IFKC_DICDI
ID IFKC_DICDI Reviewed; 1700 AA.
AC Q75JN1; Q551Y4;
DT 10-FEB-2009, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 124.
DE RecName: Full=Probable serine/threonine-protein kinase ifkC;
DE EC=2.7.11.1;
DE AltName: Full=Initiation factor kinase C;
GN Name=ifkC; ORFNames=DDB_G0276043;
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. GCN2 subfamily. {ECO:0000255|PROSITE-ProRule:PRU00159}.
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DR EMBL; AAFI02000014; EAL69321.1; -; Genomic_DNA.
DR RefSeq; XP_643344.1; XM_638252.1.
DR AlphaFoldDB; Q75JN1; -.
DR STRING; 44689.DDB0216407; -.
DR PaxDb; Q75JN1; -.
DR PRIDE; Q75JN1; -.
DR EnsemblProtists; EAL69321; EAL69321; DDB_G0276043.
DR GeneID; 8620394; -.
DR KEGG; ddi:DDB_G0276043; -.
DR dictyBase; DDB_G0276043; ifkC.
DR eggNOG; KOG1033; Eukaryota.
DR eggNOG; KOG1035; Eukaryota.
DR HOGENOM; CLU_240920_0_0_1; -.
DR InParanoid; Q75JN1; -.
DR OMA; MEYCQKI; -.
DR PhylomeDB; Q75JN1; -.
DR PRO; PR:Q75JN1; -.
DR Proteomes; UP000002195; Chromosome 2.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004694; F:eukaryotic translation initiation factor 2alpha kinase activity; IBA:GO_Central.
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:0000077; P:DNA damage checkpoint signaling; IEA:InterPro.
DR GO; GO:0032268; P:regulation of cellular protein metabolic process; IEA:UniProt.
DR Gene3D; 3.10.110.10; -; 1.
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; IPR006575; RWD-domain.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR InterPro; IPR016135; UBQ-conjugating_enzyme/RWD.
DR Pfam; PF12745; HGTP_anticodon2; 1.
DR Pfam; PF00069; Pkinase; 3.
DR Pfam; PF05773; RWD; 1.
DR Pfam; PF13393; tRNA-synt_His; 1.
DR PIRSF; PIRSF000660; Ser/Thr_PK_GCN2; 1.
DR SMART; SM00591; RWD; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF54495; SSF54495; 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.
DR PROSITE; PS50908; RWD; 1.
PE 3: Inferred from homology;
KW ATP-binding; Kinase; Nucleotide-binding; Reference proteome;
KW Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..1700
FT /note="Probable serine/threonine-protein kinase ifkC"
FT /id="PRO_0000362013"
FT DOMAIN 74..197
FT /note="RWD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00179"
FT DOMAIN 494..1027
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 454..488
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 568..639
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 689..760
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 850..901
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1134..1160
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1216..1253
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1507..1531
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 570..639
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 689..731
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 732..750
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1226..1240
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 822
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 500..508
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 523
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
SQ SEQUENCE 1700 AA; 194665 MW; 1B0C3465BF80DD94 CRC64;
MPPKPKQKAK QPSQQPPPPP PPAAAQLIED ILSSDEEEGG VKLPTKSSVK NALKKVKKER
DRELIRQLKD QQDMELEALQ AIFNDEFITM DPIIINRNMD TIIEGIKPIR ESARFRITIK
PYVGDDEKCF VSIYLVVGFP EKYPVVLPSI QVLVNKGLPQ KKAIELEEKL IRESQGKIGN
IMIFDLCEIA KDFLNENNFE PTQSIHHDFR SHQQKISIEI STNEQQQQQL QQLQQLQLQY
NNDTKKEWES TLEESQLKED RKNYRLQKSI QRAQYEKERK KTIVNEFTNG PQSKLSKQQR
NIDYSIDHSI NNNNNNNNNA FNNFNNNNNN NNTNNSNVSS IDNKTIDKQQ TMILHLLRLL
CQNDSNITND HIKTLGEQLV QMGIFNRNHL SLLNMHNSND NQIYQHIFQD YFLKQFNDIS
LSDLKNNVDS AANNSGHFLN KFWDTLNKTN ENSGLKKSPS TFEYSGEGGG GGVGGGSSQK
TINPHQQSRY HSDFEEIQLL GRGGFGQVVK VRNKLDGRYY AIKKIKLDSN QSLNRRILRE
VITLSRLHHQ HVVRYYQAWI ESAESLSLTN DNSDDDDDDD DEFESGSESE ESQSESESES
SESEESSESE ESSESSESEE SEESEYSDDS EFESEENNDF DQSFSEVFLF QNGNKRSLEF
DLTDDSYSFL HSDCGFLLEV FDLNNKIGGN NTRSMGSSNQ HLQQQQQQNQ SQQQKKQPQQ
NQSQQQKKLK NSNSKSKSKS KSKSKSKSKS NSKKSISSSK LKNIKKSTSI PYLYIQMEYC
QKILRNLTET GMNLEDDDIW KLFRQIVEGM AYVHGQGIIH RDLKPSNIFF DSCGDIKIGD
FGLAINNKTT STLSPTTNIN SSTSSAGSLT TSSNSVQSVI NTKQQQQQQQ PQNYWEDEVE
GQQQQQQQQQ QQQQQQQQQQ QQQQQHTARV GTLFYTSPEQ EAGTNGDSAY DDKVDMYSLG
IVFFEMWYVF STGHERVIVL RNLREKFEFP SDFERNHSRQ ATLIRMLIDK DPAKRPSAQQ
LLQSELMPPK MEDEYIKNSI RVITNPTNQF YQTMLNSLFS QNHQHLHSHI YHHQQSSVTS
SSYSKSLFCS LDLLQVKQLV DDVIITILKK HNANEMLTPQ MSIIKEWNEQ PNLFNNSSSS
SSTTTTTSTT NTANNTNSVV INKSTSTSNI NKVSNKTGKS ILMDDSGQLL ELRHDLRVSF
KSFIETEFLN LGDHYKHHHQ QQNDVRHDNS SNGNSNNNNS NDRHHDQDKS NTTTRSVDEI
LELLSKAPIK RYEFGHVFRK PHLVGKLPKE LSQFCFDVFG SSSLYSDAET IKVTTEIFDS
LPSTQNFYFV RLNHFGIVEY MWKFIGITDL TLKNEISQVV SQLIRQPWFT VKKVLLEKFK
LPLKQVERIA NWVLVKGTIP DVLKKLDASQ NNNPLLSGNG SLGNNNNNNN NNNNVRISSS
FTDLLEDIRQ LAVYFEKMSI SPHKVIFDLS YCFSENFYST GIMFQVILKE EKHECLAVGG
RYDSPLNLNN SNNSSSSSSS SSSNNNNSYN NYNNNNNYNY NYYSNCYLTN FNLPITGLSV
AMDKVYSRER ELYSQKRRQQ LPPTLSSESQ MIAHKFSTPD IFVISLGPNL FLERIGIVGD
LCNAGFNAET MYIENPTPEE QQDASITSGA LYIITIKEKG AKKTIKVKNI EKRREDDVSR
DEIVKFFTLS NFNSKSRLNI
