IRLF_DICDI
ID IRLF_DICDI Reviewed; 1400 AA.
AC Q556Q3; Q86AL1;
DT 10-FEB-2009, integrated into UniProtKB/Swiss-Prot.
DT 02-MAY-2006, sequence version 1.
DT 03-AUG-2022, entry version 93.
DE RecName: Full=Probable serine/threonine-protein kinase irlF;
DE EC=2.7.11.1;
DE AltName: Full=Inositol-requiring protein-like protein kinase F;
GN Name=irlF-1; ORFNames=DDB_G0273171;
GN and
GN Name=irlF-2; ORFNames=DDB_G0273903;
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}.
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DR EMBL; AAFI02000011; EAL70642.1; -; Genomic_DNA.
DR EMBL; AAFI02000009; EAL70803.1; -; Genomic_DNA.
DR RefSeq; XP_644568.1; XM_639476.1.
DR RefSeq; XP_644683.1; XM_639591.1.
DR AlphaFoldDB; Q556Q3; -.
DR SMR; Q556Q3; -.
DR STRING; 44689.DDB0229362; -.
DR PaxDb; Q556Q3; -.
DR PRIDE; Q556Q3; -.
DR EnsemblProtists; EAL70642; EAL70642; DDB_G0273903.
DR EnsemblProtists; EAL70803; EAL70803; DDB_G0273171.
DR GeneID; 8618777; -.
DR GeneID; 8619199; -.
DR KEGG; ddi:DDB_G0273171; -.
DR KEGG; ddi:DDB_G0273903; -.
DR dictyBase; DDB_G0273171; irlF-1.
DR dictyBase; DDB_G0273903; irlF-2.
DR eggNOG; KOG0516; Eukaryota.
DR eggNOG; KOG1027; Eukaryota.
DR HOGENOM; CLU_251496_0_0_1; -.
DR InParanoid; Q556Q3; -.
DR Reactome; R-DDI-381070; IRE1alpha activates chaperones.
DR PRO; PR:Q556Q3; -.
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 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..1400
FT /note="Probable serine/threonine-protein kinase irlF"
FT /id="PRO_0000362021"
FT DOMAIN 950..1235
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT DOMAIN 1238..1400
FT /note="KEN"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00725"
FT REGION 267..320
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 416..457
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 707..746
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 802..887
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1084..1113
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 689..801
FT /evidence="ECO:0000255"
FT COILED 842..933
FT /evidence="ECO:0000255"
FT COMPBIAS 267..319
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 416..453
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 721..742
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 802..857
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 858..879
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 1074
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 956..964
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 979
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
SQ SEQUENCE 1400 AA; 164197 MW; 6F96C09F5566E4AA CRC64;
MNFNFEQILE YNFDFKKLHK NKLKNNNLSE NEDDYATTVI ECLIHLCEVI PTNKIYSGAN
KFISCFYEFM NERFIETLVL EFYDLMTTDN SKVTTGIFDQ FFSLIKKSDI IYKSFYEWDS
NILENRFIFK NNNNNIDGDD DDGNEDDYFG RFSILSILED DNSHIISNYF KFTNYERLED
LWIMICHYQA TDIAKALFNL YYDSKEDCIS VFASDDNNNK ISISILRILE ITSIEFSLPV
LTVIVENTPN FLNSIPTKTS MLGMKFKLHN NNNNNNNNNN NNNNNNNNNN NNNNNNNNNN
NNNNNNINKN NNDNGNGKAE NIYRLSGDCK EKEKYDNNYS RETEIPFKVF DTKFLITTME
CSDYIRFFTS SSIIFNTEVN QTCYDDLKLI QKRLGFLIYS NSNKFTYPFD FWNNNNNNNN
NNNNNNNNNN NNNNNNNNNN NNNNNNNNNN NNNKNDDDEL EKLVEYRKGS LISLVFSFAG
YRFFSSYIIE NLTGTNIGNP NYVFDISELM TDFEIIRGLL LSKYFSILFK SRKFTVPTLT
RSTLIPILIF AFISNISYDM NCNIANVYLN YLLLNRELYK GSISISQFGC IVNYLKCQNE
IEKQYSGCLK LLEGLYNHKK EKSPNEPYRI DLLFGVINDR LKAPIFINKD KYESLYFVYQ
EDYQNPSDPF RVLPTRSVDL SKISEGISRM KNDDFLNELE KEEKQKKLKT KQKKKIKKLE
NEKKQKVLQQ DKQQEKEKKQ NYQQPQDLQQ HNLKIQTQQQ QQQQQQQQQQ QQQQQQQQQQ
QQQQQQQQQQ QSQQQQQQQQ SPQQQSQQQS QQSQQKSQQQ SQQKSQQQSP PQQQQQQSQQ
PQQQSQQQSQ QKQKHQKQQQ QQKQEKQQQK QEKQQQKQEK PQQKQQLENQ IKNLKIEIKK
EEENNKEIKN KKEEVEKEKE ENNKEIKSKS EFIIVEDEDF VSIGKFKFNR NESNILGRGS
NGTLVFKGIW SDKIPVAIKQ MQKAFNPLIN KEVEALITLT NKNCSNMIRY IDKEEDKHFV
YLGLTLCDVS LQYLVENGKL NEFINSSGKS LNELAKDIIN GVQFLHSHDI VHNDLNPRNI
LTLSTNKNNN NNNKSNNKIK SNNNSNNNSN NNSNNSFIIS DLGLSKMEVE SSYSFTTNVP
TGQGGYHPVE VLQSKRMTKS VDIFSLGCIL FYLFTNGQHP FGNDKLFRIY NIMLNKVNLE
LLGHNLLACD LIKSMISNDE SKRPTIENVL NHPLFWNVEK KIQFIDAALN ICKESNNSGG
GGGGNKFNKS LNYLFVISLS SDYIEPKSEP FLKQTWDKLI DINNLSIGST SQYQYDQIKD
LIRFIRNTIV HHKDIKRLIQ QQQQQQKQPT IELQFINNIL TNQDSILFYF ESKIPNLIYH
LYKQLKEYSS SFDYLIKFYN
