IRLE_DICDI
ID IRLE_DICDI Reviewed; 1350 AA.
AC Q54IE8;
DT 10-FEB-2009, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 03-AUG-2022, entry version 105.
DE RecName: Full=Probable serine/threonine-protein kinase irlE;
DE EC=2.7.11.1;
DE AltName: Full=Inositol-requiring protein-like protein kinase E;
GN Name=irlE; ORFNames=DDB_G0288803;
OS Dictyostelium discoideum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=44689;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4;
RX PubMed=15875012; DOI=10.1038/nature03481;
RA Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT "The genome of the social amoeba Dictyostelium discoideum.";
RL Nature 435:43-57(2005).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
CC [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
CC threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
CC Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC EC=2.7.11.1;
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane
CC protein {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. {ECO:0000255|PROSITE-ProRule:PRU00159}.
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; AAFI02000125; EAL63023.1; -; Genomic_DNA.
DR RefSeq; XP_636529.1; XM_631437.1.
DR AlphaFoldDB; Q54IE8; -.
DR SMR; Q54IE8; -.
DR STRING; 44689.DDB0229380; -.
DR PaxDb; Q54IE8; -.
DR EnsemblProtists; EAL63023; EAL63023; DDB_G0288803.
DR GeneID; 8626814; -.
DR KEGG; ddi:DDB_G0288803; -.
DR dictyBase; DDB_G0288803; irlE.
DR eggNOG; KOG1027; Eukaryota.
DR HOGENOM; CLU_257765_0_0_1; -.
DR InParanoid; Q54IE8; -.
DR Reactome; R-DDI-381070; IRE1alpha activates chaperones.
DR PRO; PR:Q54IE8; -.
DR Proteomes; UP000002195; Chromosome 5.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:1990604; C:IRE1-TRAF2-ASK1 complex; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004521; F:endoribonuclease activity; IBA:GO_Central.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IBA:GO_Central.
DR GO; GO:0051082; F:unfolded protein binding; IBA:GO_Central.
DR GO; GO:0036498; P:IRE1-mediated unfolded protein response; IBA:GO_Central.
DR GO; GO:0006397; P:mRNA processing; IEA:InterPro.
DR GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR Gene3D; 1.20.1440.180; -; 1.
DR InterPro; IPR045133; IRE1/2-like.
DR InterPro; IPR010513; KEN_dom.
DR InterPro; IPR038357; KEN_sf.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR PANTHER; PTHR13954; PTHR13954; 1.
DR Pfam; PF00069; Pkinase; 1.
DR Pfam; PF06479; Ribonuc_2-5A; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS51392; KEN; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PE 3: Inferred from homology;
KW ATP-binding; Coiled coil; Glycoprotein; Kinase; Membrane;
KW Nucleotide-binding; Reference proteome; Serine/threonine-protein kinase;
KW Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..1350
FT /note="Probable serine/threonine-protein kinase irlE"
FT /id="PRO_0000362020"
FT TRANSMEM 149..169
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 903..1166
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT DOMAIN 1169..1346
FT /note="KEN"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00725"
FT REGION 761..795
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 807..864
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 731..802
FT /evidence="ECO:0000255"
FT COMPBIAS 771..795
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 812..864
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 1034
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 909..917
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 932
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT CARBOHYD 37
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 1350 AA; 156241 MW; 76388FB2FAC70D91 CRC64;
MGKKKIDINT REDLFLSYYK EIEKNKFDLL KICSDKNFSK SNFLKAVHCL FSLSYFCKIK
DENEEEEGKE EEINDYKVKK STTGNYYRNS EGKLFKKSNE KDQIDDVSIF YKRLPTIQDF
KDTYDKYENC LNSVYYIIRK IKLLHLEYFW EILASCYGTI SFIKFFNIFS NEIFSPSENG
DSVFIMVGKF FRRKVRAETH YDLIFLKIIL ANASIPMILK LGVKDIGRFT EKEDIIVSYY
RNFSIIHSLR FDNVKEFALV YKTLKNNYPS KKKKKITLFE ENGKINVKTS KKDLMLFEFV
CKFDCVKIFK KYFLPKPQII NNNDNNEMLE CISSGSYSGF DEKSKRKIRI FFSICCRQIS
PKILKCIVDY VKDDIGFLDL QNRQDIYIGD SAPEKVLFLN CFFGNHKEQR VIDFFNLLTS
KSIIICNTIK EKPELYDYRY ITLSTVDSTF YFSDSHKGAD FGVYTDEINV IINNDDIDYD
YIGDDDNDEE IEETKDYGSS SSDIDDFYNV FEPKASMIPN ILDSCSLEIL KAYIQNITGN
GLFKISPSLF LAHDVTRLVR NPKPKTETVV KILEFINTIS RLSELSTNGV PFTFLTNRFE
IVTSIIMSLH DERSISNSVE PVQWLRALAP FVSNDEMKLI IYKVRTLYNY EPHSNGEIKY
TELVRLFDVQ YLLTKGKFSL SQFNGFETSI FLNPKLLDGT INSNILNSMI IKDKEKLDLK
ELFFKEKPLS EAELKEKFEI ATKNEKELLD QLKKENDAEK LKKKNKLKKQ KNQQQQQQAK
QQAQQQKQQH QQNIQQNYEN QHIEDQRKFN QQTKGRPISP SSIQNQNLNP TLLQNQNQTS
NPTPNLESTK KATPTTTTTT TTNSNTSAII NEIKNQDLNQ QQNITENINE IYDVSIGKFK
FNKKESNILG RGSNGTLVFK GIWNNRIPVA IKQMQKMFNP LISKEIEILI GLTNKNLNLV
GYIDQEEDEN CVYLGLTLCD GSLQSLYDQS KLNEFINQNN NQNNNNNNNR VLDLIIGMIN
GVIFLHDQNI VHNDLNPRNI LVKDNRLIIS DLGLSKMNVS STYNFSTNAI PTGQDGYHPV
EVLLEKRKTK SVDVFSLGCL IYFIMTNGAH PFGDKFSRLR YITKSKYNLS QLSNLNLVAT
HLIELMISYD ESKRPTLSSV LKHPLFWDSL KKIKFLESSL RLLGDHDFKK FNINKILISC
NSNSSSSNSI CNSSNSSSSS SSSISSSSCK ISSSSCYCVP LPWNQSLDYQ LVDSLSNQIE
KKVASYKFDQ LHDLIRFIRN TLQHYNQIYR DLKQILPNSD ILESLKSQQS ALNYFESKFP
TLIIFLFNHF SAIPEIKNSI HFSNDTCSIF
