ID A0A151I4B6_9HYME Unreviewed; 1891 AA.
AC A0A151I4B6;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 27-MAR-2024, entry version 41.
DE SubName: Full=Serine/threonine-protein kinase MRCK beta {ECO:0000313|EMBL:KYM83707.1};
GN ORFNames=ALC53_05821 {ECO:0000313|EMBL:KYM83707.1};
OS Atta colombica.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Formicoidea;
OC Formicidae; Myrmicinae; Atta.
OX NCBI_TaxID=520822 {ECO:0000313|EMBL:KYM83707.1, ECO:0000313|Proteomes:UP000078540};
RN [1] {ECO:0000313|EMBL:KYM83707.1, ECO:0000313|Proteomes:UP000078540}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Treedump-2 {ECO:0000313|EMBL:KYM83707.1};
RC TISSUE=Whole body {ECO:0000313|EMBL:KYM83707.1};
RA Nygaard S., Hu H., Boomsma J., Zhang G.;
RT "Atta colombica WGS genome.";
RL Submitted (SEP-2015) 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 -!- 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; KQ976482; KYM83707.1; -; Genomic_DNA.
DR STRING; 520822.A0A151I4B6; -.
DR Proteomes; UP000078540; 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:KYM83707.1};
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:UP000078540};
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 118..385
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 386..456
FT /note="AGC-kinase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51285"
FT DOMAIN 1155..1205
FT /note="Phorbol-ester/DAG-type"
FT /evidence="ECO:0000259|PROSITE:PS50081"
FT DOMAIN 1225..1344
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT DOMAIN 1370..1648
FT /note="CNH"
FT /evidence="ECO:0000259|PROSITE:PS50219"
FT DOMAIN 1708..1721
FT /note="CRIB"
FT /evidence="ECO:0000259|PROSITE:PS50108"
FT REGION 1093..1127
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1681..1703
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1739..1828
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1847..1891
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 461..488
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 547..837
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 923..964
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 1110..1127
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1739..1766
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1787..1811
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1862..1891
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 147
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 1891 AA; 214329 MW; F293D4F2B3B101F3 CRC64;
MSSVDCGKKQ HYLQGDMSDL SRYLYGHLPP DVMLKGLSNN GIGGKLCQLE GLFIGDSAQS
GRAGHIVSIE TLIDVLLVLY DECCNSSLRR EKTVSDFIEF VKPITSCIKN LQLTREDFEI
VKVIGRGAFG EVCVVRMRGS DKVFAMKILN KWEMLKRAET ACFREERDVL VYGDRRWITN
LHYAFQDDNN LYLVMDYYCG GDLLTLLSKF EDRLPEDMAR FYIAEMVLAI GSIHDLRYVH
RDIKPDNVLL DANGHIRLAD FGSCLRLFED GTVQSNVAVG TPDYISPEIL RAMEDGQGQY
GPECDWWSLG VCMYEMLYGE TPFYAESLVE TYGKIMNHKN CFDFPMDAMY DVSEEAKDLM
RKLICSSEFR LGQNGIDDFK KHPWFDGVDW DTLRDSTAPY IPEVSSPSDT SNFDVDDTDV
RTSDAVPPAA NSAFSALHLP FVGFSFTQGS CISDLGCIST LSQTDKRIQI LEEENIRLVQ
TIDDMKNHSS ISHSSPGISP DSNNATRKLQ DEINTLTKRN CELESQLKSM DIPRELRTLD
NGDMMKYREL EKLVRCLRLE KEEAIKDKLD AQEKLKLQDK ELKDALTQRK LAMTEYTEVS
DKLSELRQQK QKLSRQVRDK EEELEVAMQK VDTLRHDIRK AEKLRRELEN RIDEAMAETS
KERKLRERSE EYCKQMQEEM EKIRQRSLGN DASANHTLAT QEINRLKAEV EKLEVQYNEN
LTQQQSRFNL EIRSLQEQLH EAETRRELLE REVQLTKEKL DAARLENITD SEETINELNR
RHERERIILV EENKKLVLEL GALTDSVNRL QSERRQLEDE YEELRNKKEA IAQWEAQITE
IIQWVSDEKD ARGYLQALAT KMTEELEFLK HSGGIGGVGS GTTMTDKNWR NRRSQKLDKM
ELLNLQSSLQ SEIQAKQAIS EELTKTRSDL IAAQKELRDF KQRLDTMSHE LKRKDMQVKE
LQARLDTGDG LRYAILISRL QSASVYWRNE LRVGPLVAHL QTIFVTAVSS SDTTSKPPNI
VSTKPQRIIV HQPSSPLPVM RAPRITTCRL LTRFVPVNTF ISQNAVTISP PVLERPTSQM
SYLEHFLKET TSSTRHGSVD SVEGDIEDNR APSITSSKSN LSELSIDPTS PLSHELLNKS
SSTHGQINLQ PKPKSHQFLV RTFSAPTKCN HCTSLMVGLT RQGVVCEVCG FACHMPCCDK
VPSMCPVPHD QTKRPLGIDP TRGIGTAYEG YVKVPKMGGV KKGWVRQFVV VCDFKLFLYD
ISPDRNALPS VYVSQVLDMR DEEFSVSSVR DSDVIHATKK DIPCIFRITT SLLEPPGLRN
HTLMLADTES EKTKWVVALS ELHRILKRNN LPNTTIFRAK ELLDNTLAFI KNVMSGAVID
PDRLVIGTEE GLFCLDLDRN EIARVGEGKK IYLLEYVTEE QLIVVLSGKQ RHVRLVPVRA
LDGDEVEWIK VAETKGCITL TTGVVRRNPL NYCLCVAIKK QNASQIIIYE ITRTKTRHKR
IRELMLPCHA QTLQILSEGR LCVGYPSGFS IYSILGDHHP ISLVHAENTL LGFLTYSAVD
ALRCIELTRG EFLLVFHTLA VYVDNQGRKS RDREIMYPAV PMAVSYCEGY LLVYSETHID
VFDCTSGDWL QTLNVKRARP LNISGSLTSC VINDMPYVIY LSNLHQRELL NLMPLDASGR
QMTRPRRRFS LREGNRAVRP TDRRSKMISA PTNFNHISHM GPGNGIQIQR LLDLPTTLET
ADQQHTSHHG SSHLHSSQQR LYDATLQTPN KPAPLPPRHP PSDARRLSSH ISRNSGYSPH
NGSTTSRRGP APPRPTATPP SLPRTPVDQI DSESLHLRSH TPLSLGSIAS LHNKEHPSGG
SPRHSIASNN SSNPSTPPSP AHDHGSSSYD S
//
