ID   A0A1G4J1V2_9SACH        Unreviewed;       714 AA.
AC   A0A1G4J1V2;
DT   18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT   18-JAN-2017, sequence version 1.
DT   27-MAR-2024, entry version 29.
DE   SubName: Full=LAMI_0C03378g1_1 {ECO:0000313|EMBL:SCU83479.1};
GN   ORFNames=LAMI_0C03378G {ECO:0000313|EMBL:SCU83479.1};
OS   Lachancea mirantina.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Lachancea.
OX   NCBI_TaxID=1230905 {ECO:0000313|EMBL:SCU83479.1, ECO:0000313|Proteomes:UP000191024};
RN   [1] {ECO:0000313|Proteomes:UP000191024}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Devillers H.;
RL   Submitted (MAR-2016) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; LT598466; SCU83479.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1G4J1V2; -.
DR   STRING; 1230905.A0A1G4J1V2; -.
DR   OrthoDB; 10768at2759; -.
DR   Proteomes; UP000191024; Chromosome c.
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; 2.60.40.150; C2 domain; 1.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR   InterPro; IPR000961; AGC-kinase_C.
DR   InterPro; IPR000008; C2_dom.
DR   InterPro; IPR035892; C2_domain_sf.
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:SF245; AGC_AKT PROTEIN KINASE SCK2; 1.
DR   PANTHER; PTHR24351; RIBOSOMAL PROTEIN S6 KINASE; 1.
DR   Pfam; PF00168; C2; 1.
DR   Pfam; PF00069; Pkinase; 1.
DR   Pfam; PF00433; Pkinase_C; 1.
DR   SMART; SM00239; C2; 1.
DR   SMART; SM00133; S_TK_X; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF49562; C2 domain (Calcium/lipid-binding domain, CaLB); 1.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   PROSITE; PS51285; AGC_KINASE_CTER; 1.
DR   PROSITE; PS50004; C2; 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          111..271
FT                   /note="C2"
FT                   /evidence="ECO:0000259|PROSITE:PS50004"
FT   DOMAIN          305..564
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   DOMAIN          565..639
FT                   /note="AGC-kinase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51285"
FT   REGION          73..128
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          193..222
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        93..128
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         344
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ   SEQUENCE   714 AA;  79280 MW;  271A2A41CD5D042A CRC64;
     MNFFGKIPSE RSAGTERQLL ESPLLPRPAS HTATPTTALS HSSYAIGTTA LNAGSGDAAF
     QIKSVHDSAV GPQGGVASGA ASSAARTPLR ASPGPSVQGQ SQTAAARAQL HPQDTPVSNT
     TNSETGVPRG ALEVTIVAAR DLLTRSPHAR PYVVCTFESS EFISDGPENN SVGQSGGALP
     SIRENQLQTT PLYTRQSSSQ LDKLASTASE DPDHNSSNPT WHHKATFDVL GARSELDISV
     YDAAHDDMFL GQVRLRPHTH VPHRAKQNQW HKLQSRIIGE RATGDILVEW SYTSTEKRHY
     GPHDFEVLRL LGKGTFGQVY QVRKKDTKRI YAMKVLSKKV IVKKNEIAHT IGERNILVRT
     ASKSCPFIVG LKFSFQTPAD LYLVTDFMSG GELFWHLQKE GRFAEDRAKF YIAELVLALE
     YLHDNDIVYR DLKPENILLD ANGNVALCDF GLSKADLKDR TNTFCGTTEY LAPELLLDES
     GYTKMVDFWS LGVLIFEMCC GWSPFFAEDN QKMYQKIAFG KVKFPRDVLS PDGRSFVKGL
     LNRNPKHRLG ALDDGRELRA HPFFADIDWE ALRQKKTPPP FKPHLSSETD TSNFDPEFTQ
     TSTSYMNKQP IAATPLSPAM QAKFAGFTFV DESAFDDHYN AHYSNRKFLQ SSYFMEPGSF
     IPGNPNLPPD EDVIDDEDYD LDQAQLKNGN TNAQVDYDGD HHMDDEFVSG RFEI
//