Y7989_DICDI
ID Y7989_DICDI Reviewed; 1433 AA.
AC Q54YZ5;
DT 10-FEB-2009, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 03-AUG-2022, entry version 98.
DE RecName: Full=Probable serine/threonine-protein kinase DDB_G0277989;
DE EC=2.7.11.1;
GN ORFNames=DDB_G0277989;
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 -!- DOMAIN: The protein kinase domain 2 is predicted to be catalytically
CC inactive.
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; AAFI02000023; EAL68167.1; -; Genomic_DNA.
DR RefSeq; XP_642057.1; XM_636965.1.
DR AlphaFoldDB; Q54YZ5; -.
DR SMR; Q54YZ5; -.
DR STRING; 44689.DDB0230037; -.
DR PaxDb; Q54YZ5; -.
DR EnsemblProtists; EAL68167; EAL68167; DDB_G0277989.
DR GeneID; 8621269; -.
DR KEGG; ddi:DDB_G0277989; -.
DR dictyBase; DDB_G0277989; -.
DR eggNOG; KOG0581; Eukaryota.
DR eggNOG; KOG1027; Eukaryota.
DR HOGENOM; CLU_252337_0_0_1; -.
DR InParanoid; Q54YZ5; -.
DR OMA; CISCIDI; -.
DR PhylomeDB; Q54YZ5; -.
DR PRO; PR:Q54YZ5; -.
DR Proteomes; UP000002195; Chromosome 3.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
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:0006468; P:protein phosphorylation; IEA:InterPro.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR Pfam; PF00069; Pkinase; 2.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; SSF56112; 2.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 2.
PE 3: Inferred from homology;
KW ATP-binding; Kinase; Nucleotide-binding; Reference proteome; Repeat;
KW Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..1433
FT /note="Probable serine/threonine-protein kinase
FT DDB_G0277989"
FT /id="PRO_0000362063"
FT DOMAIN 1..272
FT /note="Protein kinase 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT DOMAIN 1177..1433
FT /note="Protein kinase 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 332..366
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 521..550
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 151
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 1..4
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 41
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
SQ SEQUENCE 1433 AA; 167825 MW; DDF8B623B5A18F70 CRC64;
MNEIIVGEYK IHSLLKSFAD KDEERNVYIV LNKSNEKFIC KEIIYTQNSN IDNEKRKSEY
INLKKFSDTI KYPHLNISKY IEHFIILENQ QEKEKIKKQY IITEFYDGGD LSSLKITNKK
CFSIKNGDII YLFLKMLIIF KEFQTVIIHR DIKPDGSIVN DYYLCDLGSS TQVKTINSST
LIGTNQYIAP DVIKRGGYTG TIDIYGLGKT LLLLLNRVQQ NQYNKINKIL FEMMCSNEST
ERPTVDQLIE FMVCQYDNIS FTEFDDFTHP LSKDCIEYFK NNKLNILKKD VKPIQIKIKI
KEKEYRAYGA IQALLRNFYY IDNVISIEDN NNNNNNNNNN NNNNNNNNNN NNNNNNNNNN
NNSDGPIEVA EFEWNENTDR LASELLLGHF KTETGGKNYE IANSHIEFVL KSEVLKSLSY
HDEIVIDRQA TPIYDNFINS DDSQAQIPPT STKCIHIFSN HKYNFQKFIR DLPYGELTGD
VQLKAIFHLI LVIFEIAENG PDFMYNALLE KNMGTLFIIP PSSETTPRPP TPTATTTPTP
TATTPTTTTA TTTKLSQHNF KFLFPFRSYA FSHSSNTKLH IFLNIFGDHT KDGLIVDILK
LAKELDKTKL PTVDIILQLI KMIQKEKCKL LETYSNSGLD FYFNNFETLI FNYELKESLT
KLIDKNKIIH CVDSLNQILT TRYFYFVENH YKCYAIEPYK SLELISSFNE NKNIYIRKLL
HYSSFPSMKR FKYIQTYYDK VNNSHYFVFE IPKKLLNTTK KMELTKQSSS TTTKIDRMKI
FKNLIVQHLN NIQELKTHLK SIYEYSFNLV ISLEDDNKFE LYYSNSVSPF SSDGFIRSFY
DIGKWVFGNL NNQEEEGDQL VKMKSYFSFL RILSELSWFC NILGSGNVHN SIVYNELNIY
YYLKMLLPLL NDIKINVFHY QIQNDIFAKI IIGNTQYNII NLIEPNHIDD PFSMVQYHLY
IMELEKIETS DKFTCLRKQF NQRPQKQSKI FEIPNPNNSI DEILIEPTLI VQDINTSFQF
FKVNGIIKTI EDFNQEKDYS NIIILRSFLY FLQYLFKNPS KTTLLVLFDI RKIDFDNINS
SNDIDNESIP QYLCFDFLYF IKQMYGIDIY FQFEDFLEII STRPSIVSNI IQSNKKKILN
DIICMDIIEN DISMKDVFYL LSVDIIKTIS PTVNLVIYDK RYYIQKEVGS ISKIREWKKF
GIISSHPDAV VFLKYGKKDL KSAMLDNGKV NDENYYGIAV EDYMKSNELN ILYYLLSKQE
EPDFTNIERY YLENDKIYAM FPYVNGSCNL SEIDNLNEMD LLNILYQLCF QLHQLENLGI
FHRDVKPENI ISLRYGNGGI VVFIVDFGIS QYKGKHLENY YSRDGTFGYQ APEIYREELR
GDGDIKTQKY KMDVFSLGCT MAFLIKKFNI TSTYLNDFID NMTQPHVCKS FKK
