ID E2BET6_HARSA Unreviewed; 1790 AA.
AC E2BET6;
DT 30-NOV-2010, integrated into UniProtKB/TrEMBL.
DT 30-NOV-2010, sequence version 1.
DT 27-MAR-2024, entry version 81.
DE SubName: Full=Serine/threonine-protein kinase Genghis Khan {ECO:0000313|EMBL:EFN85802.1};
GN ORFNames=EAI_04645 {ECO:0000313|EMBL:EFN85802.1};
OS Harpegnathos saltator (Jerdon's jumping ant).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Formicoidea;
OC Formicidae; Ponerinae; Ponerini; Harpegnathos.
OX NCBI_TaxID=610380 {ECO:0000313|Proteomes:UP000008237};
RN [1] {ECO:0000313|EMBL:EFN85802.1, ECO:0000313|Proteomes:UP000008237}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=R22 G/1 {ECO:0000313|EMBL:EFN85802.1,
RC ECO:0000313|Proteomes:UP000008237};
RX PubMed=20798317; DOI=10.1126/science.1192428;
RA Bonasio R., Zhang G., Ye C., Mutti N.S., Fang X., Qin N., Donahue G.,
RA Yang P., Li Q., Li C., Zhang P., Huang Z., Berger S.L., Reinberg D.,
RA Wang J., Liebig J.;
RT "Genomic comparison of the ants Camponotus floridanus and Harpegnathos
RT saltator.";
RL Science 329:1068-1071(2010).
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};
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. AGC Ser/Thr
CC protein kinase family. DMPK subfamily. {ECO:0000256|ARBA:ARBA00005719}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. AGC Ser/Thr
CC protein kinase family. PKC subfamily. {ECO:0000256|ARBA:ARBA00005490}.
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DR EMBL; GL447857; EFN85802.1; -; Genomic_DNA.
DR STRING; 610380.E2BET6; -.
DR EnsemblMetazoa; XM_011139153.3; XP_011137455.1; LOC105182022.
DR InParanoid; E2BET6; -.
DR OMA; SYCEGYL; -.
DR Proteomes; UP000008237; 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: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; 1.20.5.340; -; 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; IPR020454; DAG/PE-bd.
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 PRINTS; PR00008; DAGPEDOMAIN.
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:EFN85802.1};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
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 Reference proteome {ECO:0000313|Proteomes:UP000008237};
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 120..387
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 388..458
FT /note="AGC-kinase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51285"
FT DOMAIN 1053..1103
FT /note="Phorbol-ester/DAG-type"
FT /evidence="ECO:0000259|PROSITE:PS50081"
FT DOMAIN 1123..1242
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT DOMAIN 1268..1546
FT /note="CNH"
FT /evidence="ECO:0000259|PROSITE:PS50219"
FT DOMAIN 1606..1619
FT /note="CRIB"
FT /evidence="ECO:0000259|PROSITE:PS50108"
FT REGION 991..1050
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1578..1601
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1640..1790
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 546..836
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 1008..1050
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1579..1601
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1640..1665
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1686..1710
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1761..1790
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 149
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 1790 AA; 202667 MW; 3D9573E18FE71FF4 CRC64;
MEISSIDCGK EQPYQQRDMS DSSQYLYGHL PPDIMPKGLP NNGIGGRLRQ LEGLFIGGPG
QGGRVGHTIS IETLIDVLLV LYDECCNSSL RREKTVSDFI EFVKPIASCI KSLQLTREDF
EIVKVIGRGA FGEVCVVRMR GSDKVFAMKI LNKWEMLKRA ETACFREERD VLVYGDRRWI
TNLHYAFQDD NNLYLVMDYY CGGDLLTLLS KFEDRLPEDM ARFYIAEMVL AIGSIHDLRY
VHRDIKPDNV LLDANGHIRL ADFGSCLRLF EDGTVQSNVA VGTPDYISPE ILRAMEDGQG
QYGPECDWWS LGVCMYEMLY GETPFYAESL VETYGKIMNH KNCFDFPTDD MYDVSEEAKD
LMRKLICSSE FRLGQNGIDD FKKHPWFDGV NWDTLRDSTA PYIPEVSSPS DTSNFDVDDT
DVRTSDAVPP AANSAFSALH LPFVGFSFTQ GSCISDLGCI SALSQKDKHV QILEEENARL
IQTIDDMKNL GIASPDVSPD SNNATRKLRD EINTLTKRNC ELESQLKSMD VPRELRTLDN
GDMTKFRELE KLVRCLRLEK EEAIKDKLDA QEKLKLQDKE LKDALTQRKL AMAEYTEVSD
KLSDLRQQKQ KLSRQVRDKE EELEVVMQKV DSLRHDIRKA EKLRRELENR VDEAMAETSK
ERKLRERSEE YCKQMQEETE KIRQRSLGND ASANHALATQ EINRLKAEVE KLEVQYNENL
TQQQGRFNLD IRSLQEQLHE GETRRELLER EVQLTKEKLD AARLENITDS EETINELSRR
HEREKIMLVE ENKKLMLELG ALTDSVNRLQ GERRQLEDEY EELRNKKEAI AQWEAQITEI
IQWVSDEKDA RGYLQALATK MTEELEFLKH SGGVGGVGSG TTMADKNWRN RRSQKLDKME
LLNLQSSLQS EIQAKQAISE ELTKTRSDLI ASQKELRDFK QRLDTMSHEL KRKDMQVKEL
QARLDTGDGF LERPTSQMSY LEHFLKETTS STRHGSVDSV EGDIEDNRAP SITSSKSNLS
ELSIDPTSPL SHELLNKSSS SHGQANLQPK PKSHQFLVRT FSAPTKCNHC TSLMVGLTRQ
GVVCEVCGFA CHMPCCDKVP PMCPVPHDQT KRPLGIDPTR GIGTAYEGYV KVPKMGGVKK
GWVRQFVVVC DFKLFLYDIS PDRNALPSVY VSQVLDMRDE EFSVSSVRDS DVIHATKKDI
PCIFRITTSL LEPPGLRNHT LMLADTESEK TKWVVALSEL HRILKRNNLP NTTIFRAKEL
LDNTLAFIKN VMSGAIIDPD RLVIGTEEGL FCLDLDRSEI ARVGEGKKIY LLEYVTEEQL
IVVLSGKQRH VRLVPVRALD GDEVEWIKVA ETKGCITLTT GVVRRNPLTY CLCVAIKKQS
VSQVIIYEIT RTKTRHKRIR ELMLPCLAQT LQVLSEGRLC VGYQSGFSIY SILGDHHPIS
LVHAENTLLG FLTYSAVDAL RCIELARGEF LLVFHTLAVY VDSQGRKNRD REMMYPAVPT
AVSYCEGYLL VYSETHIDVF DCTSGDWLQT LNVKRARPLN VSGSLTSCVI NDMPHVIYLS
NLHQRELLNI TPLDASGRQM TRPRRRFSLR EGNRAVRPTD RRSKMISAPT NFNHISHMGP
GNGIQIQRLL DLPTTIETAD QQHTTGHHSS SHLHSSQQRL YDSALQTPSK PAPLPPRHPP
SDTRRLSSHM SRNSGYSPHN GSTTSRRGPA PPRPTATPPS LPRTPVDQID SESVHLRSHT
PLSLGSIASL HNKEHPSGGS PRHSIASNNS SNPSTPPSPA HDHGSSSYDS
//
