ID D8TP98_VOLCA Unreviewed; 408 AA. AC D8TP98; DT 05-OCT-2010, integrated into UniProtKB/TrEMBL. DT 05-OCT-2010, sequence version 1. DT 02-SEP-2026, entry version 60. DE RecName: Full=Serine/threonine-protein {ECO:0000256|PROSITE-ProRule:PRU10027}; DE EC=2.7.11.1 {ECO:0000256|PROSITE-ProRule:PRU10027}; GN Name=gsk3 {ECO:0000313|EMBL:EFJ50723.1}; GN ORFNames=VOLCADRAFT_80100 {ECO:0000313|EMBL:EFJ50723.1}; OS Volvox carteri f. nagariensis. OC Eukaryota; Viridiplantae; Chlorophyta; core chlorophytes; Chlorophyceae; OC CS clade; Chlamydomonadales; Volvocaceae; Volvox. OX NCBI_TaxID=3068 {ECO:0000313|Proteomes:UP000001058}; RN [1] {ECO:0000313|EMBL:EFJ50723.1, ECO:0000313|Proteomes:UP000001058} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=f. Nagariensis / Eve {ECO:0000313|Proteomes:UP000001058}; RX PubMed=20616280; DOI=10.1126/science.1188800; RA Prochnik S.E., Umen J., Nedelcu A.M., Hallmann A., Miller S.M., Nishii I., RA Ferris P., Kuo A., Mitros T., Fritz-Laylin L.K., Hellsten U., Chapman J., RA Simakov O., Rensing S.A., Terry A., Pangilinan J., Kapitonov V., Jurka J., RA Salamov A., Shapiro H., Schmutz J., Grimwood J., Lindquist E., Lucas S., RA Grigoriev I.V., Schmitt R., Kirk D., Rokhsar D.S.; RT "Genomic analysis of organismal complexity in the multicellular green alga RT Volvox carteri."; RL Science 329:223-226(2010). CC -!- CATALYTIC ACTIVITY: CC Reaction=L-seryl-[protein] + ATP = O-phospho-L-seryl-[protein] + ADP + CC H(+); 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|PROSITE-ProRule:PRU10027}; CC -!- CATALYTIC ACTIVITY: CC Reaction=L-threonyl-[protein] + ATP = O-phospho-L-threonyl-[protein] + CC ADP + H(+); Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060, Rhea:RHEA- CC COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616, CC ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; EC=2.7.11.1; CC Evidence={ECO:0000256|PROSITE-ProRule:PRU10027}; CC -!- SIMILARITY: Belongs to the protein kinase superfamily. CMGC Ser/Thr CC protein kinase family. GSK-3 subfamily. CC {ECO:0000256|ARBA:ARBA00005527}. CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein CC kinase family. {ECO:0000256|PROSITE-ProRule:PRU00159}. 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; GL378330; EFJ50723.1; -; Genomic_DNA. DR RefSeq; XP_002948316.1; XM_002948270.1. DR AlphaFoldDB; D8TP98; -. DR FunCoup; D8TP98; 1853. DR STRING; 3068.D8TP98; -. DR GeneID; 9623945; -. DR KEGG; vcn:VOLCADRAFT_80100; -. DR eggNOG; KOG0658; Eukaryota. DR InParanoid; D8TP98; -. DR OrthoDB; 272141at2759; -. DR Proteomes; UP000001058; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:TreeGrafter. DR GO; GO:0005634; C:nucleus; 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:0030154; P:cell differentiation; IEA:TreeGrafter. DR GO; GO:0007165; P:signal transduction; IEA:TreeGrafter. DR CDD; cd14137; STKc_GSK3; 1. DR FunFam; 3.30.200.20:FF:000009; Glycogen synthase kinase-3 beta; 1. DR FunFam; 1.10.510.10:FF:000082; Shaggy-related protein kinase kappa; 1. DR Gene3D; 3.30.200.20; Phosphorylase Kinase, domain 1; 1. DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1. DR InterPro; IPR050591; GSK-3. 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 InterPro; IPR039192; STKc_GSK3. DR PANTHER; PTHR24057; GLYCOGEN SYNTHASE KINASE-3 ALPHA; 1. DR PANTHER; PTHR24057:SF0; PROTEIN KINASE SHAGGY-RELATED; 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. 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}; KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|PROSITE- KW ProRule:PRU00159}; KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE- KW ProRule:PRU10141}; Reference proteome {ECO:0000313|Proteomes:UP000001058}; KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527, KW ECO:0000256|PROSITE-ProRule:PRU00159}; KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PROSITE- KW ProRule:PRU00159}. FT DOMAIN 80..363 FT /note="Protein kinase" FT /evidence="ECO:0000259|PROSITE:PS50011" FT REGION 1..44 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1..24 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 34..44 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT ACT_SITE 204 FT /note="Proton acceptor" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10027" FT BINDING 110 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141" SQ SEQUENCE 408 AA; 45713 MW; 8E3E2CD6CFCC5B85 CRC64; MSASVGNAAQ QPSVSGNDLQ QSMKELTIKD EEAGSSNKPL QNPATAEIFE GRLIEGDLKS GGHVLSASAG TGASRQTYNY STDRVVGNGS FGVVFQATCL ETGETVAIKK VLQDKRFKNR ELQIMKLVDH PNIVKLKHCF YSHTDKDETY LHLVLEFVPD TVYRISKHYA KNNQRMPNLF VKLYAYQMCR ALNSIHKMGI CHRDIKPQNL LVNTETHQLK LCDFGSAKVL IKGEPNISYI CSRYYRAPEL IFGATDYTSG IDVWSVGCVL AELLLGQPLF PGESGVDQLV EIIKVLGTPT REEINSMNPN YTEFKFPQIK AHPWTKVFSK RMPPDAVDLV SKLLQYAPQK RMTAIQAMTH PFFDELRDPN TRLPNGRSLP PLFNWLPGEL DEVPADIVRK LQPAVKTT //