ID A0A1J9QDM4_9EURO Unreviewed; 1589 AA.
AC A0A1J9QDM4;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 32.
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=AJ78_05397 {ECO:0000313|EMBL:OJD14239.1};
OS Emergomyces pasteurianus Ep9510.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Ajellomycetaceae; Emergomyces.
OX NCBI_TaxID=1447872 {ECO:0000313|EMBL:OJD14239.1, ECO:0000313|Proteomes:UP000182235};
RN [1] {ECO:0000313|EMBL:OJD14239.1, ECO:0000313|Proteomes:UP000182235}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UAMH 9510 {ECO:0000313|EMBL:OJD14239.1,
RC ECO:0000313|Proteomes:UP000182235};
RG The Broad Institute Genomics Platform;
RA Cuomo C.A., Munoz J.F., Imamovic A., Priest M.E., Young S., Clay O.K.,
RA McEwen J.G.;
RT "Emmonsia species relationships and genome sequence.";
RL Submitted (JUL-2015) 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:OJD14239.1}.
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DR EMBL; LGRN01000233; OJD14239.1; -; Genomic_DNA.
DR STRING; 1447872.A0A1J9QDM4; -.
DR OrthoDB; 8734at2759; -.
DR Proteomes; UP000182235; 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; 2.
DR SUPFAM; SSF52954; Class II aaRS ABD-related; 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:OJD14239.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|PIRSR:PIRSR000660-2};
KW Reference proteome {ECO:0000313|Proteomes:UP000182235};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 42..151
FT /note="RWD"
FT /evidence="ECO:0000259|PROSITE:PS50908"
FT DOMAIN 265..536
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 576..942
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 1..29
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 212..250
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 690..734
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 212..232
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 234..248
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 690..705
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 706..734
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 789
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000660-1"
FT BINDING 582..590
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|PIRSR:PIRSR000660-2"
FT BINDING 606
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 1589 AA; 179648 MW; ED735BF71D4C52CF CRC64;
MPHKHKKSNV LKNGTLKVEK QENPPDTPAI LPATNYKEIH ENEADALRSI YSTDFEDVEA
RQAAWHQASE VAFKLHLRAS SNPEVQVVFV VSLPATYPKT VPNLAVQGLD DLRRGAKSRI
KDVIETKPKT LLGSEMIYEL ALSIQDILED VAIAQAEDKD IPSLEEERIV QEAAAIQQAE
EQKQEELRKQ EQATAEEEKA LQTLLESKIK QRQRAKEQVS RRRSKVPLED NDSLDLSEGS
SSAVSFDPPL TMNDYDERPI TFRSVLGKTL IASAPYKETF TVRPVTPGNG THVPLLVLKE
LFIREKDSGL HDLRHEIRAS EDKLEILKRL RHPNLVDFIG FKIYRPPEPE ASHEITWHIY
TLFEYANKGS LSELLDIVGS VAADTARAWM IQLLDGLEYY HRSGIVHGNI HSGRVLLFRM
QSNNTVLKLL SGVEESLPLP SAAKRTLTSS QSPFWIPPEL TQEGSQPSTK TDVWDLGIVF
LQMSFGKDVM QRYTSANALM RAIDLSMPLE EMLGEIFRPD PKKRPTAFQI QPYEFFRIDA
PLLEPSVTPN TVALRRRSRL DSQGVLPSFS RYGQDFDEAG RLGKGGFGQV VKARNKLDGG
FYAIKKISSK SGIALKDILS EIMLLSRLNH PYVVRYFTAW LERDYHPADE EAVSSTAANS
DHPEDDVDFG YSTSGLDFIS SKGYPDIEFG YDSDGHTDSD TASEESGNHK QGSPLRTDEG
PSLQRQRSGS SSQHVTTTLY IQMEYCEKHT LRDLIRNGLH DDIEFSWRLF RQILDGLSHI
HSHGIIHRDL KPDNIFIDVA NNPRIGDFGL ATTGQFTTAV RSSNVADIGG NYTRSIGTTY
YVAPEMKSVS VGQYNEKVDM YSLGIIFLEM CHPLKTAMER DHTLQNVREK VHTLPATFEV
PEKAIQGEII ESLLSHRPSE RPTAAELLQS GKIPLQVEEE MFRKAIMGIL SDPNSPDYKK
ILSAIFSQPP KKFEDIAWDM DSRGTPPATE LLLQSLVKEK LTSIFRKHGA VEMTRSSLFP
RSEHYPSGVV RLLDPAGNLV QLPYDLTLPN ARSMPRLDSS IEKTFTFGTV YRESMHGGAP
RGHHEVDFDM VSHNTLDLAL KEAEVIKVLD EILNEFPSLR SAPMCFHINH SDLLDAIMSF
CRISPQQTPL VKEIISKLNI GRYSMQKIRS ELRSPTVGVA STSIDDLARF DFRDSPDKAL
KRLRTIMEGT QFADRLAPIF ARLNAVISYL KGFHVRRKIY VNPLSSLNDK FFRGSVLFQC
VSDTKRRDVF AAGGRYDSLI QEFHPKVLYT GTQRHAVGFN LGWEKLCLSM SNYLKGSNKA
FLKQGEVEIS GIWRSRRCDV LVASFDATVL RTVGVGVVQE LWAHGISAEL SVDSSSLEEI
LARYKNDNHS WVLIVKQDSM ERGLKVKNIN TKEEFEVRSS ELVSWLRSEI AARNQREHLT
GAGKPLRNLI HQEPNIATRE KDQDVRILTA LHRNKKTNRR NIIEAAIRES RSVMDRALNG
PIAAIDTRDE ILDALRDTRL SDPDGWRTVI QNCPLTERKY MAQVHEMLND LANERRDPQD
GKENYKNAFI YNYRTGNCIY YDLSRSNEK
//
