GenomeNet

Database: UniProt
Entry: Q552C1
LinkDB: Q552C1
Original site: Q552C1 
ID   Y9957_DICDI             Reviewed;        1555 AA.
AC   Q552C1;
DT   25-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT   24-MAY-2005, sequence version 1.
DT   27-MAR-2024, entry version 109.
DE   RecName: Full=Probable serine/threonine-protein kinase DDB_G0276181;
DE            EC=2.7.11.1;
GN   ORFNames=DDB_G0276181;
OS   Dictyostelium discoideum (Social amoeba).
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. TKL Ser/Thr
CC       protein kinase family. {ECO:0000305}.
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DR   EMBL; AAFI02000014; EAL69390.1; -; Genomic_DNA.
DR   RefSeq; XP_643307.1; XM_638215.1.
DR   AlphaFoldDB; Q552C1; -.
DR   SMR; Q552C1; -.
DR   STRING; 44689.Q552C1; -.
DR   PaxDb; 44689-DDB0229957; -.
DR   EnsemblProtists; EAL69390; EAL69390; DDB_G0276181.
DR   GeneID; 8620353; -.
DR   KEGG; ddi:DDB_G0276181; -.
DR   dictyBase; DDB_G0276181; -.
DR   eggNOG; KOG0192; Eukaryota.
DR   HOGENOM; CLU_246199_0_0_1; -.
DR   InParanoid; Q552C1; -.
DR   OMA; FNTCINR; -.
DR   Reactome; R-DDI-5673000; RAF activation.
DR   Reactome; R-DDI-5674135; MAP2K and MAPK activation.
DR   Reactome; R-DDI-5675221; Negative regulation of MAPK pathway.
DR   PRO; PR:Q552C1; -.
DR   Proteomes; UP000002195; Chromosome 2.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
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:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   GO; GO:0007165; P:signal transduction; IBA:GO_Central.
DR   CDD; cd13999; STKc_MAP3K-like; 1.
DR   Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR011993; PH-like_dom_sf.
DR   InterPro; IPR001849; PH_domain.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR   InterPro; IPR008271; Ser/Thr_kinase_AS.
DR   PANTHER; PTHR23257:SF984; MITOGEN-ACTIVATED PROTEIN KINASE KINASE KINASE; 1.
DR   PANTHER; PTHR23257; SERINE-THREONINE PROTEIN KINASE; 1.
DR   Pfam; PF00169; PH; 1.
DR   Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR   SMART; SM00233; PH; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF50729; PH domain-like; 1.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   PROSITE; PS50003; PH_DOMAIN; 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..1555
FT                   /note="Probable serine/threonine-protein kinase
FT                   DDB_G0276181"
FT                   /id="PRO_0000355169"
FT   DOMAIN          58..238
FT                   /note="PH"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT   DOMAIN          986..1309
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   REGION          1..54
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          138..208
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          342..452
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          486..508
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          781..850
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1012..1031
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1340..1383
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1457..1480
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        345..424
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        434..452
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1457..1474
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        1156
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT                   ECO:0000255|PROSITE-ProRule:PRU10027"
FT   BINDING         992..1000
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   BINDING         1061
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
SQ   SEQUENCE   1555 AA;  170901 MW;  C2E85639CA22E8F5 CRC64;
     MTSVGTTLIV KPANNSGGSD GNIKNNNNNN NNNNNNNNNN NNSNSGNNSN NNSFIDDQVL
     HTGYLTKQGG RIQNWKIRWF VLKRGTLSYY LSPINWEYTK PRGVIYLTKK TELKEVDHRN
     RRHCFAVNPN YISENQSIIQ QQQNQPILRS SSDSVNNNNN NNNNNNNNNN NNNNNNNNNN
     NNNNNNNNNN NNNNNNNNNN NNNNNSKLYP NSTRIYLISA QTVFDKSKWI EMIKLAISSD
     NSQDSKLKRA NHQLEKVKDL VFSNRKGSIP TFPSLLNRTI ATESLNDLIK VHLSKKRFYF
     YHDNLTLPAL SYIDSESPVN LQEIHHQHLI LLQQQKEELN KKLKKIQQQN NIGGGGSGSN
     IANSANKINN KNNDKINGVG SGEDKNNNKG GGGDNNSQSS SSSVSPTTVS PSVSPLSSSP
     TKPPIILSKK PLPTPPRNIS TSDNGSGTDS PFYNSAITRL PLISTSVGMV GPNGMVNITS
     MNTTTTTTTT TTTTAPTTTN TNTNIKPLPG IQQNKLQLIQ NKDGGGGGGG VLKRTNPLLS
     TSAPSMAYNQ LVANSGIIHK HQPKIVVFHL VRDSFQISNI GGCSFNFEIL SPFDPNFTLN
     FIPSSGTIQK GDSLTVLVEL MAYNHIETDI YSTLHIIGGM EFTLFCRIET DPYLPLFLKS
     CAGSVLPLEK QMKMESFMKK NPTMVKSIQE LAHTLILDGR NIIPLHLSNN ININNNNNNG
     GGGSGYNIGG GSNNSIGGSG SNNNSNVNIS NGWNIENSNR RNSGGCLNLV GGSGGGGLIN
     NNINNNNNNN NNNNNNNNNN NNNNNNNNNN NNNNNNNNNN NNNNNNNNNN NNGSGLLSSS
     PLITISNQNT PTPQARVKLS KYILNFQRNQ KKNSVGDVES VKIYQLLTDK FLISNSGSAD
     ASFQFHFPSR GKKNDLFSLS LVPTNGTVSK GEWFYIKSTL TVFVETEISE MIQLIINQRE
     VHHILITVKC ENIHPGNKEI DLEKEVVLHE RLGTGATGDI YRGLISQDNL NRHISNQDSS
     GSNSSGSGSG HNWLIARNPS NDIINKDAII GSGPQIIVAV KKLHPLADPS PEMIQDFYNE
     VRVLSMFNHP NVVKYVGGCT KIANWSIVME YVPGGNLMDV LANPVLVIPY KLVLRMALDI
     AKGLHYLHSL GILHLDMKSP NLLVSSLSTS AKVNIKVADF NTCINRSRIT AGFFNRHTGS
     GDNNKVEKDS KKGTTLWMAP EVIRGAMYSE KCDVYSFAII MWEMVTRKLP YSHIAFNCEV
     EDQVLKGLRP PIPMHCNKNY TDLMEQCWDD DPENRPYFDT IIHSISKMIE SNDITEQKAK
     ASFKGLRRTQ SNSTLNLLQV QNNNNNSNNN NNNNNNNNNN NSNSNLNNCN NSSPNLGTNS
     ANNDSGVSVL QTCSDIGVGS TGTNSGTSGT NSGFDSPVIV TKDYHLISNL QKLDLHSNDG
     SDTNGSQIGF KSDINSKKSS LEVHSKHKSK RFSYDGGSSR ASINTLNNDS NLPFKFSPPS
     TPQSSFLQLK KLDKELKSNL ESNAGTKHSF IRYKPSFTNV TSAKSKLNLN NNNNN
//
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