IFKB_DICDI
ID IFKB_DICDI Reviewed; 1358 AA.
AC Q550L8; Q7KWM3;
DT 10-FEB-2009, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 03-AUG-2022, entry version 121.
DE RecName: Full=Probable serine/threonine-protein kinase ifkB;
DE EC=2.7.11.1;
DE AltName: Full=Initiation factor kinase B;
GN Name=ifkB; ORFNames=DDB_G0276829;
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).
RN [3]
RP DEVELOPMENTAL STAGE.
RX PubMed=12697064; DOI=10.1186/1471-213x-3-3;
RA Fang R., Xiong Y., Singleton C.K.;
RT "IfkA, a presumptive eIF2 alpha kinase of Dictyostelium, is required for
RT proper timing of aggregation and regulation of mound size.";
RL BMC Dev. Biol. 3:3-3(2003).
RN [4]
RP DISRUPTION PHENOTYPE.
RX PubMed=17177855; DOI=10.1111/j.1432-0436.2006.00085.x;
RA Rai M., Xiong Y., Singleton C.K.;
RT "Disruption of the ifkA and ifkB genes results in altered cell adhesion,
RT morphological defects and a propensity to form pre-stalk O cells during
RT development of Dictyostelium.";
RL Differentiation 74:583-595(2006).
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 -!- DEVELOPMENTAL STAGE: Expression remains constant as development
CC proceeds. {ECO:0000269|PubMed:12697064}.
CC -!- DISRUPTION PHENOTYPE: Subtle morphological defects such as an aberrant
CC stalk structure; due to the redundancy between ifkA and ifkB functions.
CC Cells lacking ifkA and ifkB display severe morphological and patterning
CC defects. Mutant cells aggregate in streams that give tightly clumped
CC mounds. Fingers form from the mounds but remain attached to one
CC another, especially at their bases. The fingers culminate to give fused
CC and entangled structures lacking proper stalk but containing some
CC spores. The morphological defects are consistent with an enhanced cell-
CC cell and cell-substrate adhesiveness of the developing double null
CC cells, which may result in inappropriate cell contacts and altered cell
CC motility and sorting properties. {ECO:0000269|PubMed:17177855}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. GCN2 subfamily. {ECO:0000255|PROSITE-ProRule:PRU00159}.
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DR EMBL; AAFI02000019; EAL68916.1; -; Genomic_DNA.
DR RefSeq; XP_642914.1; XM_637822.1.
DR AlphaFoldDB; Q550L8; -.
DR SMR; Q550L8; -.
DR STRING; 44689.DDB0185219; -.
DR PaxDb; Q550L8; -.
DR EnsemblProtists; EAL68916; EAL68916; DDB_G0276829.
DR GeneID; 8620780; -.
DR KEGG; ddi:DDB_G0276829; -.
DR dictyBase; DDB_G0276829; ifkB.
DR eggNOG; KOG1035; Eukaryota.
DR HOGENOM; CLU_001222_0_0_1; -.
DR InParanoid; Q550L8; -.
DR OMA; ITVEPKH; -.
DR PhylomeDB; Q550L8; -.
DR PRO; PR:Q550L8; -.
DR Proteomes; UP000002195; Chromosome 2.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IC:dictyBase.
DR GO; GO:0004694; F:eukaryotic translation initiation factor 2alpha kinase activity; ISS:dictyBase.
DR GO; GO:0004672; F:protein kinase activity; IBA:GO_Central.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0098609; P:cell-cell adhesion; IGI:dictyBase.
DR GO; GO:0031589; P:cell-substrate adhesion; IGI:dictyBase.
DR GO; GO:0000077; P:DNA damage checkpoint signaling; IEA:InterPro.
DR GO; GO:0006468; P:protein phosphorylation; ISS:dictyBase.
DR Gene3D; 3.30.930.10; -; 1.
DR Gene3D; 3.40.50.800; -; 1.
DR InterPro; IPR045864; aa-tRNA-synth_II/BPL/LPL.
DR InterPro; IPR036621; Anticodon-bd_dom_sf.
DR InterPro; IPR016255; Gcn2.
DR InterPro; IPR041715; HisRS-like_core.
