ID A0A2P7YK09_9ASCO Unreviewed; 613 AA. AC A0A2P7YK09; DT 23-MAY-2018, integrated into UniProtKB/TrEMBL. DT 23-MAY-2018, sequence version 1. DT 03-MAY-2023, entry version 21. DE RecName: Full=non-specific serine/threonine protein kinase {ECO:0000256|ARBA:ARBA00012513}; DE EC=2.7.11.1 {ECO:0000256|ARBA:ARBA00012513}; GN ORFNames=C7M61_004116 {ECO:0000313|EMBL:PSK36292.1}; OS [Candida] pseudohaemulonii. OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes; OC Saccharomycetales; Metschnikowiaceae; Metschnikowiaceae incertae sedis; OC Candida/Metschnikowiaceae. OX NCBI_TaxID=418784 {ECO:0000313|EMBL:PSK36292.1, ECO:0000313|Proteomes:UP000241107}; RN [1] {ECO:0000313|EMBL:PSK36292.1, ECO:0000313|Proteomes:UP000241107} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=B12108 {ECO:0000313|EMBL:PSK36292.1, RC ECO:0000313|Proteomes:UP000241107}; RA Munoz J.F., Gade L.G., Chow N.A., Litvintseva A.P., Loparev V.N., RA Cuomo C.A.; RT "Candida pseudohaemulonii genome assembly and annotation."; RL Submitted (MAR-2018) 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 -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ CC whole genome shotgun (WGS) entry which is preliminary data. CC {ECO:0000313|EMBL:PSK36292.1}. 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; PYFQ01000012; PSK36292.1; -; Genomic_DNA. DR AlphaFoldDB; A0A2P7YK09; -. DR STRING; 418784.A0A2P7YK09; -. DR EnsemblFungi; C7M61_004116_t1; PSK36292.1; C7M61_004116. DR VEuPathDB; FungiDB:C7M61_004116; -. DR OrthoDB; 5475340at2759; -. DR Proteomes; UP000241107; Unassembled WGS sequence. DR GO; GO:0000144; C:cellular bud neck septin ring; IEA:EnsemblFungi. DR GO; GO:0005641; C:nuclear envelope lumen; IEA:EnsemblFungi. DR GO; GO:0031588; C:nucleotide-activated protein kinase complex; IEA:EnsemblFungi. DR GO; GO:0005774; C:vacuolar membrane; IEA:EnsemblFungi. DR GO; GO:0004679; F:AMP-activated protein kinase activity; IEA:EnsemblFungi. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule. DR GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; IEA:EnsemblFungi. DR GO; GO:0042802; F:identical protein binding; IEA:EnsemblFungi. DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA. DR GO; GO:0061762; P:CAMKK-AMPK signaling cascade; IEA:EnsemblFungi. DR GO; GO:0000132; P:establishment of mitotic spindle orientation; IEA:EnsemblFungi. DR GO; GO:0071940; P:fungal-type cell wall assembly; IEA:EnsemblFungi. DR GO; GO:0001403; P:invasive growth in response to glucose limitation; IEA:EnsemblFungi. DR GO; GO:1904262; P:negative regulation of TORC1 signaling; IEA:EnsemblFungi. DR GO; GO:0017148; P:negative regulation of translation; IEA:EnsemblFungi. DR GO; GO:0075319; P:positive regulation of ascus development; IEA:EnsemblFungi. DR GO; GO:1900436; P:positive regulation of filamentous growth of a population of unicellular organisms in response to starvation; IEA:EnsemblFungi. DR GO; GO:0045722; P:positive regulation of gluconeogenesis; IEA:EnsemblFungi. DR GO; GO:0016239; P:positive regulation of macroautophagy; IEA:EnsemblFungi. DR GO; GO:2000222; P:positive regulation of pseudohyphal growth; IEA:EnsemblFungi. DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IEA:EnsemblFungi. DR GO; GO:0006468; P:protein phosphorylation; IEA:InterPro. DR GO; GO:2000217; P:regulation of invasive growth in response to glucose limitation; IEA:EnsemblFungi. DR GO; GO:0034976; P:response to endoplasmic reticulum stress; IEA:EnsemblFungi. DR GO; GO:0006986; P:response to unfolded protein; IEA:EnsemblFungi. DR GO; GO:0090606; P:single-species surface biofilm formation; IEA:EnsemblFungi. DR GO; GO:0032933; P:SREBP signaling pathway; IEA:EnsemblFungi. DR CDD; cd12122; AMPKA_C; 1. DR CDD; cd14079; STKc_AMPK_alpha; 1. DR CDD; cd14334; UBA_SNF1_fungi; 1. DR Gene3D; 1.10.8.10; DNA helicase RuvA subunit, C-terminal domain; 1. DR Gene3D; 3.30.310.80; Kinase associated domain 1, KA1; 1. DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1. DR InterPro; IPR032270; AMPK_C. DR InterPro; IPR028375; KA1/Ssp2_C. 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; IPR013896; SNF1_UBA. DR PANTHER; PTHR24346; MAP/MICROTUBULE AFFINITY-REGULATING KINASE; 1. DR PANTHER; PTHR24346:SF82; NON-SPECIFIC SERINE/THREONINE PROTEIN KINASE; 1. DR Pfam; PF16579; AdenylateSensor; 1. DR Pfam; PF00069; Pkinase; 1. DR Pfam; PF08587; UBA_2; 1. DR SMART; SM00220; S_TKc; 1. DR SUPFAM; SSF103243; KA1-like; 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 4: Predicted; KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE- KW ProRule:PRU10141}; Kinase {ECO:0000313|EMBL:PSK36292.1}; KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE- KW ProRule:PRU10141}; Reference proteome {ECO:0000313|Proteomes:UP000241107}; KW Transferase {ECO:0000313|EMBL:PSK36292.1}. FT DOMAIN 51..302 FT /note="Protein kinase" FT /evidence="ECO:0000259|PROSITE:PS50011" FT REGION 1..45 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 389..413 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 9..24 FT /note="Basic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 28..45 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 390..409 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT BINDING 80 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141" SQ SEQUENCE 613 AA; 69549 MW; 80CDE3126589B7A8 CRC64; MSEEGKLSGH HRHHHHHSHH GHHGHDLKQQ QQQQFPPQGT APSSANRIGK YQIIKTLGEG SFGKVKLAEH STTGQRVALK IINRKTLAKS DMQGRVEREI SYLRLLRHPH IIKLYDVIKS KDEIIMVIEY AGKELFDYIV QRGRMPEDEA RRFFQQIIAA VEYCHRHKIV HRDLKPENLL LDDHLNVKIA DFGLSNIMTD GNFLKTSCGS PNYAAPEVIS GKLYAGPEVD VWSSGVILYV MLCGRLPFDD EFIPALFKKI SNGVYTLPNY LSEGAKKILT KMLVVNPLNR VTIHEIMEDP WFKEGIEDYL LPPDLSKTIH NKIDIDEDVI NALSVTMGYD RDEILNTINS CNKQQYPQQQ QNEILDAYLL MKENHSLVKD LKKNKTEHMD NFLSSSPPPS WSSPQGEEAT ATHRAPGVLQ SLTYQTLATV PDLSTLPNST IAILPSSLPS IHRASMMNVS EQGSSKINPV SSKKLKTKWH FGIRSRSYPL DVMGEIYRAL KNLGAEWAKP TEEELWTIRV RWKYGPCLVD ETVKEGESVP PALMKMQIQL FQLEPNNYLV DFKFDGWEST TTQDGKPAGK QDVDEMSSFS AYPFLHLATR LIMELAVNST QAQ //