ID Q7T2M9_CARAU Unreviewed; 513 AA. AC Q7T2M9; DT 01-OCT-2003, integrated into UniProtKB/TrEMBL. DT 01-OCT-2003, sequence version 1. DT 27-MAR-2024, entry version 121. DE SubName: Full=Interferon-inducible and double-stranded-dependent eIF-2kinase {ECO:0000313|EMBL:AAP49830.1}; OS Carassius auratus (Goldfish). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes; OC Cyprinidae; Cyprininae; Carassius. OX NCBI_TaxID=7957 {ECO:0000313|EMBL:AAP49830.1}; RN [1] {ECO:0000313|EMBL:AAP49830.1} RP NUCLEOTIDE SEQUENCE. RC TISSUE=Blastula {ECO:0000313|EMBL:AAP49830.1}; RA Zhang Y.-B., Zhang Q.-Y., Xu D.-Q., Hu C.-Y., Gui J.-F.; RT "Identification of antiviral-relevant genes in the cultured fish cells RT induced by UV-inactivated virus."; RL Chin. Sci. Bull. 48:581-588(2003). RN [2] {ECO:0000313|EMBL:AAP49830.1} RP NUCLEOTIDE SEQUENCE. RC TISSUE=Blastula {ECO:0000313|EMBL:AAP49830.1}; RA Zhang Y., Huang G., Hu C., Gui J.; RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases. RN [3] {ECO:0000313|EMBL:AAP49830.1} RP NUCLEOTIDE SEQUENCE. RC TISSUE=Blastula {ECO:0000313|EMBL:AAP49830.1}; RX PubMed=15312662; DOI=10.1016/j.fsi.2004.04.009; RA Hu C.Y., Zhang Y.B., Huang G.P., Zhang Q.Y., Gui J.F.; RT "Molecular cloning and characterisation of a fish PKR-like gene from RT cultured CAB cells induced by UV-inactivated virus."; RL Fish Shellfish Immunol. 17:353-366(2004). RN [4] {ECO:0007829|PDB:4KMF} RP X-RAY CRYSTALLOGRAPHY (1.70 ANGSTROMS) OF 2-63. RX PubMed=24682817; DOI=10.1093/nar/gku189; RA Kim D., Hur J., Park K., Bae S., Shin D., Ha S.C., Hwang H.Y., Hohng S., RA Lee J.H., Lee S., Kim Y.G., Kim K.K.; RT "Distinct Z-DNA binding mode of a PKR-like protein kinase containing a Z- RT DNA binding domain (PKZ)."; RL Nucleic Acids Res. 42:5937-5948(2014). RN [5] {ECO:0007829|PDB:2RVC} RP STRUCTURE BY NMR OF 1-64. RX PubMed=26792893; DOI=10.1093/nar/gkw025; RA Lee A.R., Park C.J., Cheong H.K., Ryu K.S., Park J.W., Kwon M.Y., Lee J., RA Kim K.K., Choi B.S., Lee J.H.; RT "Solution structure of the Z-DNA binding domain of PKR-like protein kinase RT from Carassius auratus and quantitative analyses of the intermediate RT complex during B-Z transition."; RL Nucleic Acids Res. 44:2936-2948(2016). CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AY293929; AAP49830.1; -; mRNA. DR PDB; 2RVC; NMR; -; A=1-64. DR PDB; 4KMF; X-ray; 1.70 A; A=2-63. DR PDBsum; 2RVC; -. DR PDBsum; 4KMF; -. DR AlphaFoldDB; Q7T2M9; -. DR BMRB; Q7T2M9; -. DR SMR; Q7T2M9; -. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule. DR GO; GO:0003726; F:double-stranded RNA adenosine deaminase activity; IEA:InterPro. DR GO; GO:0004672; F:protein kinase activity; IEA:InterPro. DR GO; GO:0003723; F:RNA binding; IEA:InterPro. DR GO; GO:0048856; P:anatomical structure development; IEA:UniProt. DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW. DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1. DR Gene3D; 1.10.10.10; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 2. DR InterPro; IPR011009; Kinase-like_dom_sf. DR InterPro; IPR000719; Prot_kinase_dom. DR InterPro; IPR017441; Protein_kinase_ATP_BS. DR InterPro; IPR008271; Ser/Thr_kinase_AS. DR InterPro; IPR036388; WH-like_DNA-bd_sf. DR InterPro; IPR036390; WH_DNA-bd_sf. DR InterPro; IPR042371; Z_dom. 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; PF00069; Pkinase; 2. DR Pfam; PF02295; z-alpha; 2. DR SMART; SM00220; S_TKc; 1. DR SMART; SM00550; Zalpha; 2. DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1. DR SUPFAM; SSF46785; Winged helix' DNA-binding domain; 2. DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1. DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1. DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1. DR PROSITE; PS50139; Z_BINDING; 1. PE 1: Evidence at protein level; KW 3D-structure {ECO:0007829|PDB:2RVC, ECO:0007829|PDB:4KMF}; KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE- KW ProRule:PRU10141}; Kinase {ECO:0000313|EMBL:AAP49830.1}; KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE- KW ProRule:PRU10141}; RNA-binding {ECO:0000256|ARBA:ARBA00022884}; KW Transferase {ECO:0000313|EMBL:AAP49830.1}. FT DOMAIN 1..64 FT /note="Z-binding" FT /evidence="ECO:0000259|PROSITE:PS50139" FT DOMAIN 169..501 FT /note="Protein kinase" FT /evidence="ECO:0000259|PROSITE:PS50011" FT REGION 236..255 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 261..301 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 236..254 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 263..280 FT /note="Acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 283..297 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT BINDING 199 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141" SQ SEQUENCE 513 AA; 57954 MW; 8DA87682788D9CE7 CRC64; MSAETQMERK IIDFLRQNGK SIALTIAKEI GLDKSTVNRH LYNLQRSNQV FNSNEKPPVW DLMEKTNGIK QTVKTPEQKS LTTTAETCEE KHVRDLLKSG GLKACQIAKD LGQPRKAVNK QLYSMMQTGK VKKCEISSLW LLEGEESNES HSQESDHRLG SVAGLSQSFD VITKLGEGGF GCVFKVKHKF DGKIYAVKKV VLTGEADSEV KALARLDHPN IVRYITCWPD SESCTSNQDR NQVSNTSGSS SCGVTFDRAG CEERNDEDDE DDDDDDDVSD VTSRMESLGS TAELASAAGP SGNLDPLNHS RMYLFIQMEF CEGGTLTTWI RARNRMNKQR IAVEIHKIFY EIVSGVEYIH SNSLIHRDLK PDNILFGMDG KVKIGDFGLV AAQTNHSGGP IERTKRRGTL QYMSPEQENK RNYDEKTDIF PLGLIWFEML WKLSTGMERA ELLKDLRNQR FPEGFCDSYP TENKFIEKML SFAPEDRPPA KDIKEKLEKF FSLDEDLLSQ KTI //