IFKA_DICDI
ID IFKA_DICDI Reviewed; 2258 AA.
AC Q558U1; Q86B04;
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 ifkA;
DE EC=2.7.11.1;
DE AltName: Full=Initiation factor kinase A;
GN Name=ifkA; ORFNames=DDB_G0272837;
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 FUNCTION, DISRUPTION PHENOTYPE, AND 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 -!- FUNCTION: Phosphorylates eIF2-alpha, from 1 to 7 hours after the onset
CC of development or during the preaggregation state, resulting in a shift
CC from polysomes to free ribosomes for bulk mRNA.
CC {ECO:0000269|PubMed:12697064}.
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 dramatically drops soon after the onset
CC of development and remains at a low level for the remainder of
CC development. {ECO:0000269|PubMed:12697064}.
CC -!- DISRUPTION PHENOTYPE: IfkA null cells have defects such as an earlier
CC aggregation, a formation of larger than normal mounds and ultimately a
CC formation of fruiting bodies that are also larger than normal. The
CC early aggregation phenotype reflects an apparent, earlier than normal
CC establishment of the cAMP pulsing system. Cells lacking ifkA and ifkB
CC display severe morphological and patterning defects. Mutant cells
CC aggregate in streams that give tightly clumped mounds. Fingers form
CC from the mounds but remain attached to one another, especially at their
CC bases. The fingers culminate to give fused and entangled structures
CC lacking proper stalk but containing some spores.
CC {ECO:0000269|PubMed:12697064, ECO:0000269|PubMed:17177855}.
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; EAL71056.1; -; Genomic_DNA.
DR RefSeq; XP_644975.1; XM_639883.1.
DR AlphaFoldDB; Q558U1; -.
DR SMR; Q558U1; -.
DR STRING; 44689.DDB0185218; -.
DR PaxDb; Q558U1; -.
DR EnsemblProtists; EAL71056; EAL71056; DDB_G0272837.
DR GeneID; 8618652; -.
DR KEGG; ddi:DDB_G0272837; -.
DR dictyBase; DDB_G0272837; ifkA.
DR eggNOG; KOG0198; Eukaryota.
DR eggNOG; KOG1035; Eukaryota.
DR HOGENOM; CLU_001222_0_0_1; -.
DR InParanoid; Q558U1; -.
DR OMA; QHIPHRD; -.
DR PhylomeDB; Q558U1; -.
DR PRO; PR:Q558U1; -.
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; IMP: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:0140582; P:adenylate cyclase-activating G protein-coupled cAMP receptor signaling pathway; IMP:dictyBase.
DR GO; GO:0031152; P:aggregation involved in sorocarp development; IMP:dictyBase.
DR GO; GO:0098609; P:cell-cell adhesion; IGI:dictyBase.
DR GO; GO:0031589; P:cell-substrate adhesion; IGI:dictyBase.
DR GO; GO:0048255; P:mRNA stabilization; IMP:dictyBase.
DR GO; GO:0031158; P:negative regulation of aggregate size involved in sorocarp development; IMP:dictyBase.
DR GO; GO:0006417; P:regulation of translation; IMP:dictyBase.
DR GO; GO:0006446; P:regulation of translational initiation; 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; 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; 3.
DR Pfam; PF13393; tRNA-synt_His; 1.
DR SMART; SM00220; S_TKc; 2.
DR SUPFAM; SSF55681; SSF55681; 1.
DR SUPFAM; SSF56112; SSF56112; 2.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 2.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 2.