DR InterPro; IPR024435; HisRS-related_dom.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR Pfam; PF12745; HGTP_anticodon2; 1.
DR Pfam; PF00069; Pkinase; 2.
DR Pfam; PF13393; tRNA-synt_His; 1.
DR PIRSF; PIRSF000660; Ser/Thr_PK_GCN2; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF55681; SSF55681; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 2: Evidence at transcript level;
KW ATP-binding; Kinase; Nucleotide-binding; Reference proteome;
KW Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..1358
FT /note="Probable serine/threonine-protein kinase ifkB"
FT /id="PRO_0000362012"
FT DOMAIN 1..582
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 125..359
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 443..470
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1148..1204
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 125..197
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 198..215
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 226..288
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 300..331
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 336..351
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1148..1170
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1186..1204
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 413
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 2..10
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 25
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
SQ SEQUENCE 1358 AA; 151092 MW; 0EBB171AE71478A5 CRC64;
MIGKGGFGVV VKSRNKLDCR YYAIKKIKTK GYTDSNQEPL TNKLLREVTT LSRLHHQFVV
RYYQAWIEKS CDSFQSLEEG NEDLSGDLET DASEDWFMQS SINSRSIISR DSYSGLSTSN
SNVGGANNTA GGGDSVSNAN SNKSMIVGNN NKKLTLSSSN TSSSSSLLSN NKSKILNTSK
STSTNTSTST STSNTNKNKK ISKKKKSKLS PLMKPKNKKN KNNGESEQSS SDSENGENGM
KSRIIENASD SYSDDDNNNN NDSNNNYHSD NESDSFSGSI SMSDGNGSGY EATDDEDIIN
NSGSFDDNEN DDDDEEDDDD EYDEEDDDYE TFDFQDKSRV VSNNSKLSTS SSRKKPPKET
HTLYIQMEYC SKKTLKTLID NVGGIAEEEA FRLLRQIVEG LNHIHSQQII HRDLKPANIF
IDNEQNVKIG DFGLATSGAP VSKSDDLNSS TSNAANNINL SSSTNSTAQQ TPMWDLNDEN
LSMTGGVGTP FYCCPEILEK NTKHYGTKVD MYSLGIIFFE MCFQFQTQME RSNILRDLRD
NLKFPPGFES TKPDQTQIIR SLLSRDPTQR PSTKQLLESG LLPSKMEDDI LKEAIKTIAN
PTISLFSYLM EKLFCLSNDE HIMSRYLYTS NPSLTPMHLI CREKTFSRLE KIFLNHGSIR
IDTPTLFPKN PTNSTHPGAA NVAKFLDESG TVVYLPYDLT IPWARHVVIH NIQQAKRYTF
SKVYRRSQPG FSPKELYECD FDIIGPSKSR HISDAETLRI IIEIMEEFKD ELFGNNSGSN
SGSGSGGSIN YKIRINHYGL LDSILSECGV EKRFFTVVYQ TVAQLHWRLN WAQVAQSLKE
HGLSASIVSN ISTYFRQRGE LAQCVTQLES LLANHKEATT GISDLKILVR NLQMINIIPR
FLLDLSLIHN HQYYEGLVFQ AYIERPTLSN PSRTEIIMSG GRYDKLIKSL HPNPSLSNNI
VSGVGVTLAC EKIVNSVLNY RQHLLNNCFN TTYTRRNKDP PNSNNNPNNN NLNNNVSIFT
KFQSHIEVFV CSLGSSLLGE KLQVASQLWS AGIKADYSQT DYYSSEDIYS NCRENGIPWV
VILREKAFQI GKLKVKQIET RQERTVARKD LVDFFLKSRK HNVDSKNIIQ NTSSSDLSNL
IGGINNSGSG GSGGSGGGSS MSSGGGGGGN SNIGGSDHHH HGHHSNQSTS SSGNSNNSNT
QQTSPIQHHV HFSNTKSIIG SSGIISNATF SGGSSSSSNI IHFDEPTDSF STQIVYQGVE
EIKKSKIETL VQTSLSKLFR GFIQSKSSTI RVIVTDLAYS VIRDLQISES HDNISKFQRV
SKEKLLQLKN QIFKWKVYPF IVIHSIKDDK SVIFNSVV
