ID A0A2K6QW90_RHIRO Unreviewed; 550 AA.
AC A0A2K6QW90;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE SubName: Full=Eukaryotic translation initiation factor 2 alpha kinase 2 {ECO:0000313|Ensembl:ENSRROP00000033054.1};
GN Name=EIF2AK2 {ECO:0000313|Ensembl:ENSRROP00000033054.1};
OS Rhinopithecus roxellana (Golden snub-nosed monkey) (Pygathrix roxellana).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Colobinae; Rhinopithecus.
OX NCBI_TaxID=61622 {ECO:0000313|Ensembl:ENSRROP00000033054.1, ECO:0000313|Proteomes:UP000233200};
RN [1] {ECO:0000313|Ensembl:ENSRROP00000033054.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
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DR RefSeq; XP_010371438.1; XM_010373136.1.
DR AlphaFoldDB; A0A2K6QW90; -.
DR STRING; 61622.ENSRROP00000033054; -.
DR Ensembl; ENSRROT00000057490.1; ENSRROP00000033054.1; ENSRROG00000040152.1.
DR GeneID; 104669977; -.
DR KEGG; rro:104669977; -.
DR CTD; 5610; -.
DR GeneTree; ENSGT00940000160736; -.
DR OMA; LIQMEFC; -.
DR OrthoDB; 8734at2759; -.
DR Proteomes; UP000233200; Unplaced.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:Ensembl.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0003725; F:double-stranded RNA binding; IEA:Ensembl.
DR GO; GO:0004694; F:eukaryotic translation initiation factor 2alpha kinase activity; IEA:Ensembl.
DR GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
DR GO; GO:0140374; P:antiviral innate immune response; IEA:Ensembl.
DR GO; GO:0034198; P:cellular response to amino acid starvation; IEA:Ensembl.
DR GO; GO:0030968; P:endoplasmic reticulum unfolded protein response; IEA:Ensembl.
DR GO; GO:0043066; P:negative regulation of apoptotic process; IEA:Ensembl.
DR GO; GO:0033689; P:negative regulation of osteoblast proliferation; IEA:Ensembl.
DR GO; GO:0017148; P:negative regulation of translation; IEA:Ensembl.
DR GO; GO:0045071; P:negative regulation of viral genome replication; IEA:Ensembl.
DR GO; GO:0032722; P:positive regulation of chemokine production; IEA:Ensembl.
DR GO; GO:1901224; P:positive regulation of non-canonical NF-kappaB signal transduction; IEA:Ensembl.
DR GO; GO:0032874; P:positive regulation of stress-activated MAPK cascade; IEA:Ensembl.
DR GO; GO:1902036; P:regulation of hematopoietic stem cell differentiation; IEA:Ensembl.
DR GO; GO:1902033; P:regulation of hematopoietic stem cell proliferation; IEA:Ensembl.
DR GO; GO:1900225; P:regulation of NLRP3 inflammasome complex assembly; IEA:Ensembl.
DR GO; GO:0035455; P:response to interferon-alpha; IEA:Ensembl.
DR GO; GO:0006412; P:translation; IEA:Ensembl.
DR CDD; cd19904; DSRM_EIF2AK2_rpt2; 1.
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; IPR044453; EIF2AK2_DSRM_2.
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:UP000233200};
KW RNA-binding {ECO:0000256|PROSITE-ProRule:PRU00266}.
FT DOMAIN 9..77
FT /note="DRBM"
FT /evidence="ECO:0000259|PROSITE:PS50137"
FT DOMAIN 100..167
FT /note="DRBM"
FT /evidence="ECO:0000259|PROSITE:PS50137"
FT DOMAIN 266..539
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 192..254
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 192..236
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 240..254
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 550 AA; 61722 MW; F9254B40326B94EE CRC64;
MAGDLAPGFF MEQLNKYRQK QGIKLSYQEL PNTGPPHDRR FTFRVISDRR EFPEAEGRSK
KEAKNAAAKL AVEILNKESK AVSPFSLTTT SSPEGLSIGN YIGVVNRIAQ KKRLTVNYEP
CISGVHGPEG FHYKCKMGQK EYSIGTGSTK QEAKQLAAKF AFLEISKETS VKPDSMSSGS
VAATCGSQSN PLVNNSLASE SSSESDVAAD TSEINSNSGS LNNSSLFTNG LRNNQRKAKR
SLAPRFDPPD MKETKYTADT RFGTDFKEIE FISLGGFGQV FKAKHRIDGK TYVIKRVKYN
GEKAEREVKA LAKLDHVNIV HYNGCWGGLD YDPDISAYDP ESPDYDPENI KNSSRLKTKC
LFIQMEFCEK GTLEQWIENR RGEKLDKVLA LELFEQITKG VDYIHSKNII HRDLKPSNIF
LVDTKQIKIG DFGLATSLKN DGKRTRNTGT LRYMSPEQIS SQDYGKEVDL YALGLILAEL
LHVCDTAFET SEFFKDLRDG VISDVFDKRE KTLLEKLLSK KPEDRPNTSE ILSTLTTWKK
SPEKKERHTC
//
