IRLB_DICDI
ID IRLB_DICDI Reviewed; 1448 AA.
AC Q557G1;
DT 10-FEB-2009, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 03-AUG-2022, entry version 109.
DE RecName: Full=Probable serine/threonine-protein kinase irlB;
DE EC=2.7.11.1;
DE AltName: Full=Inositol-requiring protein-like protein kinase B;
GN Name=irlB-1; ORFNames=DDB_G0273333;
GN and
GN Name=irlB-2; ORFNames=DDB_G0273857;
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}.
CC -!- CAUTION: The gene for this protein is duplicated in strains AX3 and
CC AX4. These strains contain a duplication of a segment of 750 kb of
CC chromosome 2 compared to the corresponding sequence in strain AX2.
CC {ECO:0000305}.
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; AAFI02000011; EAL70619.1; -; Genomic_DNA.
DR EMBL; AAFI02000009; EAL70884.1; -; Genomic_DNA.
DR RefSeq; XP_644545.1; XM_639453.1.
DR RefSeq; XP_644706.1; XM_639614.1.
DR AlphaFoldDB; Q557G1; -.
DR SMR; Q557G1; -.
DR STRING; 44689.DDB0220009; -.
DR PaxDb; Q557G1; -.
DR PRIDE; Q557G1; -.
DR EnsemblProtists; EAL70619; EAL70619; DDB_G0273857.
DR EnsemblProtists; EAL70884; EAL70884; DDB_G0273333.
DR GeneID; 8618805; -.
DR GeneID; 8619171; -.
DR KEGG; ddi:DDB_G0273333; -.
DR KEGG; ddi:DDB_G0273857; -.
DR dictyBase; DDB_G0273333; irlB-1.
DR dictyBase; DDB_G0273857; irlB-2.
DR eggNOG; KOG1027; Eukaryota.
DR HOGENOM; CLU_251496_0_0_1; -.
DR InParanoid; Q557G1; -.
DR Reactome; R-DDI-381070; IRE1alpha activates chaperones.
DR PRO; PR:Q557G1; -.
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..1448
FT /note="Probable serine/threonine-protein kinase irlB"
FT /id="PRO_0000362017"
FT DOMAIN 1027..1293
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT DOMAIN 1296..1448
FT /note="KEN"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00725"
FT REGION 412..446
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 975..1008
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 666..817
FT /evidence="ECO:0000255"
FT COILED 887..921
FT /evidence="ECO:0000255"
FT COILED 974..1016
FT /evidence="ECO:0000255"
FT ACT_SITE 1151
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 1033..1041
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 1056
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
SQ SEQUENCE 1448 AA; 169401 MW; BB3B99A5E785ED2B CRC64;
MNSLLNNLII DYEYDLIKVH HHIQKNIFIF PFKKQHYHST VLECLINLCS KLKYDENENL
NSLDQFKIIF YNESKFLNKN LKEYLEILKN SKEINKHVIC DYFEKDNNGS EEKNQNSSIV
FNFLNCFKDY LSMDIIEFIV RGISFQVRSY CNLIKPIEQW KQKTYQQRYQ QFKKALHLNN
EVYKRIVCNG VWKSEKLDYI YRYKSDQLSL VGIIESDCSD LFISTLLIDS NSYEQLENVW
RLICNFDSFS IASKFLIEFF KLDKVNNKLN FSIHPSSDAN ENYKRTKTST NSNLSIDLVR
LLEFTTTNFS INVAKLLISK FPTFITSIPS RNSLWGIESR SSLNPIENHF RILNCSFDFN
NHQIPIDKQK DYINLFTKNL IHFNTEINEI EDLILKERYH ISIRSINNNN HDDDDYDDYD
DDDDHHSGCN NNNNNNNDGD HNEDENSIKE ESLIEFSNYK VDSMISRLLK YNAPSTTIIA
LLSNLVCNHM GVSQRILILS TLIEEIQMIE SLLVQNDSFK TFMLCESMVS TPNRWSKQSI
PLVFFAYIGS DILNLKERPM FYKFFDLNPR LLLSIIPVPL IFKTFLSCSD IIRNNFEDDL
INFEDDDSSS VNFFGFTSNF SNSDQDYLSA LETCFENSNV FNDQQLKQMA RKLLTFSKRE
NQSRIAESEL LEELELEEKR KKQKQQEKIK KRLKREKRLK EKQDLLLIKL EKQKEKQLEE
QMKKREKKLQ KLERKRLYKK LQDDEKQKLI EKQKQKEKEK ELSKQKEKEF ELLKQKEIDE
IKQKSIQEID EINKNIQQNQ LKIDEINKKL EIKEIQNFQL PLLNQQQQQP PPLQLLKQQQ
QQPSSSLTIQ LESITPILEP KNDNVVLLKS SIETPIDSVK KIQSIIEIQL EEENQKKKEM
ETIDEYEEIN INKKQINSNM KWGGIGEPSW ISVKKDNKKS KSTITTSTTP TTTTPAKVIT
SQFKNEQTKK LIIENNKKQN LINDNNNNNN NNNNNNNNNN NNNNNNKLNN IIQDEDFVSI
GKFKFNRNES NILGRGSNGT LVFKGLWSDK IPVAIKQMQK AFNPLINKEV EALISLTSKN
CSNMIRYIDK EEDKLHVYLG LTLCDGSLQN LVESGKLNDF VISSNKSIIE LAKDILFGIQ
FLHSHDIVHN DLNPRNILTL IGKTSNNNNS SNNSFIISDL GLSKMEVESS YSFTSNIPTG
QGGYHPFEVL QSKRMTKSVD IFSLGCILFY LLTNGQHPFG NDKLFRIVNI ISNKMNLTPL
NSNQLACTLI KSMISKDESI RPTIQNVLNH PLFWNLEKKI QFIDAALNLI KEPSNSSYNS
KLTKQLNHCD DNDEPFLNDS WNHLIDVTNL LTPTKGSKIT ISYQYDKVRD LIRFIRNTIA
HHKEIKRAII QQFQNQQSRP NLEVLEYLSS QDSILLYFES KIPNLIHHIY QQLKQYSLTI
DYLFNFYN