PE 2: Evidence at transcript level;
KW ATP-binding; Coiled coil; Kinase; Nucleotide-binding; Reference proteome;
KW Repeat; Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..2258
FT /note="Probable serine/threonine-protein kinase ifkA"
FT /id="PRO_0000362011"
FT DOMAIN 319..691
FT /note="Protein kinase 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT DOMAIN 894..1482
FT /note="Protein kinase 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 43..108
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 189..308
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 358..398
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 741..768
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 782..870
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1053..1259
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1343..1370
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2048..2104
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 273..309
FT /evidence="ECO:0000255"
FT COMPBIAS 55..97
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 189..297
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 804..821
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 822..844
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 845..870
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1053..1095
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1096..1113
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1124..1188
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1200..1231
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1236..1251
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2048..2070
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2086..2104
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 498
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT ACT_SITE 1313
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT BINDING 325..333
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 348
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 900..908
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 923
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
SQ SEQUENCE 2258 AA; 252390 MW; 2A947A361D057E07 CRC64;
MAPGEIIIFE LCQAVQEFLL LYNKETVSLH EEMIKRLNTN INRVNSSDDI NNNNNNNNDD
DDDNDDYDDS DDENSDSDYD DYDDSDDENS DDEFYSDDED YNTRHQMGDI GSSVNKIINS
IDHTISHGGG VGVGIGSGNG LFSKSSSSSS PMIPYNFSFD SLNGFDPDII FEDSFQTPLK
GSSSIDFEEM NNLTNSNNSN STATTTTTTT TNNNNNNNTN NNNNNNSNNN NNNNNNNNNT
NNNTNNNNNN NNNNNNNNNN NNNNNNNNNN NSNNNNNISN NKINKINNNN NNKELIDNNN
NNKDKENDLI NDTIPKIKWK KGSCIERKSN YSVYRGVDED TDRKLICKIV NLNIDDRSSS
SLTSLSNSNN NNSNNNNNNN NNNNNNNNNN NNNNNNNNLS IDVVELKKRL IEKVKMIQKE
IESMKYLGNP YIIKYLGTNF QEGQNTLYIF QEYNSTLTLQ QKILSNGIGF EESQVKKFTY
QLLLGLLYLH SQHIPHRDFK SHNIFFNQST SKMLLSNYGG RNIKIFDHFE KLNSLKNLNS
WISSTNNSIN NINNINNNNN NNNNNINTTT TQNQINNEID RREDIINLGI VVLEMLCGSD
LANNQTVLIY LAQLNLLNNQ QQNQNFIQPP PLQYQLQQQY DLIKEIEQKT HPSSPISNNA
KDFLSLCFTI NGNGSTNDSL EAGILLKHPF LASNSNSTPP PSNFLNFTNN IKFLDQRSAA
TQALLSSPHS LIPQPIQTLI KSQTPNNNND NNNLASSNEL LSSSNGSNID LRSTNSSIVS
NPLATSSSLD NITPPPSRPI SPKPSPLNKR NQKLQTSQQK PPLSPPQTPL KQIPQSPQSP
PQQNFNTPPT TTTTTTTPTA TPTTPTMTPL TPIQKQQQID YDMFRYHSRY RTDFEEIEMI
GKGGFGVVVK SRNKLDCRYY AIKKIKTKGY TDSNQEPLTN KLLREVTTLS RLHHQFVVRY
YQAWIEKSCD SFQSLEEGNE DLSGDLETDA SEDWFMQSSI NSRSIISRDS YSGLSTSNSN
VGGVNNTAGG GDSVSNANSN KSMIVGNSNK KLTLSSSNTS SSSSLLSNNK SKILNTSKST
STNTSTSTST SNTNKNKKIS KKKKSKLSPL MKPKNKKNKN NGESEQSSSD SENGENGMKS
RIIENASDSY SDDDNNNNNN NDNNNNYHSD NESDSFSGSI SMSDGNGSGY EATDDEDIIN
NSGSFDENEN DDDDEEDDDD EYDEEDDDYE TFDFQDKSRV VSNNSKLSTS SSRKKPPKET
HTLYIQMEYC SKKTLKTLID NVGGIAEEEA FRLLRQIVEG LNHIHSQQII HRDLKPANIF
IDNEQNVKIG DFGLATSGAP VSKSDDLNSS TSNTANNINL 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
