ID A0A137QS14_9AGAR Unreviewed; 929 AA.
AC A0A137QS14;
DT 11-MAY-2016, integrated into UniProtKB/TrEMBL.
DT 11-MAY-2016, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE SubName: Full=Serine/threonine-protein kinase svkA {ECO:0000313|EMBL:KXN90088.1};
GN ORFNames=AN958_05093 {ECO:0000313|EMBL:KXN90088.1};
OS Leucoagaricus sp. SymC.cos.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Agaricales; Agaricineae; Agaricaceae; Leucoagaricus.
OX NCBI_TaxID=1714833 {ECO:0000313|EMBL:KXN90088.1, ECO:0000313|Proteomes:UP000070249};
RN [1] {ECO:0000313|EMBL:KXN90088.1, ECO:0000313|Proteomes:UP000070249}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SymC.cos {ECO:0000313|EMBL:KXN90088.1,
RC ECO:0000313|Proteomes:UP000070249};
RA Hu H.;
RT "Leucoagaricus sp. SymC.cos WGS genome.";
RL Submitted (JAN-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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DR EMBL; KQ962072; KXN90088.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A137QS14; -.
DR STRING; 1714833.A0A137QS14; -.
DR OrthoDB; 152877at2759; -.
DR Proteomes; UP000070249; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008324; F:monoatomic cation transmembrane transporter activity; IEA:InterPro.
DR GO; GO:0004672; F:protein kinase activity; IEA:InterPro.
DR GO; GO:0098771; P:inorganic ion homeostasis; IEA:UniProt.
DR GO; GO:0030003; P:intracellular monoatomic cation homeostasis; IEA:UniProt.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd06609; STKc_MST3_like; 1.
DR Gene3D; 1.10.12.70; -; 1.
DR Gene3D; 1.20.1510.10; Cation efflux protein transmembrane domain; 1.
DR Gene3D; 3.30.70.1350; Cation efflux protein, cytoplasmic domain; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR002524; Cation_efflux.
DR InterPro; IPR027470; Cation_efflux_CTD.
DR InterPro; IPR036837; Cation_efflux_CTD_sf.
DR InterPro; IPR027469; Cation_efflux_TMD_sf.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR046409; PDC10_dimerisation_sf.
DR InterPro; IPR048288; PDCD10_N.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR NCBIfam; TIGR01297; CDF; 1.
DR PANTHER; PTHR48012:SF10; SERINE_THREONINE-PROTEIN KINASE KIC1; 1.
DR PANTHER; PTHR48012; STERILE20-LIKE KINASE, ISOFORM B-RELATED; 1.
DR Pfam; PF01545; Cation_efflux; 1.
DR Pfam; PF20929; PDCD10_N; 1.
DR Pfam; PF00069; Pkinase; 1.
DR Pfam; PF16916; ZT_dimer; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF160240; Cation efflux protein cytoplasmic domain-like; 1.
DR SUPFAM; SSF161111; Cation efflux protein transmembrane domain-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.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Coiled coil {ECO:0000256|SAM:Coils};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Kinase {ECO:0000313|EMBL:KXN90088.1};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Reference proteome {ECO:0000313|Proteomes:UP000070249};
KW Transferase {ECO:0000313|EMBL:KXN90088.1};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989};
KW Transport {ECO:0000256|ARBA:ARBA00022448}.
FT DOMAIN 408..659
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 721..833
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 434..461
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 736..756
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 757..823
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 437
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 929 AA; 103628 MW; FA2C98CA61C4C3DE CRC64;
MVNSHESTSA STSKSFVTEK VPDAVVPDQA FKLETDIERA SASGSILPSD PYQFRDGIVD
DDTLAQLRSR RQSKRIAKYQ RRQNDLITSL LKPMEEHTEE ALSEEEAARL PVKIAVYGSL
FANFGLCVLQ MYAAISSISL SLLATGIDSV FDIGSNLVLF WLHKKAQKLD VNKWPVGGSR
LETIGNIVYG SLMACVNLVV IVESLRTIVT KQGDILAPFH LPSIVAVAAA LVVKSILFVY
CFSIRRQSSQ VQVLWEDHRN DLWINSFGIL MSCGGSKLRW YLDPMGGVII ASGIIVAWGR
TVYGQFELLA GKSAPHDFLQ LLIYKAATFS EKIVKIDTVR AYHSGPEYFV EIDVVMDAST
PLWKAHDISQ QLQDKIEVLP NVERAFVHVD HETTHTPDAR SQDPEDFYVK QDRIGKGSFG
EVYKGFDKRT QKTVAIKIID LESAEDEIED IQQEIQILSQ LDSPHVTKYH GSFLKGSHLW
IVMEYCSGGS CSDLMKPGVF REEYIAIIVR ELLKGLDYLH TEGKLHRDIK AANILLSAGG
EVKLADFGVS GQLSGTLSAK KNTFVGTPYW MSPEVIKQSG YDHKADIWSL GITAIELAKG
EPPYAELHPM KVLFLIPKNS PPTLEGNFSK PFREFVACCL QRDPRDRPTA RDLLKHKFIR
VAKKTSYLTE LIDRHERWKA EGGERIEEED VHPDVMDING NGEVEDLWDF GTVRHSGRTI
GRSSIKVSGP PLTWENDDLP RRRGSDESDD SVRVRRGHTS VSTASSTTVK GDLPPLPTST
PSSPSKQRFE QDTVRHASVQ SIPNNRNQPI ATDYAVPQGN HRSAQREPSD DYEDYDDQYV
DTHLAKTGAV HQKMADMHLE EDLPDTTMLD SVVLPAIASL FPRVSSQEAR IALSALQRAF
TEAERIIPGV TLELVNEIVD SVEHVEDIP
//
