ID A0A1G4K8N7_9SACH Unreviewed; 683 AA.
AC A0A1G4K8N7;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE SubName: Full=LAMI_0G04962g1_1 {ECO:0000313|EMBL:SCV00427.1};
GN ORFNames=LAMI_0G04962G {ECO:0000313|EMBL:SCV00427.1};
OS Lachancea mirantina.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Lachancea.
OX NCBI_TaxID=1230905 {ECO:0000313|EMBL:SCV00427.1, ECO:0000313|Proteomes:UP000191024};
RN [1] {ECO:0000313|EMBL:SCV00427.1, ECO:0000313|Proteomes:UP000191024}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 11717 {ECO:0000313|EMBL:SCV00427.1};
RA Devillers H.;
RL Submitted (MAR-2016) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; LT598469; SCV00427.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G4K8N7; -.
DR STRING; 1230905.A0A1G4K8N7; -.
DR OrthoDB; 10768at2759; -.
DR Proteomes; UP000191024; Chromosome g.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd11651; YPK1_N_like; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR000961; AGC-kinase_C.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR017892; Pkinase_C.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR PANTHER; PTHR24351; RIBOSOMAL PROTEIN S6 KINASE; 1.
DR PANTHER; PTHR24351:SF243; RIBOSOMAL PROTEIN S6 KINASE; 1.
DR Pfam; PF00069; Pkinase; 1.
DR Pfam; PF00433; Pkinase_C; 1.
DR SMART; SM00133; S_TK_X; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS51285; AGC_KINASE_CTER; 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:0000256|ARBA:ARBA00022777};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000191024};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 350..605
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 606..676
FT /note="AGC-kinase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51285"
FT REGION 1..65
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 81..113
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 9..40
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 383
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 683 AA; 76883 MW; 40C4260980D91EFF CRC64;
MYSWKLSKFK FGRSKEPKDT DKDREREKEQ KEKEKHGAFG LKGTQKIQTQ YAESPRKSLD
RKETIVASPS SIAPVRLSTE IHKSTTNSSA STFKESGTDI EPSEEQASNT SSISTRTRAV
KLSGIMTIKV YGGDDFRLPF PITSNGQILT KLLSSGVTNK AANDVNLEEL VSSLSQIGLS
DSQDDDNLID GDVATHYIPS TITLPGSPDL NPLLYFTIEF DNTVATIEPE SGTICKPTLN
KISTFDVTRK LPFLKIEAFA RIPSILLPSK TWQQLHSSDP QLAILLDKIN SNQDIQLGSC
SLPLKLDFDS ATSFRLYNHQ WIEFDHDCGK LNVTVDFKPA TNRALTIDDF DLLKVIGKGS
FGKVMQVRKK DTSKVYALKA IRKSYIVSKS EVTHTLAERT VLARVENPFI VPLKFSFQSP
DKLYLVLAFI NGGELFYHLQ REGRFNLSRA RFYAAELLCA LETLHSLNVI YRDLKPENIL
LDYQGHIALC DFGLCKLDMK GQDKTNTFCG TPEYLAPELL LGQGYSKVVD WWTLGVLLYE
MLTGLPPYYD ENVPKMYKKI LQEPLRFPDG FDNDAKDLLI GLLSRDPKRR LGYRGADVIK
SHAFFSQLSW KRLWVKGYIP PYKPPVLNSL DTSNFDQEFT RELPVDSVVN DFLTESVQQQ
FGGWTYVGSE QLGSSMAPGR SIK
//