ID   IRLA_DICDI              Reviewed;        1431 AA.
AC   Q559A2; Q86IF7;
DT   10-FEB-2009, integrated into UniProtKB/Swiss-Prot.
DT   24-MAY-2005, sequence version 1.
DT   03-AUG-2022, entry version 107.
DE   RecName: Full=Probable serine/threonine-protein kinase irlA;
DE            EC=2.7.11.1;
DE   AltName: Full=Inositol-requiring protein-like protein kinase A;
GN   Name=irlA; ORFNames=DDB_G0272987;
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=12097910; DOI=10.1038/nature00847;
RA   Gloeckner G., Eichinger L., Szafranski K., Pachebat J.A., Bankier A.T.,
RA   Dear P.H., Lehmann R., Baumgart C., Parra G., Abril J.F., Guigo R.,
RA   Kumpf K., Tunggal B., Cox E.C., Quail M.A., Platzer M., Rosenthal A.,
RA   Noegel A.A.;
RT   "Sequence and analysis of chromosome 2 of Dictyostelium discoideum.";
RL   Nature 418:79-85(2002).
RN   [2]
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; AAFI02000008; EAL71131.1; -; Genomic_DNA.
DR   RefSeq; XP_644914.1; XM_639822.1.
DR   AlphaFoldDB; Q559A2; -.
DR   SMR; Q559A2; -.
DR   STRING; 44689.DDB0231216; -.
DR   PaxDb; Q559A2; -.
DR   EnsemblProtists; EAL71131; EAL71131; DDB_G0272987.
DR   GeneID; 8618593; -.
DR   KEGG; ddi:DDB_G0272987; -.
DR   dictyBase; DDB_G0272987; irlA.
DR   eggNOG; KOG1027; Eukaryota.
DR   HOGENOM; CLU_248487_0_0_1; -.
DR   InParanoid; Q559A2; -.
DR   Reactome; R-DDI-381070; IRE1alpha activates chaperones.
DR   PRO; PR:Q559A2; -.
DR   Proteomes; UP000002195; Chromosome 2.
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; Kinase; Nucleotide-binding; Reference proteome;
KW   Serine/threonine-protein kinase; Transferase.
FT   CHAIN           1..1431
FT                   /note="Probable serine/threonine-protein kinase irlA"
FT                   /id="PRO_0000362016"
FT   DOMAIN          987..1261
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   DOMAIN          1264..1431
FT                   /note="KEN"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00725"
FT   REGION          1..81
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          736..879
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          57..97
FT                   /evidence="ECO:0000255"
FT   COILED          715..759
FT                   /evidence="ECO:0000255"
FT   COILED          860..971
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        25..42
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        47..66
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        67..81
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        752..834
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        840..879
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        1130
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   BINDING         993..1001
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   BINDING         1016
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
SQ   SEQUENCE   1431 AA;  166070 MW;  7CF36204084B8A2F CRC64;
     MTKPIFKSKT KPLGWSKISS KEVINEDEEE EEGGEEGGEE EEIDNNKNSN NSSSNSNNNN
     NDNNNNNGEE RKVEKEEEKE EINHYRNQFE KDLLDMELKA LNRETIDNIL SGLNSYEIFK
     EVNFDFEKLY SIIISEPPPL FDTFFDSVSS FEIFFTDCLI LLCSNFPDGI DTSITRPNFN
     DFYNHFKDRG VINKYISREN IHKALNDKLM TDYFNSGIYL GLLDTLDIAA IRFITIFGKF
     LSYEVVETIS NSLFRYRTDK IEFLSDIIRE LLLCNEKYRT LSKSYDLVQK RLQKEEFTFI
     KVFEDDDPKL FSALYQPPDI IKLITEPEKD SGFWCMIGIF KSKRILDYLI RTEPSKSWFK
     GKESDYFFSI AEMGGKYFNW TLLEPKLIKK EVNQKSLKGV IPPRELNSQQ RNTQFFRVFN
     GVTGFNDIRF VYANPSLAQH AIKFIQKVTE CGLFLNTDVR NVRDSIPNSN SFLFRKFLEV
     NFFYRYEKDN EVYQHQPTEE NSLLYSTSII SRIVEMEVTD LLSVVLKNLT QQGCSLAREA
     VDERSLLSTI HSDKYYNSSI VVLHNYWPIP PKFCDCSTSF ISMANGKLPR TYSGSDGVIP
     YIFFARNHLT LGFLLSIHNN ITDTIDINHW ISVAISGGLY YDKEEIFRKY PLLQKESTLQ
     KYPRPVNILE FQTLLENNEC IEYIARTFIK EIPPHEVPTV KHSDLLILFE ISVMKKRSIR
     SKESLQAELD LIEEEKREKK KQKDKKKNKS NQNQKNNNNQ NNQSNNNKIN SPSSNKLTQN
     VTPPSSPVNI ITSSSTTSSS TSSTTSSTTS STIEPKPPTQ TLPIKTSSPT KPESQKPSTP
     DPLIPKSSKS TTKNNNNNNN NNNNNNNNNN NNNNNNNNKE NREMALEVIN EMEKIEIEES
     LLSTSSLVQP QQQSQQSQQQ QEQQQQQQQQ QQQQQQQQQQ QQQQQQQQQQ QQEKQQEQQE
     QQESIQLNQT LTPIIPDFQI GKFKFSRDEN NIIGRGSNGT LVFRGIWNDR IPVAVKQMQK
     AFNPHISKEI EVLIRLTSNN CSNMIRYIDQ EEDQLFVYLG LTLCEESLQD LMESKRYKEF
     IEKTTTTNIT TTFNNNIIDE NLYEQRILSL FKDVINGINF LHCQDIVHND LNPRNILVHK
     GNFVISDLGL SKMQVETSYS FTNNAPTGQE GYHPIEVLQE KRKTKSVDIF SLGCILFYLL
     TNGQHPFGNN KLLRVANIVY DKPDLEPLKF NAPALDLVRL MISQDEKKRP TIDTILNHPL
     FWSTNEKIKF YESSLNLLKD PNNSQSKHSK LLNYYQNDNS GGVLFLSKPW NQIIDPFLID
     HVENNNNNNN NNNNNKQNSK KLAIVAYQYD QVRDLVRCIR NSLVHHKDIL RSITQQQNLP
     PSSKEFANDC LKSQESVLLY FECKFPDLLF HLYQQFKKSD FNSKDYLNIK F