ID J7S0I4_KAZNA Unreviewed; 1659 AA.
AC J7S0I4;
DT 31-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 31-OCT-2012, sequence version 1.
DT 27-MAR-2024, entry version 54.
DE RecName: Full=non-specific serine/threonine protein kinase {ECO:0000256|ARBA:ARBA00012513};
DE EC=2.7.11.1 {ECO:0000256|ARBA:ARBA00012513};
GN Name=KNAG0F03410 {ECO:0000313|EMBL:CCK71002.1};
GN OrderedLocusNames=KNAG_0F03410 {ECO:0000313|EMBL:CCK71002.1};
OS Kazachstania naganishii (strain ATCC MYA-139 / BCRC 22969 / CBS 8797 / KCTC
OS 17520 / NBRC 10181 / NCYC 3082 / Yp74L-3) (Yeast) (Saccharomyces
OS naganishii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Kazachstania.
OX NCBI_TaxID=1071383 {ECO:0000313|EMBL:CCK71002.1, ECO:0000313|Proteomes:UP000006310};
RN [1] {ECO:0000313|EMBL:CCK71002.1, ECO:0000313|Proteomes:UP000006310}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-139 / BCRC 22969 / CBS 8797 / CCRC 22969 / KCTC 17520
RC / NBRC 10181 / NCYC 3082 {ECO:0000313|Proteomes:UP000006310};
RX PubMed=22123960; DOI=10.1073/pnas.1112808108;
RA Gordon J.L., Armisen D., Proux-Wera E., OhEigeartaigh S.S., Byrne K.P.,
RA Wolfe K.H.;
RT "Evolutionary erosion of yeast sex chromosomes by mating-type switching
RT accidents.";
RL Proc. Natl. Acad. Sci. U.S.A. 108:20024-20029(2011).
RN [2] {ECO:0000313|Proteomes:UP000006310}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-139 / BCRC 22969 / CBS 8797 / CCRC 22969 / KCTC 17520
RC / NBRC 10181 / NCYC 3082 {ECO:0000313|Proteomes:UP000006310};
RA Gordon J.L., Armisen D., Proux-Wera E., OhEigeartaigh S.S., Byrne K.P.,
RA Wolfe K.H.;
RT "Genome sequence of Kazachstania naganishii.";
RL Submitted (AUG-2012) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
CC [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1;
CC Evidence={ECO:0000256|ARBA:ARBA00001433};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
CC threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
CC Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC EC=2.7.11.1; Evidence={ECO:0000256|ARBA:ARBA00000775};
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DR EMBL; HE978319; CCK71002.1; -; Genomic_DNA.
DR STRING; 1071383.J7S0I4; -.
DR eggNOG; KOG1035; Eukaryota.
DR HOGENOM; CLU_001222_2_0_1; -.
DR OMA; EFYHRSG; -.
DR OrthoDB; 8734at2759; -.
DR Proteomes; UP000006310; Chromosome 6.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004694; F:eukaryotic translation initiation factor 2alpha kinase activity; IEA:InterPro.
DR GO; GO:0000077; P:DNA damage checkpoint signaling; IEA:InterPro.
DR CDD; cd00773; HisRS-like_core; 1.
DR CDD; cd14012; PK_eIF2AK_GCN2_rpt1; 1.
DR CDD; cd14046; STKc_EIF2AK4_GCN2_rpt2; 1.
DR Gene3D; 3.40.50.800; Anticodon-binding domain; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 2.
DR Gene3D; 3.10.110.10; Ubiquitin Conjugating Enzyme; 1.
DR InterPro; IPR045864; aa-tRNA-synth_II/BPL/LPL.
DR InterPro; IPR036621; Anticodon-bd_dom_sf.
DR InterPro; IPR016255; Gcn2.
DR InterPro; IPR041715; HisRS-like_core.
DR InterPro; IPR024435; HisRS-related_dom.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR006575; RWD_dom.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR InterPro; IPR016135; UBQ-conjugating_enzyme/RWD.
DR PANTHER; PTHR11042:SF197; EIF-2-ALPHA KINASE GCN2; 1.
DR PANTHER; PTHR11042; EUKARYOTIC TRANSLATION INITIATION FACTOR 2-ALPHA KINASE EIF2-ALPHA KINASE -RELATED; 1.
DR Pfam; PF12745; HGTP_anticodon2; 1.
DR Pfam; PF00069; Pkinase; 3.
DR Pfam; PF05773; RWD; 1.
DR Pfam; PF13393; tRNA-synt_His; 1.
DR PIRSF; PIRSF000660; Ser/Thr_PK_GCN2; 1.
DR SMART; SM00591; RWD; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF55681; Class II aaRS and biotin synthetases; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 2.
