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Database: UniProt
Entry: A0A1E3QW23_9ASCO
LinkDB: A0A1E3QW23_9ASCO
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ID   A0A1E3QW23_9ASCO        Unreviewed;      1032 AA.
AC   A0A1E3QW23;
DT   18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT   18-JAN-2017, sequence version 1.
DT   27-MAR-2024, entry version 33.
DE   RecName: Full=non-specific serine/threonine protein kinase {ECO:0000256|ARBA:ARBA00012513};
DE            EC=2.7.11.1 {ECO:0000256|ARBA:ARBA00012513};
GN   ORFNames=BABINDRAFT_170486 {ECO:0000313|EMBL:ODQ81858.1};
OS   Babjeviella inositovora NRRL Y-12698.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; CUG-Ser1 clade incertae sedis; Babjeviella.
OX   NCBI_TaxID=984486 {ECO:0000313|EMBL:ODQ81858.1, ECO:0000313|Proteomes:UP000094336};
RN   [1] {ECO:0000313|Proteomes:UP000094336}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NRRL Y-12698 {ECO:0000313|Proteomes:UP000094336};
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.
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DR   EMBL; KV454427; ODQ81858.1; -; Genomic_DNA.
DR   RefSeq; XP_018987186.1; XM_019130746.1.
DR   AlphaFoldDB; A0A1E3QW23; -.
DR   STRING; 984486.A0A1E3QW23; -.
DR   GeneID; 30148599; -.
DR   OrthoDB; 1630at2759; -.
DR   Proteomes; UP000094336; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR   GO; GO:0004521; F:RNA endonuclease activity; IEA:InterPro.
DR   GO; GO:0030968; P:endoplasmic reticulum unfolded protein response; IEA:InterPro.
DR   GO; GO:0006397; P:mRNA processing; IEA:InterPro.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   CDD; cd10422; RNase_Ire1; 1.
DR   Gene3D; 1.20.1440.180; KEN domain; 1.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR   Gene3D; 2.130.10.10; YVTN repeat-like/Quinoprotein amine dehydrogenase; 1.
DR   InterPro; IPR045133; IRE1/2-like.
DR   InterPro; IPR010513; KEN_dom.
DR   InterPro; IPR038357; KEN_sf.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR011047; Quinoprotein_ADH-like_supfam.
DR   InterPro; IPR008271; Ser/Thr_kinase_AS.
DR   InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR   PANTHER; PTHR13954; IRE1-RELATED; 1.
DR   PANTHER; PTHR13954:SF6; NON-SPECIFIC SERINE_THREONINE PROTEIN KINASE; 1.
DR   Pfam; PF00069; Pkinase; 1.
DR   Pfam; PF06479; Ribonuc_2-5A; 1.
DR   SMART; SM00580; PUG; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   SUPFAM; SSF50998; Quinoprotein alcohol dehydrogenase-like; 1.
DR   PROSITE; PS51392; KEN; 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};
KW   Kinase {ECO:0000256|ARBA:ARBA00022527};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000094336};
KW   Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          593..900
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   DOMAIN          903..1032
FT                   /note="KEN"
FT                   /evidence="ECO:0000259|PROSITE:PS51392"
FT   REGION          490..546
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          562..588
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        490..511
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1032 AA;  116255 MW;  601D0487677840AF CRC64;
     MYVYRFALIP ILRELPYTFE CDCIIRIYAT LKLQTTHSLL KVASELYARP LEAWDVTDTL
     LASDIEGALH GLNRTTGEVL WTLPGTPLVQ IVNQTHTSPE DQRSEVIWAV EPLDDGRLYY
     FSKEMGLQEF PVSIKHLVLE SPFVLSGDDK IYTGAMRSLL YDIRVSDGEV LGTYGPGSPS
     MQCPVDPRGP EEPHVYVSQT IYELTIQGSN QGKDQATWKV TYASWGPNNM DKDLVQQSRY
     PRDMFLAPNY DASVLAMDLE LPTPKWVSRL PAIAVNVFDI FLSHSAELAV LPHPLKPDSE
     AFNPKADYGT FLDQTSTGSW YAMSGFNYPL LVASAPRSQY WTSSRWHSRD VPSSPDFENL
     TLNGVHKSLV LETTHTRERL PSPAATILKN LPATTTTTTP WGHQRIPKPI QPVTLDITED
     YLTMSLGKIV LRIVENAVTT LVVVMVMVGL GKMGVIPPFT KILVKLGFFR RTQNAIEIVE
     KMLSEEEVDL ARELSTPEPD DKRKKSVTIL DHGEISKTTD AVSSPEDAGP KRRKRGSRGG
     KKNKKESEIA LESLSLEVDS SISSEVGSST KSEGSLLSEV GSANSRSSTG NLVISDTVLG
     YGSHGTVVYK GTFESRPVAV KRMLLDFFDV AQHEVALLQE SDDHPNVVRY FCSQESEKFL
     YIALELCSAS LEDVVEKAQR YPELSSMRPN TILYQIACGL NYLHSLKIVH RDLKPQNILV
     APPKHRHRGE AVPPRTLISD FGLCKKLEAD QSSFRATTAN AAGTAGWRAP ELLVDEHDSV
     YNNIITNGTM TSDLNHSIPG MNATGASEPL VYDSLSKRKL TRAIDVFSMG CVFYYVLTSG
     QHPFGDRYLR EGNIIKGEYC LDLLDVLPDA FEARHLIAHM IARNPRLRLD SLQIMKHPYF
     WLYEKRFDFL LKVSDRFEVE RRDPPSPLLL KLEEIAPQVV GKDWRAKFGR LFLDNLGKYR
     KYHGLKLMDL LRALRNKYHH FNDMPEALME EMGPLPDGFY AYFNSRFPNM LMEIYFVVQE
     NLADEQTLRA FY
//
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