ID A0A226DSI5_FOLCA Unreviewed; 1203 AA.
AC A0A226DSI5;
DT 25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT 25-OCT-2017, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE SubName: Full=Interferon-induced, double-stranded RNA-activated protein kinase {ECO:0000313|EMBL:OXA48183.1};
DE Flags: Fragment;
GN ORFNames=Fcan01_17471 {ECO:0000313|EMBL:OXA48183.1};
OS Folsomia candida (Springtail).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Collembola;
OC Entomobryomorpha; Isotomoidea; Isotomidae; Proisotominae; Folsomia.
OX NCBI_TaxID=158441 {ECO:0000313|EMBL:OXA48183.1, ECO:0000313|Proteomes:UP000198287};
RN [1] {ECO:0000313|EMBL:OXA48183.1, ECO:0000313|Proteomes:UP000198287}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VU population {ECO:0000313|EMBL:OXA48183.1,
RC ECO:0000313|Proteomes:UP000198287};
RC TISSUE=Whole body {ECO:0000313|EMBL:OXA48183.1};
RA Faddeeva A., Derks M.F., Anvar Y., Smit S., Van Straalen N., Roelofs D.;
RT "The genome of Folsomia candida.";
RL Submitted (DEC-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OXA48183.1}.
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; LNIX01000012; OXA48183.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A226DSI5; -.
DR STRING; 158441.A0A226DSI5; -.
DR OMA; YSNQRRW; -.
DR Proteomes; UP000198287; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004672; F:protein kinase activity; IEA:InterPro.
DR GO; GO:0017148; P:negative regulation of translation; IEA:UniProtKB-KW.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR Gene3D; 1.25.40.10; Tetratricopeptide repeat domain; 2.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR InterPro; IPR019734; TPR_repeat.
DR PANTHER; PTHR11042; EUKARYOTIC TRANSLATION INITIATION FACTOR 2-ALPHA KINASE EIF2-ALPHA KINASE -RELATED; 1.
DR Pfam; PF00069; Pkinase; 1.
DR Pfam; PF13374; TPR_10; 2.
DR Pfam; PF13181; TPR_8; 1.
DR SMART; SM00220; S_TKc; 1.
DR SMART; SM00028; TPR; 5.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR SUPFAM; SSF48452; TPR-like; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|PROSITE-ProRule:PRU10141};
KW Kinase {ECO:0000313|EMBL:OXA48183.1};
KW Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU10141};
KW Reference proteome {ECO:0000313|Proteomes:UP000198287};
KW Transferase {ECO:0000313|EMBL:OXA48183.1}.
FT DOMAIN 37..375
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT BINDING 66
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
FT NON_TER 1203
FT /evidence="ECO:0000313|EMBL:OXA48183.1"
SQ SEQUENCE 1203 AA; 137149 MW; 844EFACDF34AF462 CRC64;
MLKSSPYSIA TAAGNTLYPK FSTDLKPPWS SSTGFELVES EALGKGAFGE VFKARHRLDL
IVYAIKQIDI FPALLKFRGQ STGDDSLDEL LAKLKREVVL HSKINSSFVV RYHSHWIEGP
GSDQFKINEI ENLVSLVLKN VGTATSGEGS NSDSVQRTFL YIQTEFCNQT SLDKFLISAT
ESEKLSEFPR IIYQTAKGLS AIHAQGIIHR DLKPDNIYAT KKAGRDLNIW KIGDFGLSIK
FGPSPPNLFD ALEFQIDSEG SSLESFKGAD TFRSPEMYNQ HPYSSKTDIY SLALIFICVL
FKFPSVKKRR AYFIDLQLGH CTPESVHLQE TMDNNPETKI KYCSLIEKML SHKPDERPDA
LEIYNQTSTP LHFYKRGNEL LDPSRIYGRE ADLTKLDTLF QKNSNFLIIT NSEKYSELSL
GKTALVHKFL ATSPRLKNYS TIWLESSTED LFLQQLFNLC DELDIPTRQP GAINFTRAIE
EILKDLCNFL TGKNTVIVFD DLFSSENIAI SDTIAKLIQN VANIKEIFFI ITTTHVNPMP
KSLSIAPENN LIPLKVLNIQ DGLLLLNSEL GLFPESRQSY ATLLNVLHSN PAALTNAIKV
ISGWQTTRGI LIPFGVILCS RKVLTLRKGL TNLKKIMEPL GYSTNKYVMS TLTTFVQSNF
HVQKFCNENE LSSTILSFLY CIYPEKVAVD LKLFLHLLPT VDIQRTLELM QDFNLIKVEN
NDISLVKNAY LTTNLPDMET FLDKTLATFQ SLMPTREESW VPIVSTIIDQ AQSYPDLMKK
YVHFILDMSN VFRFYKNFKQ DISIRLNAFK KCFGPEHEHT LSMENIYISG FFEDGKFQKA
LNKWKKLGDI TGRRLDQNHW LNIDVKHAVA LLHHNLGMFL EAREEYEKLL ELDIKNNSTR
INVKANYALT LTELRDDEKA LSLLNEVLAF YRTTDQFGDE SEGVITAKCR IAAIYYLQDR
FSEALPIFKE VLDVRTKMFG EEYGLTLDAK GWVVKTISKI NGKNINQNLT EAITQVFRHV
HSVREKAFGK RHPETVGNLR NLAVHLLEHG NNKDHIVEAR DIFGLVLSLN SELFGESHPI
TLDTKTFLAQ VLEKREDFNG ALKIYEEILK SHETIFGTEH KTTVKTKCSV GRVWYELKQF
GKAKSIFEQI YSRNKAFERE TKETLYARLN FAMSLNKCGA REKAMQVFGE ILKLEGEFEK
DDK
//
