TLK1B_DANRE
ID TLK1B_DANRE Reviewed; 756 AA.
AC Q90ZY6;
DT 23-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 110.
DE RecName: Full=Serine/threonine-protein kinase tousled-like 1-B;
DE EC=2.7.11.1;
DE AltName: Full=PKU-beta;
DE AltName: Full=Tousled-like kinase 1-B;
GN Name=tlk1b; Synonyms=tlk1; ORFNames=wu:fe11e12;
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Chou C.-M., Lee I.-L., Leu J.-H., Huang C.-J.;
RT "The zebrafish homolog of the human pKU-beta protein kinase.";
RL Submitted (MAY-2000) 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 -!- 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;
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. {ECO:0000255|PROSITE-ProRule:PRU00159}.
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DR EMBL; AF265345; AAK52418.1; -; mRNA.
DR AlphaFoldDB; Q90ZY6; -.
DR SMR; Q90ZY6; -.
DR STRING; 7955.ENSDARP00000006738; -.
DR PaxDb; Q90ZY6; -.
DR PRIDE; Q90ZY6; -.
DR ZFIN; ZDB-GENE-030131-4933; tlk1b.
DR eggNOG; KOG1151; Eukaryota.
DR InParanoid; Q90ZY6; -.
DR PhylomeDB; Q90ZY6; -.
DR PRO; PR:Q90ZY6; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Unplaced.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IBA:GO_Central.
DR GO; GO:0007059; P:chromosome segregation; IBA:GO_Central.
DR GO; GO:0035556; P:intracellular signal transduction; IBA:GO_Central.
DR GO; GO:0018105; P:peptidyl-serine phosphorylation; IBA:GO_Central.
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 Pfam; PF00069; Pkinase; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 2: Evidence at transcript level;
KW ATP-binding; Coiled coil; Kinase; Nucleotide-binding; Nucleus;
KW Reference proteome; Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..756
FT /note="Serine/threonine-protein kinase tousled-like 1-B"
FT /id="PRO_0000273529"
FT DOMAIN 450..728
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 1..56
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 69..185
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 339..375
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 734..756
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 243..268
FT /evidence="ECO:0000255"
FT COILED 397..435
FT /evidence="ECO:0000255"
FT COMPBIAS 1..31
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 38..56
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 70..105
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 106..130
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 157..185
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 344..364
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 734..751
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 580
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 456..464
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 479
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
SQ SEQUENCE 756 AA; 85454 MW; 3F1616718D35BDE2 CRC64;
MSVQSNSNSS GSLDGAPSCS QFSTGSPTPG SVSPLDIFAP RRHKEGMDEL HSLDPRRQEL
LEARFIGAVS GNTGGSTGSA SGGPKGLNNN ECSSHSFGSL GSSSDKESET PEKKHFESSR
GRKRKVDNQS ESSQGKSSGR GPKISDYFDF QGGNGSSPVR GLPSVLRSPQ NSHSAPGAIV
RQNSSSPTSL CFMDHTMNLK QLSSRSVQTD LTLLKLAALE SNKNLDLEKK EGRIDDLLRA
NCDLRRQIDE QQKLLERFKE RLNKCTTMSK KLLIEKSTQE KQSCREKSMQ DRLRLGHFTT
VRHGASYSEQ WTDGYAFQNL VKQQEWINQQ REEIERQRKL LAKRKPSSTP SSQSPTPNES
KQRKTKAVNG ADNDPFLKPS LPTLLTVAEY HEQEEIFKLR LGHLKKEEAE IQAELERLER
VRNLHIRELK RINNEDSSQF KDHPTLNERY LLLHLLGRGG FSEVYKAFDL FEQRYAAVKI
HQLNKNWREE KKENYHKHAC REYRIHKQLD HPRIVKLYDY FSLDTDTFCT VLEFCEGNDL
DFYLKQHKLM SEKEARSIVM QIVNALRYLN EIKPSIIHYD LKPGNILLVD GTACGEIKIT
DFGLSKIMDD DSYGVDGMDL TSQGAGTYWY LPPECFVVGK EPPKISNKVD VWSVGVIFFQ
CLYGRKPFGH NQSQQDILQE NTILKATEVQ FPAKPVASNE AKAFIRRCLA YRKEDRSDVH
QLGSDSYLLP HMRRSNSSGN LQATPASPAP SGIISY
