Y9955_DICDI
ID Y9955_DICDI Reviewed; 916 AA.
AC Q55GU0;
DT 25-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 03-AUG-2022, entry version 81.
DE RecName: Full=Probable serine/threonine-protein kinase DDB_G0267514;
DE EC=2.7.11.1;
GN ORFNames=DDB_G0267514;
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. TKL Ser/Thr
CC protein kinase family. {ECO:0000305}.
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DR EMBL; AAFI02000003; EAL73210.1; -; Genomic_DNA.
DR RefSeq; XP_647094.1; XM_642002.1.
DR AlphaFoldDB; Q55GU0; -.
DR SMR; Q55GU0; -.
DR STRING; 44689.DDB0229955; -.
DR PaxDb; Q55GU0; -.
DR EnsemblProtists; EAL73210; EAL73210; DDB_G0267514.
DR GeneID; 8615898; -.
DR KEGG; ddi:DDB_G0267514; -.
DR dictyBase; DDB_G0267514; -.
DR eggNOG; KOG0192; Eukaryota.
DR HOGENOM; CLU_317952_0_0_1; -.
DR InParanoid; Q55GU0; -.
DR OMA; MGEDYTE; -.
DR PRO; PR:Q55GU0; -.
DR Proteomes; UP000002195; Chromosome 1.
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:0006468; P:protein phosphorylation; IEA:InterPro.
DR GO; GO:0007165; P:signal transduction; IBA:GO_Central.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR PRINTS; PR00109; TYRKINASE.
DR SMART; SM00220; S_TKc; 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.
PE 3: Inferred from homology;
KW ATP-binding; Kinase; Nucleotide-binding; Reference proteome;
KW Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..916
FT /note="Probable serine/threonine-protein kinase
FT DDB_G0267514"
FT /id="PRO_0000355167"
FT DOMAIN 662..916
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 283..311
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 461..518
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 550..646
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 784
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 668..676
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 689
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
SQ SEQUENCE 916 AA; 103257 MW; 8BEC703A476F7C06 CRC64;
MKGGGFYQNQ YLVPNVYFGN SSPVIAPIGG NALNNNNNNN NNNNNNGNNN NGININISNF
QHQQHQIHQQ HFGGLSPNMN QNHIIQHISH HQHQQAQQIQ IIQNNNQPQP QQHQIQHQQQ
QQQQIQQQIQ QQQIQQQQIQ QQQIQQQQQQ QIQQQQQQSK MNFIRGHHQR NSSFDEFSLS
DVSVGSFKDM GWEEIYFCYH HFTQMDEGKG YLKSFQQLIR YITGLYPDIS PSPNSQFLFS
LGLLYPNALP QVQSPNMILS LTLKQMIETY SYTKSMVYSG SGSGGGNSGS GGGNSGSGGS
SGNGTSGSGG SNNGSTIIIN NTNLNNINNN NNTNNNNTNN INIPSTPPIL RSLANGASST
NINIRKFSPQ QACHIIDVFN SVKDNKTGGV STLKLSLFGA DASLLPLTTL PFHEFVQYIG
LNIIPFENLF KPPPPPSSQL QSSPPIESQH LFLSEIDELT NNNQNNQNNN QQQQQYQQQQ
HHQQQQQQYQ QQPQPQPQPQ HQPFIYFEDT SNNNSPLDGN FNNSFGLFNN NNVVNHSPLG
NNILNNIQQF NNQNNNQNNN NNNNNNNNNN NNNNNNNNNN NNNNNNNNNN HNNNNHNNNN
NNNNQNNIFN HNQNQNNHLI NNHSPNQYNN QGNILKNSGS VVEPPSQQQQ YFSDIEISFS
ELKISSKLGE GTFGVVYKGL WRGSSVAIKQ IKINEDVNNQ VLEEFRKELT ILSRLRHPNI
VLLMAACTAP PNLCFITEYL PGGSLYDALH SKKIKMNMQL YKKLAIQIAQ GMNYLHLSGV
IHRDIKSLNL LLDEHMNVKI CDFGLSKLKS KSTEMTKSIG SPIWMSPELL MGEDYTEKVD
VYAFGIILWE LGTGELPYSG LDSVQLALAV TTKSLRPPIP NAWPYQLSHL IQACWHQDPL
KRPSFTEILN LLNEIP