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Database: UniProt
Entry: A0A0A0AD47_CHAVO
LinkDB: A0A0A0AD47_CHAVO
Original site: A0A0A0AD47_CHAVO 
ID   A0A0A0AD47_CHAVO        Unreviewed;      1596 AA.
AC   A0A0A0AD47;
DT   07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT   07-JAN-2015, sequence version 1.
DT   24-JAN-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};
DE   Flags: Fragment;
GN   ORFNames=N301_08582 {ECO:0000313|EMBL:KGL92031.1};
OS   Charadrius vociferus (Killdeer) (Aegialitis vocifera).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Charadriiformes; Charadriidae; Charadrius.
OX   NCBI_TaxID=50402 {ECO:0000313|EMBL:KGL92031.1, ECO:0000313|Proteomes:UP000053858};
RN   [1] {ECO:0000313|EMBL:KGL92031.1, ECO:0000313|Proteomes:UP000053858}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BGI_N301 {ECO:0000313|EMBL:KGL92031.1};
RA   Zhang G., Li C.;
RT   "Genome evolution of avian class.";
RL   Submitted (JUN-2014) 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   -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC       kinase family. GCN2 subfamily. {ECO:0000256|ARBA:ARBA00037982}.
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DR   EMBL; KL871394; KGL92031.1; -; Genomic_DNA.
DR   STRING; 50402.A0A0A0AD47; -.
DR   Proteomes; UP000053858; 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:0003743; F:translation initiation factor activity; IEA:UniProtKB-KW.
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-domain.
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   PANTHER; PTHR11042:SF186; KINASE, PUTATIVE-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; 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   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PIRSR:PIRSR000660-
KW   2}; Coiled coil {ECO:0000256|SAM:Coils};
KW   Initiation factor {ECO:0000313|EMBL:KGL92031.1};
KW   Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:KGL92031.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|PIRSR:PIRSR000660-2};
KW   Protein biosynthesis {ECO:0000313|EMBL:KGL92031.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000053858};
KW   Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          1..90
FT                   /note="RWD"
FT                   /evidence="ECO:0000259|PROSITE:PS50908"
FT   DOMAIN          248..491
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   DOMAIN          543..961
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   REGION          182..213
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          641..696
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          709..734
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          96..153
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        655..676
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        709..732
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        794
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000660-1"
FT   BINDING         549..557
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000660-2"
FT   BINDING         572
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000660-2,
FT                   ECO:0000256|PROSITE-ProRule:PRU10141"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:KGL92031.1"
FT   NON_TER         1596
FT                   /evidence="ECO:0000313|EMBL:KGL92031.1"
SQ   SEQUENCE   1596 AA;  181583 MW;  86166079B2025AED CRC64;
     IQQPPEINLV LRPQGLTGDN EVYAKVDLWV KCPHTYPDTV PEIQLKNSKG LSNEKINELK
     SRLAELAKQR CGEVMIFELA DHVQSFLSEY NKPPSKSFHE EMLKNHQKEQ ERLAQEELRR
     AQEQREILNE IQRREEEKRE ERKKKEIAKQ ERLEVAALTS QENSHRRDAA GYRVASSLNG
     SCLEHGVNNK HRPNSAGRSK RERQFSVSNN EESPGNYEVL NFSTSGSGQL IVHKGKCLSK
     DEQLGKSVYN ALEIRSGDFV LVYEWVLHWQ KKMGKFLTSH EIEKIEKCKK QLQGAETEFS
     SLMKLSHPNI VHYKCMNLKE RDDSIVVDIL VEHISGYSLS TYLYKETPVP IEQLRHYVTQ
     ILSALDYLHN NSVVHKVLCA SSILVDAEGN IKVTDYSISK RLADICKADV FEQTKVRFSE
     DGLPSKPGKK GDIWSLGLLL LSLSQGQVTK EYPVAVPTNL PADFQDFLEK CVCLEDKERW
     TPQQLLQHSF INIPRMKIPV AEENLDDSAG IDCIETVVPS SRISSASFFT ETQRQFSRYY
     NEFEELKLLG KGAFGAVIKV RNKLDGCYYA VKRIRINPAS KQFRRIKGEV TLLSRLNHEN
     IVRYYNAWIE KHESPVPTVS SETTEGKRMP TKAGLFIPAT EETNDVEANA PPPVLTSSVE
     WSTSCERSSS NKFSGADQES SDDDDDGDGV FSHSFLPTTD SESEIIFDNE DETSKDHPPD
     EEDNERNSRG GEDRAPVIQT VHYLYIQMEY CEKSTLRDTI DQGLYEDTSR LWRLFREILD
     GLAYIHEKGM IHRDLKPVNI FLDSDDHVKI GDFGLATDHP ANAVVSKQDE NPSDSSAMSD
     PSGNLTGMVG TALYVSPEVQ GSTKSTYNQK VDLFSLGIIF FEMSYHPMST ASERIFVLGQ
     LRLPNIVFPQ DFDEVKNAKQ RSVITWLLNH DPAARPTAVE LLKSEHLPPP QMEESELHEV
     LHHTLANVDG KAYRTMMSQI FSQRVSPAID YTYDSDMLKG SFSIWAAKIQ QHVCEIVSRI
     FKRHGAIKLH TPLLMPRNKK LYEHNEASYF MDHSGMLVML PYDLRIPFAR FVARNNISNL
     KRYCIERVFR PRKLDRCHPK ELLECAFDII TSTGNSFLPI AETIYAISEI IQEFSVLQER
     NYSIYLNHTA LLKAILLHCG IPEDKLNQVY IILYDAVTEK LTKREVEAKF CNLSLTSNSL
     SRLYRFIEQK GEASNVFPFL NTMIKQKPGV TQLLKHGMKD LEEIIGLLKQ LGIKLQISIN
     LGLVYKIQQH NGIIFQFIAY IKRRQRTVPE ILAAGGRYDH LIPQFRGPQM VGPVPSAVGV
     SIAIDKITAA VSSVEESVSA SSCDLLVVSV GQMSMGRAIN IVQKLWMAGI PAEIMYDWSQ
     SQEELQEYCR CSGITYVALV SDKEGSHVKV KSFEKDRQTE KRILESDLVD HLIQKLKTKI
     CDERCSRETS DNLSVPNQKG SFTNNSGVFE SHGTLVVPNV SVIAPEKLSA SARRRQEIQV
     QTRLQTFISS LQQKTSEIEI LAVDLPKATV MPFLSLKFDG DRQAFDATVR QLMSRWPKQR
     CSYLQAICDE IYSIKMEKRV PALILYSYRD EYKVLF
//
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