ID A0A1D2VJF7_9ASCO Unreviewed; 843 AA.
AC A0A1D2VJF7;
DT 30-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 30-NOV-2016, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE SubName: Full=Pkinase-domain-containing protein {ECO:0000313|EMBL:ODV61745.1};
GN ORFNames=ASCRUDRAFT_7236 {ECO:0000313|EMBL:ODV61745.1};
OS Ascoidea rubescens DSM 1968.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Ascoideaceae; Ascoidea.
OX NCBI_TaxID=1344418 {ECO:0000313|EMBL:ODV61745.1, ECO:0000313|Proteomes:UP000095038};
RN [1] {ECO:0000313|Proteomes:UP000095038}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 1968 {ECO:0000313|Proteomes:UP000095038};
RG DOE Joint Genome Institute;
RA Riley R., Haridas S., Wolfe K.H., Lopes M.R., Hittinger C.T., Goker M.,
RA Salamov A., Wisecaver J., Long T.M., Aerts A.L., Barry K., Choi C.,
RA Clum A., Coughlan A.Y., Deshpande S., Douglass A.P., Hanson S.J.,
RA Klenk H.-P., Labutti K., Lapidus A., Lindquist E., Lipzen A.,
RA Meier-Kolthoff J.P., Ohm R.A., Otillar R.P., Pangilinan J., Peng Y.,
RA Rokas A., Rosa C.A., Scheuner C., Sibirny A.A., Slot J.C., Stielow J.B.,
RA Sun H., Kurtzman C.P., Blackwell M., Grigoriev I.V., Jeffries T.W.;
RT "Comparative genomics of biotechnologically important yeasts.";
RL Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. STE Ser/Thr
CC protein kinase family. MAP kinase kinase kinase subfamily.
CC {ECO:0000256|ARBA:ARBA00006529}.
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DR EMBL; KV454478; ODV61745.1; -; Genomic_DNA.
DR RefSeq; XP_020048052.1; XM_020192062.1.
DR AlphaFoldDB; A0A1D2VJF7; -.
DR STRING; 1344418.A0A1D2VJF7; -.
DR GeneID; 30965698; -.
DR InParanoid; A0A1D2VJF7; -.
DR OrthoDB; 145974at2759; -.
DR Proteomes; UP000095038; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004672; F:protein kinase activity; IEA:InterPro.
DR GO; GO:0000165; P:MAPK cascade; IEA:UniProt.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR Gene3D; 1.10.150.50; Transcription Factor, Ets-1; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR029458; Ras-bd_By2.
DR InterPro; IPR001660; SAM.
DR InterPro; IPR013761; SAM/pointed_sf.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR PANTHER; PTHR48016; MAP KINASE KINASE KINASE SSK2-RELATED-RELATED; 1.
DR PANTHER; PTHR48016:SF29; MITOGEN-ACTIVATED PROTEIN KINASE KINASE KINASE 1A; 1.
DR Pfam; PF00069; Pkinase; 1.
DR Pfam; PF14847; Ras_bdg_2; 1.
DR Pfam; PF07647; SAM_2; 1.
DR SMART; SM01304; Ras_bdg_2; 1.
DR SMART; SM00220; S_TKc; 1.
DR SMART; SM00454; SAM; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR SUPFAM; SSF47769; SAM/Pointed domain; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
DR PROSITE; PS50105; SAM_DOMAIN; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Kinase {ECO:0000313|EMBL:ODV61745.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Reference proteome {ECO:0000313|Proteomes:UP000095038};
KW Transferase {ECO:0000313|EMBL:ODV61745.1}.
FT DOMAIN 32..92
FT /note="SAM"
FT /evidence="ECO:0000259|PROSITE:PS50105"
FT DOMAIN 575..835
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 124..168
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 454..512
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 604
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 843 AA; 95263 MW; B519620E7DC1C33E CRC64;
MVAISPLIDH VSSSHSSHNN RSPNSDILKN FDIKTWLDEI NCKQYYRLFK ENDIKSLDLI
LNLDYTLLKE LGINKVGDLI IFENSIELLK VRKLNNNLNK DSQLISLFID QFLNSQSDIL
NKNDTDTNHF DHSHNPKNNS NKINNKSILK KKKTESPTTD TIKSNDSDET LKIDPPIFIP
IATKNKSSAS SPVDNKSTVN NKEVTFILID GSTDKIYVDG CYNVDTIKNR LLKHLNIKDL
AENYNTYYTI DNTKNLHLIH DIELMAICHS QTREEKNRII FIKSNQKPSQ KAINKSVEIA
SQSSSNNKNH YISKNKNKTN QKVLPNIIID ETINPDNFKT VYGQRPPSEL ISTNLAEYFP
DADSTQLRET IRNSVRLSRA CSKLSMLDLS SDIRDSIMSS SSSFSFSSNF STLSINSNKR
KTIGDNYINN NLIYNNGNNS FEEFDNFSTL KSPKYHSNKK SSLQHSISIS DDENDNNHNS
SNIPNSNIPN NNIHNNNSDN SDNNNNNNNN NRLSIMVHNN ELGNTETIDI DMSDNNTDFY
NSDAQTIKGE DEERSILEDL SILEAANYSQ GPTKWLKGSR IGAGSFGVVY LGLNALTGEL
MAVKRVEIPK NVSPNTKSNP MVESLQHEIS LLKELSHENI VRYLGSNYDS NYLNIFLEYV
PGGSVSSMLN NYGPFEEPLV RNFTGQVLVG LKYLHSKHII HRDIKGGNIL IDNKGCVKIT
DLGISKKLTS KDKTSKRASM QGSVYWMAPE VVNQTAYTER TDIWSLGCLV VEMLTGKHPY
PTLDITQAIF RIGGKKYPDI PEKCTKDAKN FLEKTFVVDY LIRPSAAELL YHPFLKTLIL
PKI
//
