ID H2S269_TAKRU Unreviewed; 503 AA.
AC H2S269;
DT 21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT 17-JUN-2020, sequence version 3.
DT 27-MAR-2024, entry version 56.
DE RecName: Full=Eukaryotic translation initiation factor 2-alpha kinase 2 {ECO:0008006|Google:ProtNLM};
OS Takifugu rubripes (Japanese pufferfish) (Fugu rubripes).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Eupercaria; Tetraodontiformes; Tetradontoidea; Tetraodontidae; Takifugu.
OX NCBI_TaxID=31033 {ECO:0000313|Ensembl:ENSTRUP00000006490.3, ECO:0000313|Proteomes:UP000005226};
RN [1] {ECO:0000313|Ensembl:ENSTRUP00000006490.3, ECO:0000313|Proteomes:UP000005226}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=21551351;
RA Kai W., Kikuchi K., Tohari S., Chew A.K., Tay A., Fujiwara A., Hosoya S.,
RA Suetake H., Naruse K., Brenner S., Suzuki Y., Venkatesh B.;
RT "Integration of the genetic map and genome assembly of fugu facilitates
RT insights into distinct features of genome evolution in teleosts and
RT mammals.";
RL Genome Biol. Evol. 3:424-442(2011).
RN [2] {ECO:0000313|Ensembl:ENSTRUP00000006490.3}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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DR AlphaFoldDB; H2S269; -.
DR Ensembl; ENSTRUT00000006532.3; ENSTRUP00000006490.3; ENSTRUG00000002791.3.
DR GeneTree; ENSGT00940000160736; -.
DR HOGENOM; CLU_023682_1_0_1; -.
DR Proteomes; UP000005226; Chromosome 4.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004672; F:protein kinase activity; IEA:InterPro.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR Gene3D; 3.30.160.20; -; 2.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR014720; dsRBD_dom.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR PANTHER; PTHR11042; EUKARYOTIC TRANSLATION INITIATION FACTOR 2-ALPHA KINASE EIF2-ALPHA KINASE -RELATED; 1.
DR PANTHER; PTHR11042:SF163; INTERFERON-INDUCED, DOUBLE-STRANDED RNA-ACTIVATED PROTEIN KINASE; 1.
DR Pfam; PF00035; dsrm; 2.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00358; DSRM; 2.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF54768; dsRNA-binding domain-like; 2.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS50137; DS_RBD; 2.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000005226};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW RNA-binding {ECO:0000256|PROSITE-ProRule:PRU00266}.
FT DOMAIN 3..71
FT /note="DRBM"
FT /evidence="ECO:0000259|PROSITE:PS50137"
FT DOMAIN 99..166
FT /note="DRBM"
FT /evidence="ECO:0000259|PROSITE:PS50137"
FT DOMAIN 228..497
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 73..95
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 481..503
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 80..95
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 481..497
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 503 AA; 57792 MW; B5AD886E758704F2 CRC64;
MENYVARLNE YAQENRLSLQ YQDVGCDGPD HLKTFRVRAV IDDQAYPEGL GKNKKEAKKK
AAENAWRALM QEHRDSETQT ENAGQSPSTP SQAPITRTNF VAWLNEYGQK NRVSVKLVES
TRPGLRGAEL CCRFVVGDQE YPDAVGKTKR EAKEEAARLV YNEICGAEEP TCCDVAGDVL
AGASTPKSTI LAPNFLNVRR NSKEENMSNF SDKMRLNEET PSRFTSEFNS IVLLAQGSFG
YVYKARSKLL GKEMAVKIVH CDDFRKALRE VQALSELNHP NIVRYYTCWL EDAGYEGRLR
SAQDSTLKYL YIQMELCSTE TLRKWINKKN RNQNQWRKEE SLSVFTQIVS GVEYVHSRKF
IHRDLKPENI MFSSNKEVKI GDFGLVTAEA DDAADLVKRT VYKGTPRYMA PEQKEKETYD
RKVDIFALGL IYFELLWNFS HEERREVWKN IKTQKTPAAF SGSYPFEDQL IKRMLSMKPE
DRPEAEAVKR ELEHNPSCER TTV
//