ID K9J805_XENTR Unreviewed; 1300 AA.
AC K9J805;
DT 06-FEB-2013, integrated into UniProtKB/TrEMBL.
DT 02-JUN-2021, sequence version 4.
DT 27-MAR-2024, entry version 71.
DE RecName: Full=non-specific serine/threonine protein kinase {ECO:0000256|ARBA:ARBA00012513};
DE EC=2.7.11.1 {ECO:0000256|ARBA:ARBA00012513};
GN Name=tnik {ECO:0000313|Ensembl:ENSXETP00000020078};
OS Xenopus tropicalis (Western clawed frog) (Silurana tropicalis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana.
OX NCBI_TaxID=8364 {ECO:0000313|Ensembl:ENSXETP00000020078};
RN [1] {ECO:0000313|Ensembl:ENSXETP00000020078}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Nigerian {ECO:0000313|Ensembl:ENSXETP00000020078};
RX PubMed=20431018; DOI=10.1126/science.1183670;
RA Hellsten U., Harland R.M., Gilchrist M.J., Hendrix D., Jurka J.,
RA Kapitonov V., Ovcharenko I., Putnam N.H., Shu S., Taher L., Blitz I.L.,
RA Blumberg B., Dichmann D.S., Dubchak I., Amaya E., Detter J.C., Fletcher R.,
RA Gerhard D.S., Goodstein D., Graves T., Grigoriev I.V., Grimwood J.,
RA Kawashima T., Lindquist E., Lucas S.M., Mead P.E., Mitros T., Ogino H.,
RA Ohta Y., Poliakov A.V., Pollet N., Robert J., Salamov A., Sater A.K.,
RA Schmutz J., Terry A., Vize P.D., Warren W.C., Wells D., Wills A.,
RA Wilson R.K., Zimmerman L.B., Zorn A.M., Grainger R., Grammer T.,
RA Khokha M.K., Richardson P.M., Rokhsar D.S.;
RT "The genome of the Western clawed frog Xenopus tropicalis.";
RL Science 328:633-636(2010).
RN [2] {ECO:0000313|Ensembl:ENSXETP00000020078}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (DEC-2012) to UniProtKB.
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 -!- SIMILARITY: Belongs to the protein kinase superfamily. STE Ser/Thr
CC protein kinase family. STE20 subfamily.
CC {ECO:0000256|ARBA:ARBA00008874}.
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DR Ensembl; ENSXETT00000020078; ENSXETP00000020078; ENSXETG00000009142.
DR AGR; Xenbase:XB-GENE-480067; -.
DR Xenbase; XB-GENE-480067; tnik.
DR eggNOG; KOG0587; Eukaryota.
DR HOGENOM; CLU_001831_2_0_1; -.
DR TreeFam; TF105138; -.
DR Bgee; ENSXETG00000009142; Expressed in brain and 12 other cell types or tissues.
DR ExpressionAtlas; K9J805; baseline.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004672; F:protein kinase activity; IEA:InterPro.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR001180; CNH_dom.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR PANTHER; PTHR47096:SF1; CNH DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR47096; MISSHAPEN LIKE KINASE 1; 1.
DR Pfam; PF00780; CNH; 1.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00036; CNH; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS50219; CNH; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 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, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Kinase {ECO:0000256|ARBA:ARBA00022777};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW Transferase {ECO:0000256|ARBA:ARBA00022777}.
FT DOMAIN 1..265
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 987..1274
FT /note="CNH"
FT /evidence="ECO:0000259|PROSITE:PS50219"
FT REGION 252..323
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 368..811
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 907..936
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 264..296
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 297..312
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 368..441
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 442..462
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 511..525
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 543..566
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 603..617
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 637..656
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 666..707
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 746..771
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 774..788
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 921..936
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 30
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 1300 AA; 148378 MW; 49DC6C27360266D0 CRC64;
SHSYSPIGNG TYGQVYKGRH VKTGQLAAIK VMDVTGDEEE EIKQEINMLK KYSHHRNIAT
YYGAFIKKNP PGMDDQLWLV MEFCGAGSVT DLIKNTKGNT LKEEWIAYIC REILRGLSHL
HQHKVIHRDI KGQNVLLTEN AEVKLVDFGV SAQLDRTVGR RNTFIGTPYW MAPEVIACDE
NPDATYDFKS DLWSLGITAI EMAEGAPPLC DMHPMRALFL IPRNPAPRLK SKKWSKKFQS
FIESCLVKNH SQRPTTEQLM KHPFIRDQPN ERQVRIQLKD HIDRTKKKRG EKDETEYEYS
GSEEEEEDND SGEPSSILNL PGESTLRRDF LRLQLANKER SEALRRQQLE QQQRENEEHK
RQLLAERQKR IEEQKEQRRR LEEQQRREKE MRKQQERDQR RRYEEQMRRE EERRRAEHEK
EYKRKQLEEQ RQAERLQRQL QQERDYLVSL QQQQQQQQRS SEKKPLYHYK EGLNPAEKPA
WAKEVEERSR LNRQSSPAMP HKVANRISDP NLPPRSESFS ISGVQPARTP PMHRPIDPQQ
LPLLVSVKTQ GSSLSASQSV HEQSAKGMSA FQEGIISHRP EMPRQNSDPT SENPPLPPRI
EKFDRSSWLR QEEDLPPKVP QRTTSISPAL ARKNCAGNGN SLGNSLATQP VRASNPDLRR
TETVIENPIQ RISSGSSSSS STPSSQPSSQ GGSQPGSQAG SSERNRARAG NNKPEGSPLL
PHETSNSKPE ENRDVTRPSR PADLTALAKE LRELRIEETN RPIKKVTDYS SSSEESESSE
EEEGESEAQD GTVPVSDIPR LIPTGISGNE PYNAGTQGME MSQSETFRSI SREGTLMIRE
TSGDKKRTGH AESNGFAGHI NLPDLVQQSH SPVGTPTEAL GRGPTHAQEM DTVNEYGVAN
NTKASFTPFV DPRVYQTSPT DNDDEEDEDD DDDEETSATA LFTSELLRQE QAKLNEARKI
SVVNVNPTNI RPHSDTPEIR KYKKRFNSEI LCAALWGVNL LVGTENGLML LDRSGQGKVY
NLINRRRFQQ MEVLEGLNVL VTISGKKNKL RVYYLSWLRN RILHNDPEVE KKQGWITVGE
LEGCVHYKVV KYERIKFLVI ALKNAVEIYA WAPKPYHKFM AFKSFTDLQH RPLLCDLTVE
EGQRLKVIFG SSTGFHVIDV DSGNTYDIYI PSHIQGNITP HAIVILPKTD GMEMLVCYED
EGVYVNTYGR ITKDVVLQWG EMPTSVAYIH SNQIMGWGEK AIEIRSVETG HLDGVFMHKR
AQRLKFLCER NDKVFFASVR SGGSSQVFFM TLNRNSMMNW
//
