ID A0A194Q6K8_PAPXU Unreviewed; 1560 AA.
AC A0A194Q6K8;
DT 05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2016, sequence version 1.
DT 27-MAR-2024, entry version 36.
DE SubName: Full=Serine/threonine-protein kinase Genghis Khan {ECO:0000313|EMBL:KPJ01172.1};
GN ORFNames=RR46_03043 {ECO:0000313|EMBL:KPJ01172.1};
OS Papilio xuthus (Asian swallowtail butterfly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Lepidoptera; Glossata; Ditrysia; Papilionoidea;
OC Papilionidae; Papilioninae; Papilio.
OX NCBI_TaxID=66420 {ECO:0000313|EMBL:KPJ01172.1, ECO:0000313|Proteomes:UP000053268};
RN [1] {ECO:0000313|EMBL:KPJ01172.1, ECO:0000313|Proteomes:UP000053268}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ya'a_city_454_Px {ECO:0000313|EMBL:KPJ01172.1};
RC TISSUE=Whole body {ECO:0000313|EMBL:KPJ01172.1};
RX PubMed=26354079; DOI=10.1038/ncomms9212;
RA Li X., Fan D., Zhang W., Liu G., Zhang L., Zhao L., Fang X., Chen L.,
RA Dong Y., Chen Y., Ding Y., Zhao R., Feng M., Zhu Y., Feng Y., Jiang X.,
RA Zhu D., Xiang H., Feng X., Li S., Wang J., Zhang G., Kronforst M.R.,
RA Wang W.;
RT "Outbred genome sequencing and CRISPR/Cas9 gene editing in butterflies.";
RL Nat. Commun. 6:8212-8212(2015).
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. PKC subfamily. {ECO:0000256|ARBA:ARBA00005490}.
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DR EMBL; KQ459386; KPJ01172.1; -; Genomic_DNA.
DR STRING; 66420.A0A194Q6K8; -.
DR Proteomes; UP000053268; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
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:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd20809; C1_MRCK; 1.
DR CDD; cd01243; PH_MRCK; 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; 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 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; 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; PS50003; PH_DOMAIN; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 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};
KW Coiled coil {ECO:0000256|ARBA:ARBA00023054, ECO:0000256|SAM:Coils};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:KPJ01172.1};
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};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000053268};
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 97..356
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 357..424
FT /note="AGC-kinase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51285"
FT DOMAIN 969..1019
FT /note="Phorbol-ester/DAG-type"
FT /evidence="ECO:0000259|PROSITE:PS50081"
FT DOMAIN 1039..1157
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT DOMAIN 1183..1463
FT /note="CNH"
FT /evidence="ECO:0000259|PROSITE:PS50219"
FT REGION 423..445
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 919..965
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1539..1560
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 450..716
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 919..933
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 941..960
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1560 AA; 171344 MW; 6F108FA1A7198ADE CRC64;
MSDEEDSSPD RALVPTNNVP VKGIKRLKQI ETMFISRRLQ GPRNGFSAET LLDMLLVLYD
ECCNSSLRRE KAVADFIQYV KPVATALKRL RLSRDDFELV KVIGRGAFGE VCVVRASFMQ
GTDGGGNMAA AAGGTVSSTT GERVYAMKIL NKWEMLKRAE TACFQEERDV LVFGDRRWIT
NLHYAFQDEH NLSSINSLVK QTNTFFKNER DIKPDNVLLD ASGHIRLADF GSCLRLGDDG
KVQSNVAVGT PDYISPEILR AMEDGQGRYG PECDWWSLGV CMYEMLFGET PFYAESLVET
YGKIMNHARC FHCPPPDDLA PQVSEEAKDL IRRLICSSEN RLGKNGLQDF KSHPWFAGLE
WDNVREMQAP FVPDVSSPTD TSNFDVDDTD IAVPPPPPSA AFSGRHLPFV GFTFTAGSRL
SDLGAPTPLS PAKNAPSQQA PSNAGDRAAL KALERENALL AQTIAELRSG GSGLDVTSEE
LIQLKEELST LSKRNSDLEA QLRCHEQLTA GVTTTDSSSP QDVPTRLREL ELLVASLNSE
KDELIKDKTD AQEKLRLQDK ELKDALSQCK LAMAEYNEVS ERLSELRQQK QKLSRQVRDK
EEELEVAMQK IDALRQDIRR SDKGRRELEA RLDTAISEAT KERKLREETL RSQREGMAAA
TGPAADVARL QADVEALELQ YKESLAQQQA RYNAELASLR EQLQEGDAVR NVLNRELQTS
KEKLESRRLE QMSDSEDKQM LINDNRKLAK DLDAIADIIR WVADEKEARG YLQALATKMT
EELDYLKHAS SGRSGMVPPS SPPAVGWAGG GAGGGAGAAG GGAGAAGAAG GWRNRRSQKL
DKMEILTLQS SLHSEIQAKQ AVGEELSRTR AELLASQSMV FSVLDRPPSQ MSYLDQFLKD
APAERHYDNV ASMNNEQKMY GSQQSSALSG SADSPEEVEQ RAASPASTKS SPSDMSTDPS
LGPGGKQKIH QFLVRTFSSP TKCNHCTSLM IGLTRQGVVC ETCGLAVHTR CCSRVAARCP
LPPERSRRPL GIDPARGQGT AYEGYVKVPK PGGVKKGWMR QFVVVCDFKL FLYDISQDRN
ALPSVCVSQV LDMRDPEFSV TSVKDSDVIH ASKRDIPCIF RISTSQLEGG KRYHTLMLAE
SESEKTKWVV ALSELHRILK RNNLPDKCVY SACVVGEASG ALVRGAACAC VLERGRVCVG
GEPGLALLDL ERAELVPRRA HAPVARMRYV PHEQLLVVIA GRGRHVRLVP IRALECPEVE
SVKLAEAKGA VDLAVGELSA STYGFAVVCK RQNSWVVYVY EITRTAARRR RVAELRAPGA
VLSVQLSRAR LVLGYRGGFA AHALPEPRRA QDQPAVSLVH PENQVNMFLS HSGARPLCAV
QAAGGDWLLV FSALALYVDR AGMRARDAEI MYTAQPLYHA INDTHLMIFT SSHIDIYEIE
SGEWVQTLNL PNSRPLDECG YIVCVGAEGP LNLETTSWGS NKRRFSVREQ SHQAIEAHNR
LSIGGGSQGS GSLLERSITP LSLGSMSSLH DVLKVGTDMG EGLHSEDSSC GASPPHPMDP
//