DR SUPFAM; SSF54495; UBC-like; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 2.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
DR PROSITE; PS50908; RWD; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PIRSR:PIRSR000660-
KW 2}; Coiled coil {ECO:0000256|SAM:Coils};
KW Kinase {ECO:0000256|ARBA:ARBA00022777};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|PIRSR:PIRSR000660-2};
KW Reference proteome {ECO:0000313|Proteomes:UP000006310};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 17..128
FT /note="RWD"
FT /evidence="ECO:0000259|PROSITE:PS50908"
FT DOMAIN 202..526
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 592..982
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 548..569
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 667..697
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 718..772
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1512..1541
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 142..172
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 681..697
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 718..748
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 751..765
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1517..1541
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 836
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000660-1"
FT BINDING 598..606
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR000660-2"
FT BINDING 621
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR000660-2"
FT BINDING 622
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 1659 AA; 188896 MW; 5428804ABE5D87CE CRC64;
MSLSHLTLDQ YYEIQSNELE AIRSIYMDDF VDLTRKKSGW DKQPQIIFEI SLRSGEKDPV
ESSLTLHIAL TPMYPHTTPE ITFKNVENVL DSQLQSLVDE YKKIHRGARG QEFIFDIATS
TQEKLDEFQR GANPQSLEDD RLQRIKETTE KLEREEMESQ RQIEKLKISE QQRIDEIVQK
ELEKRQDDDD MFFNSGNQIN FLPPNEWISS GEAIVFPKII KAKLPNNSLL KFKAVVNPKE
VKISSDLLCF AKQYLVKPYI SPDSPLAESL MSSEVMENFY FLMTEVELDN SYFNTSNGKK
EISHFEKILD SLLKVKHDNV NQLYGYLVER MGKNNSTFVW KIKFLSEYSM SYPLGDIVQS
VGFINLATAR IWMIRLLEGL EALHKLGVHH ACIGLQTVYL VKDPDFGTTI PKIVYPEYGY
MLVNMLTRYP NRHGTQVELP SNPWTAPESS NYKNTKSQRM TDIWQLGVLF IQMINGVNTV
LDYSTPLDFM ESNDMESSLS DFLEKMLNVD PKRRLGPLEL LPMKFLRTNI DSDVNKLNLL
PGTSSTELNS MDIPRSTPRA LSHSSSGRRS FNVGSRFSSM NRSSRSRYAT DFEEIAVLGK
GAFGQVVKAR NTLDSRYYAV KKIRHTEEKL STILSEVMLL ASLNHQYVVR YYAAWLEEDY
LNENVIDSSD EDDTEDDTEE ASVTASASYS ESMRSKQPLH NSNWDFISNS GYPEIEFGNS
STGPNITGSG VSDGIVFENS TEEGGVGNTE DSNSEDEKDS PGLRVGKQKK NSTFRKSVGN
RKSILFIQME YCENRTLYDL IHAENLNNER DGYWRLFRQI LEALSYIHSQ GIIHRDLKPM
NIFIDESRNV KIGDFGLAKN VQRPLDISKL DSATAQRSTD NLTSAIGTAL YVAVEVLSGK
GNYNEKIDMY SLGIIFFEMV YPFSTGMERV NILKNLRSPT VEFPRDFDDT KMKTERKIIT
LLLDHDPNKR PAARALLNSG WLPVKHQDEV IKEALKSLSN PSSPWQQQVR DSLFTQSYSL
SNDILFDNVQ SATTRFTQVL RSQMTEEVVK IFRKHGGIEN NAPSRIFPKA PIYSTQNVYE
VLDHGGSVLQ LQYDLTYPMA RYLSKNPPCV SKQFRLQFVY RPPEQLKSSM EPRKFGEIDF
DIVSSSSAQS PFYDAESIKI IDEILTTFPV FEKGNTLFVL NHADILESVF DFSNIDKAQR
PLISRMLSQI GFAKSFKEVK AELKSQLNIP SISLNDLDLF DFKLDFETAK RRFHKVMVDS
PYLRKIDESL VHISKVLNFL KPLDVTRNVV ISPLSNYNSA FYKGGIMYQA VYDDGSNRSL
IAAGGRYDNL ISYFARPSGS KRSSTKRAVG FNLAWETIFG VAQSYFKLAS GNKVKKRNKF
LKDGAIEWKP RRCDILISSF SNSILETMGV PMLNQLWKIG IKADLLFDCY TVDDVVSAAK
HDGVDWIVLI KQQTYTLSNH KRKYKPLKVK KMSSDLDVDL DIHEFLQLYE HETEGSGSFN
VGMALPDKHD EFGYGEDGSS ASSSHEGDPQ NEEPTKSNQK VIYVPNMATR SKKANKREKW
VYEDSARNAS NAIINSLTQA PVITVDAIRD ETLEIISITS LAQKEEWLRK VFGSVNNSSP
RSFATSIYNS LSKEAAKGNK WAILHCHKTG KSCVIDLQR
//
