ID A0A0N1I6M3_PAPMA Unreviewed; 1671 AA.
AC A0A0N1I6M3;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 27-MAR-2024, entry version 38.
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=RR48_04393 {ECO:0000313|EMBL:KPJ12498.1};
OS Papilio machaon (Old World swallowtail butterfly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Lepidoptera; Glossata; Ditrysia; Papilionoidea;
OC Papilionidae; Papilioninae; Papilio.
OX NCBI_TaxID=76193 {ECO:0000313|EMBL:KPJ12498.1, ECO:0000313|Proteomes:UP000053240};
RN [1] {ECO:0000313|EMBL:KPJ12498.1, ECO:0000313|Proteomes:UP000053240}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ya'a_city_454_Pm {ECO:0000313|EMBL:KPJ12498.1};
RC TISSUE=Whole body {ECO:0000313|EMBL:KPJ12498.1};
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. {ECO:0000256|ARBA:ARBA00009903}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; KQ460772; KPJ12498.1; -; Genomic_DNA.
DR STRING; 76193.A0A0N1I6M3; -.
DR InParanoid; A0A0N1I6M3; -.
DR Proteomes; UP000053240; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd00992; PDZ_signaling; 1.
DR CDD; cd05609; STKc_MAST; 1.
DR Gene3D; 2.30.42.10; -; 1.
DR Gene3D; 1.20.1480.20; MAST3 pre-PK domain-like; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 2.
DR InterPro; IPR000961; AGC-kinase_C.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR037711; MAST.
DR InterPro; IPR015022; MAST_pre-PK_dom.
DR InterPro; IPR023142; MAST_pre-PK_dom_sf.
DR InterPro; IPR001478; PDZ.
DR InterPro; IPR041489; PDZ_6.
DR InterPro; IPR036034; PDZ_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR PANTHER; PTHR24356:SF414; NON-SPECIFIC SERINE_THREONINE PROTEIN KINASE; 1.
DR PANTHER; PTHR24356; SERINE/THREONINE-PROTEIN KINASE; 1.
DR Pfam; PF08926; DUF1908; 1.
DR Pfam; PF17820; PDZ_6; 1.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00228; PDZ; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF140482; MAST3 pre-PK domain-like; 1.
DR SUPFAM; SSF50156; PDZ domain-like; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 2.
DR PROSITE; PS51285; AGC_KINASE_CTER; 1.
DR PROSITE; PS50106; PDZ; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:KPJ12498.1};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000053240};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 409..719
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 720..791
FT /note="AGC-kinase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51285"
FT DOMAIN 1000..1073
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT REGION 1..67
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 96..117
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 136..203
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 365..408
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 757..923
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 963..985
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1085..1165
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1191..1214
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1229..1268
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1291..1671
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 98..117
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 138..162
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 368..383
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 902..923
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 963..979
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1102..1121
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1122..1151
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1308..1323
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1324..1341
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1347..1364
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1376..1399
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1409..1444
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1445..1555
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1592..1609
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1640..1660
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1671 AA; 181879 MW; BFD210341C5FC3E0 CRC64;
MRRSALGKSA PALSVHVKEQ CAVSRRPSRL PPPPPHHRLS LVVGSGRCSS PGTGPLSPAE
GPRWPHAHHA HPLHHALLSS SVKRGKEIDG RRWSVASLPS SGYGTTPGSS SLSSQCSSQE
RLLAAQGAYE APRAPCPHCQ QHQNSLNSSQ GSGMNWASLS DSGGSGHAPR APSPRPAPKR
VRSRSLSSPS RSPGGGSGGE GAREDAVTAM SALFASRFPT AQKHMDDKLR GLIDELTELD
KKPDRPPIER FVQRQVLEMA RDCLHKSESK QVTSSYFYDM ADSLDRLLAE TREKSAEAGA
QVAPLVTRLV LAMARPARLL ECLEFDPERF YRLLEAAEGH ARQSQGITTD IPQYIIHKLG
LSRDPLAELN APPPPPPPPQ HNASPSKGRG RQSPPGAPPG GAPPSENDYH VIKLISNGAY
GAVYLVKHKL TRQRYAMKKI SKNNLILRNQ VEQAFAERDI LSFADNPFVV TMYCSFETKR
HLCLILEFVE GGDCATLLRA GPLPPDMARH YFAEAVLAVE YLHSYGIVHR DLKPDNLLIT
ATGHIKLTDF GLSKMGLMSL ATNLYEEYAD REARQFSDKQ VCGTPEYIAP EVILRQGYGK
PVDWWSMGII LYEFLVGCVP FFGDTPEELF AHTGYGKPVD WWSMGIILYE FLVGCVPFFG
DTPEELFAHT VNDDIEWPSE EDFPIAIEAR TIITELLARN PRDRLGTGGT HQVKDHIYFY
GLDWNNLLRR KAEFIPQLEN DEDTSYFDSR CDRYNHSEAD TDEAGEGGEP GEDPLFAAFS
STSPQWRRHY NHSHSHSHSH SVVSHDSRST DSWPGTPDSA GPPTTPTAPH HHPKCPLVGT
GGGSTAESSQ TDSDDVSPAA RRRAALRPPS LAAHAHGHAH THVGHALAHS HPHPHPPVLP
RITDTSKREE KGADRVDKPE KTKPIALAAP KAMRRSASTS GLSLVIHPAE ESGVIAGGAA
SPCAGNTSST NSSRDSSPCR DPPSPFAIAN HSLIQSSKPP IVVRRGPRGF GFTIHTVRVY
YGDTDYYTMH HLVSAVSEQG AAWAAGLRAG DLITQLNGES VQGLLHTQVL KLLLTAPHAT
LRATPLDQTT IQAGGRRRAG GRRASAPPRP RPRRRCSLFR RISTKRASQE MHQMVTAAGS
GECSSSPAAS PAADSPLHAN THYQRPSSLH GLKHKLSAGE VRRASLQHMP LSPLARTPSP
SPQPQPASPT RKSFVQSVPL TKCWATGHSR CEARSPSPLA ARECGRRPWP RRDPASPLLR
RALSPDRLHP RSAEAKCSIS PLCCGVGVAV SSGGGASASR RGAGWRAPAP APPTPPPPEK
PDEPPLPRIA EEKDSPTHHA GHSKLPTRTP AKQSTPSIFT SSPKSVDRGV ADANASFASL
SLSDESFMDT SIDTSNLDTS REVFLDDSRS STEPNVTTDT SKKTSTTFET MPSSSQTDPH
SKTRQTPESS SKEEDLKKDK NKTKEKSELK KQDSIKKMEI SEIKEEKTEV KIEEKPKTEK
TMERVGSMKK SEKAEAKKEK QEKAELKKQE KMEAKKNESA KKLEGLKRQE SVEINKSPEA
VECGSGGVVV VGGAEAGRGR NSMVSKLLGV MGRKTPRDRD DDDHRPAKKQ DKHAKKKGQN
NPQTPQVVVA LPPKPNEPTI PERASEKTDI VEDKKTKKGR GRASSSSSGE K
//
