ID A0A164KNT3_9CRUS Unreviewed; 2541 AA.
AC A0A164KNT3;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 33.
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=APZ42_033871 {ECO:0000313|EMBL:KZS03423.1};
OS Daphnia magna.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Crustacea; Branchiopoda;
OC Diplostraca; Cladocera; Anomopoda; Daphniidae; Daphnia.
OX NCBI_TaxID=35525 {ECO:0000313|EMBL:KZS03423.1, ECO:0000313|Proteomes:UP000076858};
RN [1] {ECO:0000313|EMBL:KZS03423.1, ECO:0000313|Proteomes:UP000076858}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Xinb3 {ECO:0000313|EMBL:KZS03423.1,
RC ECO:0000313|Proteomes:UP000076858};
RC TISSUE=Complete organism {ECO:0000313|EMBL:KZS03423.1};
RA Gilbert D.G., Choi J.-H., Mockaitis K., Colbourne J., Pfrender M.;
RT "EvidentialGene: Evidence-directed Construction of Genes on Genomes.";
RL Submitted (MAR-2016) 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 -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KZS03423.1}.
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DR EMBL; LRGB01003275; KZS03423.1; -; Genomic_DNA.
DR STRING; 35525.A0A164KNT3; -.
DR Proteomes; UP000076858; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProt.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0009966; P:regulation of signal transduction; IEA:UniProt.
DR GO; GO:0034976; P:response to endoplasmic reticulum stress; IEA:UniProt.
DR Gene3D; 1.25.40.20; Ankyrin repeat-containing domain; 3.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR Gene3D; 3.80.10.10; Ribonuclease Inhibitor; 3.
DR Gene3D; 3.30.70.1390; ROC domain from the Parkinson's disease-associated leucine-rich repeat kinase 2; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR002110; Ankyrin_rpt.
DR InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR InterPro; IPR032171; COR.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR001611; Leu-rich_rpt.
DR InterPro; IPR025875; Leu-rich_rpt_4.
DR InterPro; IPR003591; Leu-rich_rpt_typical-subtyp.
DR InterPro; IPR032675; LRR_dom_sf.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR011047; Quinoprotein_ADH-like_supfam.
DR InterPro; IPR020859; ROC_dom.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR PANTHER; PTHR24198; ANKYRIN REPEAT AND PROTEIN KINASE DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR24198:SF169; NON-SPECIFIC SERINE_THREONINE PROTEIN KINASE; 1.
DR Pfam; PF00023; Ank; 2.
DR Pfam; PF12796; Ank_2; 1.
DR Pfam; PF13637; Ank_4; 1.
DR Pfam; PF16095; COR; 1.
DR Pfam; PF12799; LRR_4; 1.
DR Pfam; PF00069; Pkinase; 1.
DR Pfam; PF08477; Roc; 1.
DR PRINTS; PR00449; RASTRNSFRMNG.
DR SMART; SM00248; ANK; 8.
DR SMART; SM00364; LRR_BAC; 6.
DR SMART; SM00365; LRR_SD22; 3.
DR SMART; SM00369; LRR_TYP; 8.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF48403; Ankyrin repeat; 2.
DR SUPFAM; SSF52058; L domain-like; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR SUPFAM; SSF50998; Quinoprotein alcohol dehydrogenase-like; 1.
DR PROSITE; PS50297; ANK_REP_REGION; 3.
DR PROSITE; PS50088; ANK_REPEAT; 4.
DR PROSITE; PS51450; LRR; 3.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
DR PROSITE; PS51424; ROC; 1.
PE 4: Predicted;
KW ANK repeat {ECO:0000256|ARBA:ARBA00023043, ECO:0000256|PROSITE-
KW ProRule:PRU00023};
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Differentiation {ECO:0000256|ARBA:ARBA00022782};
KW GTP-binding {ECO:0000256|ARBA:ARBA00023134};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:KZS03423.1};
KW Leucine-rich repeat {ECO:0000256|ARBA:ARBA00022614};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Reference proteome {ECO:0000313|Proteomes:UP000076858};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW Transferase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:KZS03423.1}.
