ID A0A3B3RFP2_9TELE Unreviewed; 1586 AA.
AC A0A3B3RFP2;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=Eukaryotic translation initiation factor 2-alpha kinase 1 {ECO:0000256|ARBA:ARBA00040433};
DE EC=2.7.11.1 {ECO:0000256|ARBA:ARBA00012513};
DE AltName: Full=Heme-regulated eukaryotic initiation factor eIF-2-alpha kinase {ECO:0000256|ARBA:ARBA00042914};
DE AltName: Full=Hemin-sensitive initiation factor 2-alpha kinase {ECO:0000256|ARBA:ARBA00042456};
GN Name=EIF2AK4 {ECO:0000313|Ensembl:ENSPKIP00000016496.1};
OS Paramormyrops kingsleyae.
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Osteoglossocephala;
OC Osteoglossomorpha; Osteoglossiformes; Mormyridae; Paramormyrops.
OX NCBI_TaxID=1676925 {ECO:0000313|Ensembl:ENSPKIP00000016496.1, ECO:0000313|Proteomes:UP000261540};
RN [1] {ECO:0000313|Ensembl:ENSPKIP00000016496.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
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:ARBA00001127};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:17990;
CC Evidence={ECO:0000256|ARBA:ARBA00001127};
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:ARBA00001416};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:46609;
CC Evidence={ECO:0000256|ARBA:ARBA00001416};
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 Ensembl; ENSPKIT00000040991.1; ENSPKIP00000016496.1; ENSPKIG00000002734.1.
DR GeneTree; ENSGT00940000156798; -.
DR Proteomes; UP000261540; Unplaced.
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:SF136; EUKARYOTIC TRANSLATION INITIATION FACTOR 2-ALPHA KINASE 1; 1.
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; 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 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PIRSR:PIRSR000660-
KW 2}; Coiled coil {ECO:0000256|SAM:Coils};
KW Kinase {ECO:0000256|ARBA:ARBA00022777};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|PIRSR:PIRSR000660-2};
KW Protein synthesis inhibitor {ECO:0000256|ARBA:ARBA00023193};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 19..132
FT /note="RWD"
FT /evidence="ECO:0000259|PROSITE:PS50908"
FT DOMAIN 287..530
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 582..996
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 184..249
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 659..707
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 712..731
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 750..782
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 317..344
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 184..202
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 750..779
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 841
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 ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 1586 AA; 178461 MW; 56808EAB4DF5367E CRC64;
MSFKNPTDGA ESYLAQQENE LEALASIFGD DFEDIRKKQP WKVKRPPEVY LYLRPKGLSD
GKESYVSVDL EVKCPPNYPD VPPKVELKNA KGLSNGNLQN LHVELAKLAA ERCGEVMIYE
LADYVQGFLT EHNVPPPRSF HEEMLKNQQR EQERLVQEEQ RRIDLERHKE EQTKIEILAE
LQRREEEKKE EKKRKEVAKQ ERFENAAQPA SEIQVPAPEQ SETRKGCSSR RRANSSNRHR
RETNHSVCSD DGIRQQEVLH FSNSALGEIK VHKGRLIGES EALSRSVYRA FNASSGDFAV
VYEWTLCWNK KMGKFLTDQE KEKIEKCKKQ IQGMESELNS LLKLEHLHLV QYMALSHREL
EDSLVVDLLV EHVTGHSLSQ TLARGAPLPT DRLRQLAAQL LSALDYLHSN SVVHKRLTAS
SVLLDAEGTV RLTDYSLSKR LADVCKEDVF EQTRVRFSEA AVPAKAGKKG DVWSLGLLLL
ALSQGSEVKE YPVSVPSSLP ADFQDFLSRC VCLNDAERWN TQQLLSHAFF NPPSPRTSPH
CYDSPEDVGD DFASTVVSRG RILETPFSTD IQKQFSRYYN EFEELQMLGK GAFGAVIKVQ
NKLDGCYYAV KRIQVNPASK QFRRIKGEVT LLSRLNHENI VRYYNAWIER HERPSVGVLS
SDSSEMVSSP GKPPQCVSRP RNELGLPDDV EDKAPPPALS SSVEWSTSIE RSTSAKCSGA
NSESSDEDDE EEDVFCPSFL PCSSDSDSDI VFDNDHGSKD SLSQEAQSKG KEESAMESTD
SETPHLIAHY LYIQMEYCEK STLRDTIDKG LHLDCSRLWR LFREILDGLA YIHEQGMIHR
DLKPVNIFLD SQDHVKIGDF GLATDHPANV AASKQEMEES VSALLIKPDP TDNMTGMVGT
ALYVGPEVQG STKSSYNQKV DLFSLGIILF EMSYRPMTTA SERIAVLSQL RTESIQFPED
FRGSEQGTQM KVISWLLNHD PAKRPTAVEL LKSDLLPPPQ MEESELHEVL QHTMNNVNGK
AYRTMVNRLF AQSVAPGIDY AYDIDFHKGS FNSSAAKLQQ YVHETISRIF KKHGAVRFQT
PLLMPKSKAL YEGSDLACFM DHSGMLVTLP YDLRLAFARY VARSNISSLK RYSIDRVFRP
RKPDRTHPKE LLECAFDIVT PATSSLLPDA ETIYTISEII QEFSTLQERN YSIYLNHTSL
LKAVLLHSGI PEDKLQQASN ILCDTMTEKL TRREVEAKFC NLSLSTNSVQ TLYKYIEQKG
ALHELLPLIN SLTKRKTAVS QLAKQGVKDL EEVTGLLRKL GIKLHVVVNL GLVYKVQHHR
GVIFQFVAFV RRRKRTVLEI IAAGGRYDHL FQEFRGPTSP PVALSAVGAS VALDRICASL
ANMEEPPSVG SCDALVLPVG HTSMSRAIVV VQKLWSCGVS AEIVYDVSQP QEAVLEHSRQ
AGITCVVLVS DKEGSYVKVK CFEKDRQSEK RIPETDLLDH IVQKCRTRSF DDRNGRDMCE
SASLQNPKGS ILATSGLSEP HGSNVPMTIS VNLITPEKVS ASTRRRHETQ IQTRLQNLGS
YLQNKSSNIE VVAVSDPFFS PRFSLS
//
