ID A0A397GG46_9EURO Unreviewed; 1575 AA.
AC A0A397GG46;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 18.
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=CDV56_103158 {ECO:0000313|EMBL:RHZ48784.1};
OS Aspergillus thermomutatus.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=41047 {ECO:0000313|EMBL:RHZ48784.1, ECO:0000313|Proteomes:UP000215305};
RN [1] {ECO:0000313|EMBL:RHZ48784.1, ECO:0000313|Proteomes:UP000215305}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HMR AF 39 {ECO:0000313|EMBL:RHZ48784.1,
RC ECO:0000313|Proteomes:UP000215305};
RA Parent-Michaud M., Dufresne P.J., Fournier E., Martineau C., Moreira S.,
RA Perkins V., De Repentigny L., Dufresne S.F.;
RT "Draft genome sequence of azole-resistant Aspergillus thermomutatus
RT (Neosartorya pseudofischeri) strain HMR AF 39, isolated from a human nasal
RT aspirate.";
RL Submitted (AUG-2018) 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};
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:RHZ48784.1}.
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DR EMBL; NKHU02000190; RHZ48784.1; -; Genomic_DNA.
DR STRING; 41047.A0A397GG46; -.
DR VEuPathDB; FungiDB:CDV56_103158; -.
DR OrthoDB; 8734at2759; -.
DR Proteomes; UP000215305; Unassembled WGS sequence.
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; 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; 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; 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 PIRSF; PIRSF000660; Ser/Thr_PK_GCN2; 1.
DR SMART; SM00591; RWD; 1.
DR SMART; SM00220; S_TKc; 2.
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}; Kinase {ECO:0000256|ARBA:ARBA00022777};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|PIRSR:PIRSR000660-2};
KW Reference proteome {ECO:0000313|Proteomes:UP000215305};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW Transferase {ECO:0000256|ARBA:ARBA00022777}.
FT DOMAIN 48..158
FT /note="RWD"
FT /evidence="ECO:0000259|PROSITE:PS50908"
FT DOMAIN 226..542
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 582..948
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 1..43
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 165..202
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 699..733
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 11..43
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 167..202
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 795
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000660-1"
FT BINDING 588..596
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR000660-2"
FT BINDING 611
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR000660-2"
FT BINDING 612
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 1575 AA; 177949 MW; 15C4F7BC706E1BDE CRC64;
MPHKQKKNPS NAHKNGSPRA ERKQSTSNTA PLAQPGLATT NYREIHQNEV EALRSIYGDD
DFEEIKHRPS AWQQSSDVAF KLHLRASSNP EVRVDLLVEL PTTYPKTYPN LSLGNSENIR
HRARLKIQDI IRNKPKELLG SEMIYELAVS IQDVLEDVAQ AQAQDKDLPS LEEERMEQEA
AANQRAELER QEELRKQEAA TAEEERALQQ LLEDKLRERT KARLSRRKSR TSGIGLSGSV
DAVDHFPGAI TFDPPLIIND TDEQPLGFRA VYGKTLLQSS PGKQTFTVRP VVSESRSHAP
LIVLKELSLD GKGTASLVFR ERMRASEDKL EALKKLRHPN LVDFIGFKIY RPLDSFEAQD
STWRVYLLLE YANKGSLSEF LDIVGSVSVE IIRSWMIQLL EALEFYHRNG FVHGNIHCGR
ILLFRNPHGG TIVKLQGSIE DTLPDTDGSK RSLTISKSPF WMPPELTQES TPPTMKTDVW
DMGIVFLQMA FGKDVLQRYT SANALMGTLG LSAPLQDLLH EFFRPDPKKR PTAFQLQPFE
FFRVDTPLIA RTSTSNSVSL PRRPRLDSIG GLPAFSRYNQ DFDEAGRLGK GGFGQVVKAR
NKLDGRFYAI KKISQRSASA LKDTLSEIML LSRLNHPYVV RYFTAWLEEE YDHIEEEAIS
STEGDPFASR DANGFGYSTG GLDFISSSGY PKIEFASDSE DEHDASVSHR GGTESYDAYG
EESVPGTELS RVRSGSQGRA HLTTLYIQME YCEKHTLRDL IRNGLCDDID RSWRLFRQIL
DGLSHIHSHG IIHRDLKPDN IFIDVASNPR IGDFGLATSG QFTTAVRSST TADFEGNLTR
SLGTTYYVAP EMKSGFAGHY NEKVDMYSLG IIFFEMCHPL PTGMERDQTL RAIREEHHIL
PPTFQYSEKA VQGSIIKSLL SHNPEERPSA SELLQSGKIP LQVEEETFRR AIVHLLSDPN
APDYKKILSA IFSQSPKKYE DIAWDMDSRA APAANELLVQ GLVKERLTAI FRRHGAVETT
RQMLFPRSQH YRSGAVRLLD ASGNLLQLPF DLTLPNARSI SRQDPSLEKT FAFGTVYREM
PHGSEPRTHK EVDFDIVSHN TLDLALKEAE VIKVLDEIIE EFPPLRSSPM SFLVNHSDLL
QLIMEFCRIT PSQIPLVKEV ISKLNFGKWT MQKIRSELRS PAIGVASTSL DDLARFDFRD
TPKQAQKRLR SIMEGTEFAE RLSPIFARIN VLVTYMQGFD VKRKVYVNPL GSLNDKFFRA
GGRYDRLVQE FCPKVLRSRS QTHAVGFNLS WDRLSSAMLE YLKGTTKAPV KHAESDAGAF
WKTRRCDVLV ASFDATVLRT MGVKLVQDLW ASDISAELAV DASSLEELLS EYKDHNHSWI
VIAKQDSKER GFKVKCLVPK EELDIRSSEL IPWLRNEIRA RNQREGAPDL RQSRLPSQSD
AIAGANERAN DVRILVSQHR SKKTNRRNIV ESALLRSREV VEKAINGPIA AIDTRDDLLE
AIRDTRLSDP ESWRSVIQSA PLTERKYLSQ VHELLLDLAN ESLTKDGPDS VSNAFIYNYR
TGSCLYYDLG RGSEK
//
