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
//