ID A0A319A4P0_ASPLB Unreviewed; 1592 AA.
AC A0A319A4P0;
DT 10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT 10-OCT-2018, sequence version 1.
DT 27-MAR-2024, entry version 22.
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=BO96DRAFT_81407 {ECO:0000313|EMBL:PYH54869.1};
OS Aspergillus lacticoffeatus (strain CBS 101883).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=1450533 {ECO:0000313|EMBL:PYH54869.1, ECO:0000313|Proteomes:UP000247441};
RN [1] {ECO:0000313|EMBL:PYH54869.1, ECO:0000313|Proteomes:UP000247441}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 101883 {ECO:0000313|EMBL:PYH54869.1,
RC ECO:0000313|Proteomes:UP000247441};
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; KZ821356; PYH54869.1; -; Genomic_DNA.
DR OrthoDB; 8734at2759; -.
DR Proteomes; UP000247441; 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; 2.
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:PYH54869.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|PIRSR:PIRSR000660-2};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 49..158
FT /note="RWD"
FT /evidence="ECO:0000259|PROSITE:PS50908"
FT DOMAIN 273..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..201
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 221..240
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 695..735
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1443..1462
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 27..43
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 709..735
FT /note="Polar 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 1592 AA; 180162 MW; E35FC407D03DDB8D CRC64;
MPHKQKKNFS NAPKHGSPRA EKKQQLRPDS PSFSPPVVAP TNYQEIHQNE VEALRSIYGD
DFEEVQHRRS AWQQSSEVSF KLHLRASSNP DVHLELLVEL PTTYPKTYPN LSLENLDDLR
KGARSRIQDI IQNKPKTLLG SEMIYELAVS IQDVLEDVAE AQAQDKDLPS LEEERMEQEA
AANQRAELER QEEIRKQEAA TAEEERALQQ LLEDKVRERA KARLSRRKSR TPGLDANGDA
DAVENIPGAI TFDPPLAMTD SDQATLVFRA VYGKSLLQIG PGKETYTVRP VVSDNRSHAP
LLVLREISLD EKGVEPLLFR EKMRSSEDRL EGLKKLRHPN LVDFVGFKIT RPLSMQDAQD
SIWTVYALQE YSNKGTLAEF LDIVGTVPVE VLRSWTIQLL EALEFYHRSG FVHGNIHCGR
ILLFRTRTGG TIVKLRAGIE EALPDSPASK RLLTTSKSPF WMPPELTHGT APLTMKTDVW
DLGIVFLQMG FGMDVLQRYT SANALMGTLG LTTALQDLLH EFFRPDPKKR PTAFQLQPSE
FFRVDTPLIS RTSASNSISL PRRPRLDSLN GLPAFSRYNQ DFDEAGRLGK GGFGQVVKAR
NKLDGRFYAV KKITQKSTAA LKDTLSEIML LSRLNHPYVV RYYTAWIEED YDYVDEEAIS
STESDVFASR DTHAYDYSTG GLDFISSSGY PKIEFGSDSE EDNDGTLSNG DKGDTPSTFE
TESATGKELS RVRSGSQGRP VLTTLFIQME YCEKHTLRDL IRNGLYDDVD RSWRLFRQIL
DGLSHIHGHG IIHRDLKPDN IFIDVANNPR IGDFGLATSG QFTTAVRSST TADFEGNFTR
SLGTTYYVAP EMKSGFTGNY NEKVDMYSLG VIFFEMCHAL STGMERDQTL RAIREPNHTL
PSTFQSSEKV VQGRIINSLL SHNPSERPTA SDLLRSGKIP LQVEEETFRR AIMHLLSDPN
SPDYKKILSG IFSQSPKKFE DIAWDMDSRG TPGATELLIQ GLVKEKLTSI FRRHGAVETQ
RQMLFPRSQH YNNGAVRLLD SSGNLLQLPF DLTLPNARAI PRQDPSLEKT YAFGTVYREL
PHGGEPRTHK EVDFDIVSHN TLDLALKEAE VIKVLDEIIE EFPPLRSSPM CFVINHSDLL
QIIMEFCRIT PSQIPRVKEV VSKLNVGKWT MQKIRSELRS PAIGVASTSL DDLARFDFRD
SPKQVQKRLR AIMQGTIFAE RLAPIFARIN LLVAYLQNFD VKRKVYMNPL GSLNDKFFRG
SILFQCVFDS KRRDVFAAGG RYDSLVQEFR PKVLASRSQT HAVGFNLSWD RLSSAMLEYL
GTPAKTPAKS FDMEAGAFWK TRRCDVLVAS FDPTVLRTMG IKIVQDLWLN DVSAELAVDA
SSLEELLNKY RDDSHGWIVI AKQDSQERGF KVKSLSPREE FDIRGSELVP WLRNEIRARY
QREGADPLRQ SRLPSQADPG PSFNERFSDV RILVPQHRSK KSNRRNIVET ALFRSREVVE
DALNGPVAAI DTRDELLEAI RNTRLSDPES WRTVIQNAPL TERKYLTQVH ELLLDLANES
RVDGMESFSN AFIYNYRTGS CIYYDLGSAA DR
//
