ID A0A1B9IG23_9TREE Unreviewed; 353 AA. AC A0A1B9IG23; DT 02-NOV-2016, integrated into UniProtKB/TrEMBL. DT 02-NOV-2016, sequence version 1. DT 27-NOV-2024, entry version 20. DE RecName: Full=Casein kinase II subunit alpha {ECO:0000256|RuleBase:RU369118}; DE Short=CK II alpha {ECO:0000256|RuleBase:RU369118}; DE EC=2.7.11.1 {ECO:0000256|RuleBase:RU369118}; GN ORFNames=L486_08052 {ECO:0000313|EMBL:OCF54503.1}; OS Kwoniella mangroviensis CBS 10435. OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Tremellomycetes; OC Tremellales; Cryptococcaceae; Kwoniella. OX NCBI_TaxID=1331196 {ECO:0000313|EMBL:OCF54503.1, ECO:0000313|Proteomes:UP000092583}; RN [1] {ECO:0000313|EMBL:OCF54503.1, ECO:0000313|Proteomes:UP000092583} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CBS 10435 {ECO:0000313|EMBL:OCF54503.1, RC ECO:0000313|Proteomes:UP000092583}; RG The Broad Institute Genome Sequencing Platform; RA Cuomo C., Litvintseva A., Chen Y., Heitman J., Sun S., Springer D., RA Dromer F., Young S.K., Zeng Q., Gargeya S., Fitzgerald M., Abouelleil A., RA Alvarado L., Berlin A.M., Chapman S.B., Dewar J., Goldberg J., Griggs A., RA Gujja S., Hansen M., Howarth C., Imamovic A., Larimer J., McCowan C., RA Murphy C., Pearson M., Priest M., Roberts A., Saif S., Shea T., Sykes S., RA Wortman J., Nusbaum C., Birren B.; RT "The Genome Sequence of Kwoniella mangroviensis CBS10435."; RL Submitted (JUL-2013) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|Proteomes:UP000092583} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CBS 10435 {ECO:0000313|Proteomes:UP000092583}; RA Cuomo C., Litvintseva A., Heitman J., Chen Y., Sun S., Springer D., RA Dromer F., Young S., Zeng Q., Chapman S., Gujja S., Saif S., Birren B.; RT "Evolution of pathogenesis and genome organization in the Tremellales."; RL Submitted (DEC-2013) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Catalytic subunit of a constitutively active CC serine/threonine-protein kinase complex that phosphorylates a large CC number of substrates containing acidic residues C-terminal to the CC phosphorylated serine or threonine. {ECO:0000256|RuleBase:RU369118}. 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|RuleBase:RU369118}; 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|RuleBase:RU369118}; CC -!- SUBUNIT: Heterotetramer. {ECO:0000256|RuleBase:RU369118}. CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|RuleBase:RU369118}. CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein CC kinase family. CK2 subfamily. {ECO:0000256|RuleBase:RU369118}. 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; KI669470; OCF54503.1; -; Genomic_DNA. DR AlphaFoldDB; A0A1B9IG23; -. DR STRING; 1331196.A0A1B9IG23; -. DR Proteomes; UP000092583; Unassembled WGS sequence. DR GO; GO:0005829; C:cytosol; IEA:TreeGrafter. DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell. DR GO; GO:0005956; C:protein kinase CK2 complex; IEA:TreeGrafter. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule. DR GO; GO:0106310; F:protein serine kinase activity; IEA:UniProtKB-UniRule. DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-UniRule. DR GO; GO:0006974; P:DNA damage response; IEA:TreeGrafter. DR GO; GO:0018105; P:peptidyl-serine phosphorylation; IEA:TreeGrafter. DR GO; GO:0018107; P:peptidyl-threonine phosphorylation; IEA:TreeGrafter. DR GO; GO:0051726; P:regulation of cell cycle; IEA:TreeGrafter. DR GO; GO:0006356; P:regulation of transcription by RNA polymerase I; IEA:TreeGrafter. DR GO; GO:0006359; P:regulation of transcription by RNA polymerase III; IEA:TreeGrafter. DR CDD; cd14132; STKc_CK2_alpha; 1. DR FunFam; 1.10.510.10:FF:000059; Casein kinase II subunit alpha; 1. DR FunFam; 3.30.200.20:FF:000088; Casein kinase II subunit alpha; 1. DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1. DR InterPro; IPR045216; CK2_alpha. 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; PTHR24054; CASEIN KINASE II SUBUNIT ALPHA; 1. DR PANTHER; PTHR24054:SF0; CASEIN KINASE II SUBUNIT ALPHA; 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|RuleBase:RU369118, ECO:0000313|EMBL:OCF54503.1}; KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE- KW ProRule:PRU10141}; Nucleus {ECO:0000256|RuleBase:RU369118}; KW Reference proteome {ECO:0000313|Proteomes:UP000092583}; KW Serine/threonine-protein kinase {ECO:0000256|RuleBase:RU000304}; KW Transferase {ECO:0000256|RuleBase:RU369118}. FT DOMAIN 38..323 FT /note="Protein kinase" FT /evidence="ECO:0000259|PROSITE:PS50011" FT BINDING 67 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141" SQ SEQUENCE 353 AA; 41595 MW; CAC78ACC2AEBEBC1 CRC64; MAAGRSVARV YANVNDKLGR SWWDYDNLVV QWGIQDNYEI VRKVGRGKYS EVFESIHLPS NSKCIVKVLK PVKKKKIKRE IKILQNLAGG PNVVGLLDVV RDNQSKTPSI VTEYVNNVEF KTLYPKFTDF DVRFYMFELL KALDFCHSKG IMHRDVKPHN VMIDHEKRTL RLIDWGLAEF YHPGTEYNVR VASRYFKGPE LLVDFQEYDY SLDMWSLGCM FASMIFRKEP FFHGHDNADQ LVKITKVLGT DELFIYLERY EIDLDSQFDD ILGRYPRKPW SRFITSENQR YISNEAIDFL DKLLRYDHQE RLTAQESQEH PYFGELYHYS HTKRSADMEV DCVAPVREAA IRQ //