FTAYFLRGEA
TAMSLVHPEN QLCAFLNYSG VDAVRVIEIL CPSGGNFGEY LLVFQTLAIY VDLQGRKSRD
REIMYPAFPT YITFCDGHLL VFSETHLDIF NTQTAEWVQS IGLKQSIPLN NQGNVVLSSV
NDTPLIVYLS NIHTKGLLQY REGNRKGMAN IKRRFSIREI NKTIKSDRRS KMISAPTNFN
HISHMGPGEG IQNQRLLDLP TTLETADCSP IIHSLSSIPS RKSNFLEQVD ANSDDYGNDN
IISRTPSPMA SSFMDGLSNN D
//
