ID A0A318Z3W4_9EURO Unreviewed; 1588 AA.
AC A0A318Z3W4;
DT 10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT 10-OCT-2018, sequence version 1.
DT 27-MAR-2024, entry version 20.
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=BP01DRAFT_394572 {ECO:0000313|EMBL:PYH42011.1};
OS Aspergillus saccharolyticus JOP 1030-1.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=1450539 {ECO:0000313|EMBL:PYH42011.1, ECO:0000313|Proteomes:UP000248349};
RN [1] {ECO:0000313|EMBL:PYH42011.1, ECO:0000313|Proteomes:UP000248349}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JOP 1030-1 {ECO:0000313|EMBL:PYH42011.1,
RC ECO:0000313|Proteomes:UP000248349};
RG DOE Joint Genome Institute;
RA Vesth T.C., Nybo J., Theobald S., Brandl J., Frisvad J.C., Nielsen K.F.,
RA Lyhne E.K., Kogle M.E., Kuo A., Riley R., Clum A., Nolan M., Lipzen A.,
RA Salamov A., Henrissat B., Wiebenga A., De Vries R.P., Grigoriev I.V.,
RA Mortensen U.H., Andersen M.R., Baker S.E.;
RT "The genomes of Aspergillus section Nigri reveals drivers in fungal
RT speciation.";
RL Submitted (DEC-2016) 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; KZ821256; PYH42011.1; -; Genomic_DNA.
DR STRING; 1450539.A0A318Z3W4; -.
DR OrthoDB; 8734at2759; -.
DR Proteomes; UP000248349; 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; 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; 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}; Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:PYH42011.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|PIRSR:PIRSR000660-2};
KW Reference proteome {ECO:0000313|Proteomes:UP000248349};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 47..156
FT /note="RWD"
FT /evidence="ECO:0000259|PROSITE:PS50908"
FT DOMAIN 267..535
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 575..941
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 1..27
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 163..204
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 216..238
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 688..731
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1433..1458
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 216..230
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 689..711
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 712..731
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1442..1458
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 788
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000660-1"
FT BINDING 581..589
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR000660-2"
FT BINDING 604
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR000660-2"
FT BINDING 605
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 1588 AA; 179722 MW; 7B6E09B227265B90 CRC64;
MPHKQKKNFN NAPKIGSPRA ERKKLSPDAS AFAPIVAPTN YQEIHQNEVE ALRSIYGDDF
EEVAHRRSAW QQSSELVFKL HLRAMSNPDV HLELLVELPT TYPKTVPNLT LENVDNLRQG
ARSRIQDIVR TKPKTLLGSE MIYELAVSIQ DVLEDLAEAQ AQDRDLPSLE EERMEQEAAA
NQRAELERQE ELRKQEAATA EEERALQQLL EDRLRERTKL SRRKSRTPGL DPNGDSDGVT
QVAGAITFDP PLVLTEPGQD PLFFRAVSGK SLLKSRQYKE TCTVRPIPSD NRAHAPLLVL
KEMSLDQKGV DPLTFREKMR LSEDKLEGLK KLRHPNIRDF IGFQISRPMS SQESFWKVSA
LVEYSNKGTL SEFLDMVGTV PVEMLRSWTL QLLEALEYYH RSGFVHGNIS CGRILLFRNP
TGGTIVKLQA SIEESLPVST AGKRSLTISK SPFWVPPELA HEGAPPTMKT DVWDVGIVFL
QMGFGMDVLQ RYTSANAMMG TLGLTAPLQD LLHEFFRPDP RKRPTAFQLQ PSEFFRVDSP
LIARTSASNS ISLPRRPRLD SLGALPAFSR YNQDFDEAGR LGKGGFGQVV KARNKLDGRF
YAVKKISQKS TTALKDTLSE IMLLSRLNHP YVVRYYTAWI EEDYDYVDEE ALSSTDSDVF
ASRDSGAYDY STGGLDFISS SGYPKIQFGS DSDEDDDGTL SHRRKGDTPD TYETESGTGR
ELSRIGSGSQ GRPVHTTLYI QMEYCEKHTL RDLIRNGLYD DVDRSWRLFR QILDGLSHIH
GHGIIHRDLK PDNIFIDVAN NPRIGDFGLA TSGQFTTAVR SSTTADFEGD FTRSLGTTYY
VAPEMKSGLA ENYNEKVDMY SLGVIFFEMC HPLPTGMERD QTLRAIREKN LTLPSTFQYS
EKILQGRIIR SLLNHDPSQR PSASDLLRSG QIPLQVEEET FRRAIMHLLS DPNSPDYKKI
LSGIFSQSPK KYEDIAWDMD SRGAPAAHEL LVRGLVKERL TSIFRRHGAV ETTRQMLFPR
SQHYHNGAVR LLDSSGNLLQ LPFDLTLPNA RAIPRQDPSL QKTYAFGTVY RETPHGGEPR
THKEVDFDIV SHNTLDLALK EAEVIKVLDE IIDEFPPLRS SPMCFLVNHS DLLQLIMEFC
RITPSQIPRV KEVISRLNVG KWTMQKIRSE LRSPSIGVAS TSLDDLARFD FRDSPKQTQK
RLRAIMEGTR FAERLAPIFA RLNMLTAYLQ GFDVKRKVYV NPLGSLNDKF FRGSILFQCV
FDSKRRDVFA AGGRYDSLVQ EFRPKVLANR SQTHAVGFNL SWDRLSSAML EYLGSGITAK
TAVKHPETET GAFWKTRRCD VLVASFDPTV LRTMGIKLVQ DMWANDISAE LAVDASSLEE
LLNKYKEDSH SWIVIAKQDS QERGFKVKSF SPREELDIRS AELVPWIRNE MRARSQREGT
AEPQRQSRLL SQAEASTVNG DRASDVRILI PQHRSKKSNR RNIVESALFR SREVVEDALH
GPIAAIDTRD DLLEAIRNTR LSDPESWRTV IQNAPLTERK YLNQVHELLS DLANEAQTGD
GTEPLYTNAF IYNYRTGSCI YYDLGSGC
//
