ID A0A1G4IQ64_9SACH Unreviewed; 753 AA.
AC A0A1G4IQ64;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE SubName: Full=LADA_0A08460g1_1 {ECO:0000313|EMBL:SCU78904.1};
GN ORFNames=LADA_0A08460G {ECO:0000313|EMBL:SCU78904.1};
OS Lachancea dasiensis.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Lachancea.
OX NCBI_TaxID=1072105 {ECO:0000313|EMBL:SCU78904.1, ECO:0000313|Proteomes:UP000190274};
RN [1] {ECO:0000313|EMBL:SCU78904.1, ECO:0000313|Proteomes:UP000190274}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 10888 {ECO:0000313|EMBL:SCU78904.1};
RA Devillers H.;
RL Submitted (MAR-2016) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; LT598460; SCU78904.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G4IQ64; -.
DR STRING; 1266660.A0A1G4IQ64; -.
DR OrthoDB; 10768at2759; -.
DR Proteomes; UP000190274; Chromosome A.
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; 2.
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:UP000190274};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 143..309
FT /note="C2"
FT /evidence="ECO:0000259|PROSITE:PS50004"
FT DOMAIN 343..602
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 603..677
FT /note="AGC-kinase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51285"
FT REGION 1..33
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 98..117
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 125..161
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 697..742
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 125..151
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 719..742
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 382
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 753 AA; 84407 MW; 561791BCF3F2C9E2 CRC64;
MINFFGTKSV ESQAQNNDQG RLDGTKPPPL QLQQQNMQSN GLFPSFTAQT ATPTTALCDN
SYAMGTTGLA SNQPETALTQ MKSMSSQSEL HLQAMKFPDQ QQQDIPSLRP ASANGNVKTF
PQLSQQANQH VPSAGSSNGS TTEQRDAISS LDSDPAETGI PRGRLEVTIA EAQGLLTRSS
QSQPYVVCTF ESSEFISEGP ESVDNKPVTH NTISGWTNEL PAIAEKHKKP LYTRQSSSQL
DKLNSQSVAT NNNCSNPIWH HETTFDVLGA HSELDISVYD AAHDDMFLGQ VRLRPDLHTS
SLSKHEQWYK LQSRIVGESV AGLIRVKWHF KSTKKRQYGP QDFEVLRLLG KGTFGQVYQV
RKKDTKRIYA MKVLSKKVIV KKNEIAHTIG ERNILVRTAS KSCPFIVGLK FSFQTLADLY
LVTDFMSGGE LFWHLQKEGR FTEDRAKFYI AELVLALEYL HENDIVYRDL KPENILLDAN
GNIALCDFGL SKADLKDRTN TFCGTTEYLA PELLLDESGY TKMVDFWSLG VLIFEMCCGW
SPFFAEDNQK MYQKIAFGKV KFPRDVLSPE GRSFVKGLLN RNPRHRLGAL DDGRELRAHP
FFADIDWEAL RLKKIPPPFK PHLSGETDTS NFDPEFTQTS TSYMNRQTMA ATPLSPAMQA
KFAGFTFVDE STMDELHNNN YNNRKFLQNS YFMEPGSFIP GNPELPADED VIDDDAGQDT
ELGDGKPAGS HEQVDFDGDH HMDDEFVSGR FEI
//
