IRLD_DICDI
ID IRLD_DICDI Reviewed; 1505 AA.
AC Q55DJ9;
DT 10-FEB-2009, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 03-AUG-2022, entry version 103.
DE RecName: Full=Probable serine/threonine-protein kinase irlD;
DE EC=2.7.11.1;
DE AltName: Full=Inositol-requiring protein-like protein kinase D;
GN Name=irlD; ORFNames=DDB_G0269632;
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; EAL72166.1; -; Genomic_DNA.
DR RefSeq; XP_646132.1; XM_641040.1.
DR AlphaFoldDB; Q55DJ9; -.
DR SMR; Q55DJ9; -.
DR STRING; 44689.DDB0231221; -.
DR PaxDb; Q55DJ9; -.
DR PRIDE; Q55DJ9; -.
DR EnsemblProtists; EAL72166; EAL72166; DDB_G0269632.
DR GeneID; 8617082; -.
DR KEGG; ddi:DDB_G0269632; -.
DR dictyBase; DDB_G0269632; irlD.
DR eggNOG; KOG1027; Eukaryota.
DR HOGENOM; CLU_248487_0_0_1; -.
DR InParanoid; Q55DJ9; -.
DR OMA; DTHESIY; -.
DR PhylomeDB; Q55DJ9; -.
DR Reactome; R-DDI-381070; IRE1alpha activates chaperones.
DR PRO; PR:Q55DJ9; -.
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: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 SMART; SM00220; S_TKc; 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..1505
FT /note="Probable serine/threonine-protein kinase irlD"
FT /id="PRO_0000362019"
FT DOMAIN 1054..1324
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT DOMAIN 1327..1505
FT /note="KEN"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00725"
FT REGION 1..30
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 121..211
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 548..571
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 862..1013
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 846..892
FT /evidence="ECO:0000255"
FT COMPBIAS 1..17
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 126..140
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 141..211
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 862..886
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 887..922
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 923..971
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 972..993
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 994..1008
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 1194
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 1060..1068
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 1083
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
SQ SEQUENCE 1505 AA; 172514 MW; FF87B1A163F7AD75 CRC64;
MGPKKGKRSH SKNHHHHNNG NNNNNNNSGG GSSSDILYTY SQDTRILLFK VILTQNEEII
CMVIQIAYGL PGLPKISDIS RDLGILILKL PNRTIRELEL FLESKNIYFR EDQHINYLNE
IPQPTTTTTS PPPPPPPSSI STTTTTTTAT AIEIESSSGL TSNITDSTEI QLDSTTTDTK
TTSTTSTTTN NSSDSNNNNN NNNNNNSNNI LNFPFNCQNK SKQKRPISKE ESFNKMVQYN
FDLGKIFDEF TREVLLDDLK NDLKIDNIPI DNISISPTPI ISPVFQEYDL FLMDSFIILC
GQLDNVKLTL EEFKDYYKKY KLLNQYIEDF KDNLINDFLV TVEILASWYI PQKDYSIVKF
INCFGEMLDS TIIESFSYIF NKTIKKEDDW SISFIQAALG SNEEFKRQVM CLNDELIQDR
YDQSLYSIMH PIKFDNVREF ILIYSRDENY FEPQEFWYLI CKYDAIAITQ HIINNNIAEE
DLSKRSGKTY NSNLSENPLE INPLSLLEIC SANFSHKIAS ILFQFYDFKD SMPTRFSLRG
VFKPTTTTTT TTTTTTTTTT TIDKDEKDKE NNNNNVISQQ FQYFRVLDVN CYFNDVIKKR
APIFIDLMTQ SNIYLNTEVG EGSDENVDTH ESIYSFQNST EYLAINSNSI HRLKRSSISL
LSKVLEFNDR DTLISLLKNL TQGGCTLCKD LIDEKQLLIT ISRPQYHQSI QILHQNGYTI
IPKYQLRDPY IFFAGSKQIL QYLLEIHTNS LSETIDIRHW IQAIMSAGQY SSETEFFQYY
PKIQELSLRD KYSRTLNILE LQYILGHIEG IEFLLEKYLD FTKPYHLDNQ ELLEIFDVTF
VQKKDIRTEE SLKAEKDLLE QEENEKKRLK EKRKKEEKEK KKQQNLKQKS LITNNTTTTT
TTTPIPITVP IPTQTQTPTQ TPTQTPIPTP IPTTPIPTTP IPIPIQLTPT TPKTPKTPKT
PKTPTTPKTP ITPKTPKNST LDKQTISTPK TPPPLSVNTT PITPSPPPQT IATTITTTTT
TPKTTKTTTT SKIPTLIIEL NKYDISIGKF KFSRKDEFII GRGSNGTLVF KGIWNDRIPV
AIKQMHKAFN PLISKEIEVL ITLTNKNCNN IVRYIDQEED DMFVYLGLTL CNGSLQNLVE
KDLEINLIST SNNENNNNNK LKNFIGSELR LLELIKDIVY GIQFLHQQGI VHNDLNPRNI
LIKDDRFIIS DLGLSKMEVT SSYSFTMHAP TGQEGFHPAE VLLEKRKTKS VDIFSMGCIL
FYLMTGGQHP FGDKFFRMAN ILTDKPILEP LKHNLVACDL ISQMISKNES DRPTTENILL
HPFFWNHEKK VKFIDASLNL FKDSNGLFTS KLNKLINQFQ DTDGVNTTST PFLSKPWNQL
IDPTLIEHIT NKQNQLSGGS SIGNNNNNSL TLSGKKFYFY DYSQVKDLVR CIRNTIQHHK
EIQRLISQSP SSSNKQEVLD CLESQELVLS YFEEKVPDLL LFLYQKFKKH LDSKSLIYFN
DLIIK