FT REPEAT 50..82
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 86..118
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 223..246
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 405..437
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT DOMAIN 1043..1257
FT /note="Roc"
FT /evidence="ECO:0000259|PROSITE:PS51424"
FT DOMAIN 1818..2117
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 1453..1484
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1697..1758
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1742..1756
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 1850
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 2541 AA; 284304 MW; 1B4F0EC0EC26D47C CRC64;
MSIPSSPNSD DLEDFPGRLL HQAALWDNAE LLEDLLHADQ LQHIDGVDAW GRTPLHAAAT
TENSSCLRIL LQSGANPNIP CGPRGEYRTS LHVTAEYGHV NNLRLLLSHD ARIDVRDGLG
FSPLDLALKG SHIECASALK TAQSTQEACR VEIFNGLLKA CIEGSPDLML KLFKELKEDL
QLVINMMVEG SNTLLFKASE IGHREIVHLL LANGADARVH PVTKYSPLYI ACYNGHKEVV
ELLLRKFPEL VQTPTVEKWF PSHGCCIQGH VQVLDLLLKY PYPSSIMKKY TDKTGNYEYE
LPFDINAKDV SGQTVLYIAA YMGNLKMVEL ILKYRVKGKT LKSNDQTTTV LSATESITAK
KRISDSIQAL MSRLNVNLKP DSATPAANIQ QTLSPVNVDV YCDHGTQTAL HAAVKSKHFA
IASLILGAGA NPNLTIYLNE EELSKLRSRT ALDEYVFTGS SVLVEAVRQR DMGMIDLLLK
HGARDLESKA LYVAVQAKDD IITSKLLALK SHIDRENSIN KKAGSPNESR GFASLSQVFP
TNAVMINWHG QQCLEYIRPQ WLSEAAVSLN PKMKLHPRAY HVALHSITRI DLSNNVLVEL
PPCMLQLQSI RHLNVAQNKI ERLPSGLYNC PLLEELLLDF LPDALFKLPS LAILDVSNNK
LQHIPIDMWT APKLKEMNAS FNLLVDLPNF LTDVAFDLTS SGDSGKKLDF SAPRSNKSTP
DKFNLSFSDE DSLGDARMMR SMQLATFNLT PQKLVHDSLW SHTVDINETL PADMDDMPQS
CSQLVHLNLA HNNFSSVPVS LACIAVNLVR LNMSFNKLTD IGPLSNYPHG LKQLDLSHNQ
IENWPPFSNW DILQLDEPMS PLSTSSPFLS SSATITCFAG IDRNPPKTPV TQGRKFHKSS
KVVACAHRRH HKLEGLRTLV LGDNQMTGIH LWMDEGLEED VDTLVSSAHK SKLLFPNLSA
LDISNNRIRE IPNVIHELSN LAVFNVSGNP DIVELPPRMG LLSKLWNLNV RGCNLQEPLR
SMIESKKYKT MDVVGYLKSI LEDARPYARM KLMLVGVQGI GKTSLLEQLR QEGTGSYKKK
PPEHWAKRMG NRNIHSRTPR GVNLSTVGVD IGDWTYDKKA KGHGPVTFRT WDFAGQKEYY
ATHQYFLSKR SLYLVLWRIT DGVKGIDEIF HWLVNIQARA PNSPVLIVGT HYDLVKDTFP
SSYSEDLQQL VRDRFINVVD AEKCGLPRVL DTIEISCRTR HNVRLLCNLI YDAVFSLKLP
GSKERMLEQR IPATYLALED VIGLLATEQK NCGRDPVLSA EEYRVGVAHI MNSRFRMSFR
DTAELNQATA FLHENGVMLH YEDATLKDLY FLDPQWLCDM LAHVVTIREI NPFAPNGIMR
LEDLQLVFRS STSAPAEAQA YVVNLLNKFE VALTWDSRTL LIPSLLPTED QTAYDLPGSD
VRVKIPVRSR GRAMRPRKGP RFNRAVSMPS RPGSAAAQGH KGFPSEETIT DGKCEVSFQS
DMETAIYRLL LLSYVPTGFW SRLITRLLAE DSIVDTLRSY FNIPRHVDAD LTHTLEWKAE
WRCWQTGIEL HYLGTTLLRI KEVANRVGVS PFDYRAFRYI AKQEGHWSEL DTASAAMIEI
FLPNETIAIR YQTFALEPSV ESVTKLLTIS VDHIDTLLED WYPILGTRFV HTSEGKYLVT
RLVPCPMCLC GLNPPADSPH ERPQENHQFF PLKTEPVARG SRNSARSEGA DSGVGHESPV
LSRKTSTEEH SNIQELLRSH SSHSETVYSF TVEECILLSH GNRHVHCPVH NDIHLAQVAP
DTMFMDIGER NIVNGQNIKR GGLLGRGAFG FVYRATANIN GNPNAEVAVK MLQPIDPGHE
ARSSVIQIYK AAISQWERDP LQYACKAYCT VRQELAILLT LRHANIVPFI GLCTEPLALV
LDLAPLGALD SNLRNFRRSG AKLNLSVIQQ IVVQIAKALE YLHQQRIIYR DLKSENVLVW
SLPSPDERQP EVKVDVKLAD YGISRISLPT GAKGFGGTEG FMAPEIMRFN GEEEYTDKVD
CFSFGMFLYE LLTLRQPFES HESVKEFILE GGRPSITPRD ATHPVYLLDL MVLCWSQQPK
DRPTASQIVS IASAPEFTHL LDVVSLNHNG FCTDGIAVPV PNSSEETLHE LWLSSTACQV
DLLLASSQPP EIANGCGSWL DYYTLESEID QPVTAACLVG ESVWLGDARG QIFCFSTRTY
QCLFRYSLEP DSSCTASIRR LIHLPSLHRV AVALANGRLF LCRDDFIPLT STQGEGTFVM
TELGLGGSGA PLHCMAAIYS TSRGKVELWC GQSQGSICVF ALGEGVVIGQ ELINHYDPVL
PGLEVLQIVA VDNLIIENHV DTFDYEEEMP NENVIETTSS VIWSYVYPGC VVYRWCANTR
RILHRLDCSK LAPCSESLQS ISIEEHLSPG RCQVTSLAVQ GRELYIGTTW GCLIVAEASS
LRPITVFRPY EDEIRVILPL SSYDKEKEKQ SLLVATIGKG YRNLLHRYGS WTHFNKSSSS
GYVSERNQNM QVLLWRAGDW I
//
