Y9628_DICDI
ID Y9628_DICDI Reviewed; 737 AA.
AC Q55DK2;
DT 10-FEB-2009, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 03-AUG-2022, entry version 90.
DE RecName: Full=Probable serine/threonine-protein kinase DDB_G0269628;
DE EC=2.7.11.1;
GN ORFNames=DDB_G0269628;
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=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. NEK Ser/Thr
CC protein kinase family. NIMA subfamily. {ECO:0000305}.
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DR EMBL; AAFI02000005; EAL72164.1; -; Genomic_DNA.
DR RefSeq; XP_646129.1; XM_641037.1.
DR AlphaFoldDB; Q55DK2; -.
DR STRING; 44689.DDB0229344; -.
DR PaxDb; Q55DK2; -.
DR EnsemblProtists; EAL72164; EAL72164; DDB_G0269628.
DR GeneID; 8617078; -.
DR KEGG; ddi:DDB_G0269628; -.
DR dictyBase; DDB_G0269628; -.
DR eggNOG; KOG0589; Eukaryota.
DR HOGENOM; CLU_376626_0_0_1; -.
DR InParanoid; Q55DK2; -.
DR OMA; HWFLAYC; -.
DR Reactome; R-DDI-1169408; ISG15 antiviral mechanism.
DR Reactome; R-DDI-381042; PERK regulates gene expression.
DR PRO; PR:Q55DK2; -.
DR Proteomes; UP000002195; Chromosome 1.
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:0008080; F:N-acetyltransferase activity; IEA:InterPro.
DR GO; GO:0004672; F:protein kinase activity; IBA:GO_Central.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR InterPro; IPR016181; Acyl_CoA_acyltransferase.
DR InterPro; IPR000182; GNAT_dom.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR Pfam; PF00583; Acetyltransf_1; 1.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF55729; SSF55729; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 3: Inferred from homology;
KW ATP-binding; Kinase; Nucleotide-binding; Reference proteome;
KW Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..737
FT /note="Probable serine/threonine-protein kinase
FT DDB_G0269628"
FT /id="PRO_0000362068"
FT DOMAIN 8..488
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 155..251
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 278..298
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 155..212
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 213..227
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 349
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 14..22
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 36
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
SQ SEQUENCE 737 AA; 82091 MW; 803279E9A78FAD00 CRC64;
MEDPLSSYKL IKDLRSGGEG KAILYEKDGV KYVGKKRLFD NLKDANQGLK EAMSLARIVH
PNTVRFEDAI MTQIGDQIEI TIMMEFCEMG DLLDFLIELS EPQHHHTVTL GSELSSLNLG
SEYTGSDIDS TTSRTSSSSS TNFEAALLLE NNNNNTIQHS HSSSSLVNGT TSPTNATTPP
ITTTTPNNRH SISTPTLAGT TTATTASPSS PSSPSSPSSP SSPSSPLSPQ QHPVTSPQRK
SSKSERKKKC SLKERKCIVK MTVDLTKKIF KKDNSNHTTA ATTTTTTNTT HSSSSSSNLN
IEEHVIHSNE IKKGVDSIYL IEQTQLIEWL LDLSYGVQAL HRASMIHRDL KSENIFISGS
NKLKIGDFGL AIQSAHHTGS IHSETVGTYC YSSPEILNST YDKTTDIFSL GCIFYELITL
KLLSHNRIYL GEDMLNDRFD SMQFLSTFPE KYEKLAPLVL SMISKNPTFR PSIESIIETL
QKMDTSLLKE RVVIKRENTI KGIRKQLDKS HFQEASLLLA TSFVKDPRFF NIFPPSDPHS
IPHLQHLYKY ILKVLSSYNC SIWGYFAIDG TMVSCFVWLN PEKKKEIRLS DCIKGSLSLV
TKIGLKRVGL ILDLMRFDDN ILSMAQNNNN NPNTSTSNLQ TFKGSSSSSS SSCNHWFLAY
CCTSEIFRGN GIGSHMIENV LNWADHNGVE TRTVVFENNS IEFFQHHGFE VGSEFKSNLP
KGVNKVMVLV RKPKQIY
