IRLC_DICDI
ID IRLC_DICDI Reviewed; 1444 AA.
AC Q55DJ8;
DT 10-FEB-2009, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 03-AUG-2022, entry version 102.
DE RecName: Full=Probable serine/threonine-protein kinase irlC;
DE EC=2.7.11.1;
DE AltName: Full=Inositol-requiring protein-like protein kinase C;
GN Name=irlC; ORFNames=DDB_G0270894;
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 -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. {ECO:0000255|PROSITE-ProRule:PRU00159}.
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DR EMBL; AAFI02000005; EAL72797.1; -; Genomic_DNA.
DR RefSeq; XP_646133.1; XM_641041.1.
DR AlphaFoldDB; Q55DJ8; -.
DR SMR; Q55DJ8; -.
DR STRING; 44689.DDB0231222; -.
DR PaxDb; Q55DJ8; -.
DR EnsemblProtists; EAL72797; EAL72797; DDB_G0270894.
DR GeneID; 8617083; -.
DR KEGG; ddi:DDB_G0270894; -.
DR dictyBase; DDB_G0270894; irlC.
DR eggNOG; KOG1027; Eukaryota.
DR HOGENOM; CLU_248487_0_0_1; -.
DR InParanoid; Q55DJ8; -.
DR OMA; QNINHEE; -.
DR Reactome; R-DDI-381070; IRE1alpha activates chaperones.
DR PRO; PR:Q55DJ8; -.
DR Proteomes; UP000002195; Chromosome 1.
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:0008270; F:zinc ion binding; IEA:InterPro.
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 InterPro; IPR007527; Znf_SWIM.
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.
DR PROSITE; PS50966; ZF_SWIM; 1.
PE 3: Inferred from homology;
KW ATP-binding; Coiled coil; Kinase; Metal-binding; Nucleotide-binding;
KW Reference proteome; Serine/threonine-protein kinase; Transferase; Zinc;
KW Zinc-finger.
FT CHAIN 1..1444
FT /note="Probable serine/threonine-protein kinase irlC"
FT /id="PRO_0000362018"
FT DOMAIN 981..1246
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT DOMAIN 1279..1444
FT /note="KEN"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00725"
FT ZN_FING 495..529
FT /note="SWIM-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00325"
FT REGION 335..370
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 584..619
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 864..938
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 593..620
FT /evidence="ECO:0000255"
FT COILED 847..879
FT /evidence="ECO:0000255"
FT COMPBIAS 584..613
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 876..934
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 1116
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 987..995
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 1010
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
SQ SEQUENCE 1444 AA; 167425 MW; D37E930910AF1CAC CRC64;
MKSNYSTYLY KMSELERIVN GGDVSSIFIE QDDVLGEIKN FNYDLYTKYD SLVLKDPQTQ
NNSPKPPSLE IFILVNLIAL CGRINDKFPN LDKFLTHYKY ATNIFNLLSE NIINSIEKFK
ETLSKDLPSF QLSVIANSSI VKKDNSIIKF LSCFGSFMKL ESIEYFGSVF NSLIGEEDQF
SLDLLQVLID SSNEYKKFLQ ILEFNQLQKY YDDGHLCLFH SIKFDNLNEF KLLFNDSTWC
QQQQQQQQIN PQIFWFILCK YNSSKIAHYL LNDYQINKKS LKQKNPLEIS PVTLLEIAFL
CFSDKIAIVL FSQFNYHELL PKKSKMKHLI KSTSTLINNN NNNNNNNNNN NNNNNNNNNN
NNNNNNNNSK NIGLTQYTVL EGYFLINIRT RSRIAPFIEV LTMNGIHLTN DIIHTRIKSM
SSDSIFRIFT EQYQQQQQNP LNNNQKQIQF NENFTRQQKI DFDNCPNEID TFILDKTQCN
LITLSQEFSI KVRAFTFYLS FGEIFTCSCE DYKREFSCKH MFFILLNYYH VPRNSYLIYQ
RQFTEIERYS IIMNIDLSKI NSRIYGTPNF NTFFKIKSSP SSTTSPFQSI NNNNNNNLNN
NNNNNLNNNN NNENENKFKE DGDDEILQNL NRLNYILLRD FEFGPNDITT KLRETHINLF
DRLLLIEDNL EALDKILKNF TQKGCTLSRD LVGDRNLLVL VAILDSTSKE KLSLLNKYWP
LPEKTKKFAI PLIFFAISEE CLKMFIQISP NLVKSTLNLH DWISILTEFA LINETFLDHY
PLLSAWYSDA RSVETSLFRL FTCMDKIDCI NYLIQTYLLP IPTFKNTLNN FETCYFFETY
FLENSSIKAE QYLLEQELLE KKKQKEKKKQ KQKQSKSKII NNPLSSSSSS SSSPSTSNTT
ITSTTPTTTT TTTTTTTPTT TTTTTTTSSP KQKPITPIKK EIEKEFEKIE LTTPPPPLAT
TKQQQINENY DISIGKFKFN RKEENVLGRG SNGTLVFKGI WNNRIPVAIK QMQKMFNPLI
SKEIEVLITL TNKNCYNIVR YIDQEEDESC VYLGLTLCDG SLQNLVEKGD NNLTLTQFLG
YDINSSSKNN SRLLELIKDI VYGIQFLHQQ GIVHNDLNPR NILIKDDRFI ISDLGLSKME
VTSSYSFTMH APTGQEGFHP AEVLLEKRKT KSVDIFSMGC ILFYLMTGGQ HPFGDKFYRI
VNILTDKPIL EPLKHNLVAC DLISQMISKN ESDRPTIEKI LLHPFFWNHE KKVKFIDASL
NLFKDSNGLF TSKLNKLINY QEINLKNNID SSSSNNNNNI NSNVINNNNN NNNGMATNIP
FLSKPWNQLI DQTLIEHIIN KQNQLNGVGN NKKVIIYSFD QVKDLVRCIR NTIQHHKEIQ
RLVRQSPSSN GDNKQEVLDC LESQELVLSY FEEKVPDLLL FLYQKFKKHL DSKSLIYFND
LIIK
