ID A0A1J0KIM5_TUPBE Unreviewed; 288 AA. AC A0A1J0KIM5; DT 15-FEB-2017, integrated into UniProtKB/TrEMBL. DT 15-FEB-2017, sequence version 1. DT 29-MAY-2024, entry version 16. DE RecName: Full=non-specific serine/threonine protein kinase {ECO:0000256|ARBA:ARBA00012513}; DE EC=2.7.11.1 {ECO:0000256|ARBA:ARBA00012513}; OS Tupaia belangeri (Common tree shrew) (Tupaia glis belangeri). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Scandentia; Tupaiidae; Tupaia. OX NCBI_TaxID=37347 {ECO:0000313|EMBL:APC93947.1}; RN [1] {ECO:0000313|EMBL:APC93947.1} RP NUCLEOTIDE SEQUENCE. RA Evans L.H., Alamgir A., Owens N., Weber N.D., Virtaneva K., Barbian K., RA Babar A., Rosenke K.; RL Submitted (APR-2016) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:APC93947.1} RP NUCLEOTIDE SEQUENCE. RA Yang M.H., Li Y.H.; RT "Cloning and bioinformatics analysis of tree shrews Tssk gene families' RT cDNA."; RL Submitted (NOV-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 --------------------------------------------------------------------------- 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; KX091163; APC93947.1; -; mRNA. DR AlphaFoldDB; A0A1J0KIM5; -. DR SMR; A0A1J0KIM5; -. DR GO; GO:0005737; C:cytoplasm; IEA:TreeGrafter. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule. DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:TreeGrafter. DR GO; GO:0035556; P:intracellular signal transduction; IEA:TreeGrafter. DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW. DR GO; GO:0007283; P:spermatogenesis; IEA:UniProtKB-KW. DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1. DR InterPro; IPR011009; Kinase-like_dom_sf. DR InterPro; IPR000719; Prot_kinase_dom. DR InterPro; IPR017441; Protein_kinase_ATP_BS. DR PANTHER; PTHR24346; MAP/MICROTUBULE AFFINITY-REGULATING KINASE; 1. DR PANTHER; PTHR24346:SF100; TESTIS-SPECIFIC SERINE_THREONINE-PROTEIN KINASE 1; 1. DR Pfam; PF00069; Pkinase; 1. DR SMART; SM00220; S_TKc; 1. DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1. DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1. DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1. PE 2: Evidence at transcript level; KW ATP-binding {ECO:0000256|PROSITE-ProRule:PRU10141}; KW Differentiation {ECO:0000256|ARBA:ARBA00022871}; KW Kinase {ECO:0000313|EMBL:APC93947.1}; KW Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU10141}; KW Spermatogenesis {ECO:0000256|ARBA:ARBA00022871}; KW Transferase {ECO:0000313|EMBL:APC93947.1}. FT DOMAIN 10..285 FT /note="Protein kinase" FT /evidence="ECO:0000259|PROSITE:PS50011" FT BINDING 39 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141" SQ SEQUENCE 288 AA; 32215 MW; D0A66B4BBF87B14F CRC64; MEDFLLSNGY QLGKTIGEGT YSKVKEAFSK KHQRKVAIKI IDKMGGPEGQ RLAARTQPGL AEGRSWFQEF IQRFLPRELQ IVRTLDHKNI IRVHELLESA DGKIFLVMEL AEGGDVFDCV LNGGPLPESQ AKALFRQMVE AIRYCHGCGV AHRDLKCENA LLQGFNLKLT DFGFAKVLPK SRCELSQTFC GSTAYAAPEV LRGIPHDSKK GDVWSMGVVL YVMLCASLPF DDTDIPKMLW QQQKGVSFPT SLGISAECQD LLKQLLEPDM TLRPSIEEVS WHPWLAST //