ID H9ZBA6_MACMU Unreviewed; 554 AA.
AC H9ZBA6;
DT 13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT 13-JUN-2012, sequence version 1.
DT 27-MAR-2024, entry version 42.
DE SubName: Full=Interferon-induced, double-stranded RNA-activated protein kinase isoform a {ECO:0000313|EMBL:AFH33222.1};
GN Name=EIF2AK2 {ECO:0000313|EMBL:AFH33222.1};
OS Macaca mulatta (Rhesus macaque).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Macaca.
OX NCBI_TaxID=9544 {ECO:0000313|EMBL:AFH33222.1};
RN [1] {ECO:0000313|EMBL:AFH33222.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Thymus {ECO:0000313|EMBL:AFH33222.1};
RX PubMed=25319552; DOI=10.1186/1745-6150-9-20;
RA Zimin A.V., Cornish A.S., Maudhoo M.D., Gibbs R.M., Zhang X., Pandey S.,
RA Meehan D.T., Wipfler K., Bosinger S.E., Johnson Z.P., Tharp G.K.,
RA Marcais G., Roberts M., Ferguson B., Fox H.S., Treangen T., Salzberg S.L.,
RA Yorke J.A., Norgren R.B.Jr.;
RT "A new rhesus macaque assembly and annotation for next-generation
RT sequencing analyses.";
RL Biol. Direct 9:20-20(2014).
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DR EMBL; JU476418; AFH33222.1; -; mRNA.
DR AlphaFoldDB; H9ZBA6; -.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0003725; F:double-stranded RNA binding; IEA:InterPro.
DR GO; GO:0004672; F:protein kinase activity; IEA:InterPro.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
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 2: Evidence at transcript level;
KW Kinase {ECO:0000313|EMBL:AFH33222.1};
KW RNA-binding {ECO:0000256|PROSITE-ProRule:PRU00266};
KW Transferase {ECO:0000313|EMBL:AFH33222.1}.
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..544
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 193..215
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 554 AA; 62122 MW; 55DDA95009DB2B2D CRC64;
MAGHLVPGFY MEELNKYRQK QGISLSYQEL PNTGPPHDRR FTFQVVTDRR TFPEAEGRSK
KEAKNAAAKL AVDILNKESE AVSPFSLTTT SSSEGLSIGN YIGVVNRIAQ KKRLTVNYEQ
CTSGVHGPEG FHYKCKIGDK EYGIGTGSSK QEAKQLAAKL ALLEISEETS VKPDSMSSGS
FAATCDSQSN PLVNNSLASE SSAESDVSAD TSEINSKSGS LHISSLFTNG LRNNQRKAKR
SLAPTFDPPD MKGPKYTEDA RFSTDFKEIE FISVGGFGQV FKAKHRIDGK TYVIKRVKYN
SKKAEREVKA LAKLDHVNIV HYNGCWDGLD YDPEISAYEP ESTDFDPENQ KNSLRNFIPR
SKTKCLFIQM EFCEDGTLED WLDRRKGKEL DKVLALELFE QITKGLDYIH SKNIIHRDLK
PSNIFLVDTK QIKIGDFGLA TSLKNDVKRT SNTGTLRYMS PEQISSQDYG KEVDLYALGL
ILAELLYVCD TASETLQLFR DLRGGTISDV YDKREKTLLK KLLSKKPEDR PNTSEILSTL
TTWKKSPEKK RHTC
//
