Y1664_DICDI
ID Y1664_DICDI Reviewed; 959 AA.
AC Q54EM1;
DT 10-FEB-2009, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 03-AUG-2022, entry version 95.
DE RecName: Full=Probable serine/threonine-protein kinase DDB_G0291664;
DE EC=2.7.11.1;
GN ORFNames=DDB_G0291664;
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. Ser/Thr protein
CC kinase family. {ECO:0000255|PROSITE-ProRule:PRU00159}.
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DR EMBL; AAFI02000177; EAL61816.1; -; Genomic_DNA.
DR RefSeq; XP_635219.1; XM_630127.1.
DR AlphaFoldDB; Q54EM1; -.
DR SMR; Q54EM1; -.
DR STRING; 44689.DDB0229339; -.
DR PaxDb; Q54EM1; -.
DR PRIDE; Q54EM1; -.
DR EnsemblProtists; EAL61816; EAL61816; DDB_G0291664.
DR GeneID; 8628166; -.
DR KEGG; ddi:DDB_G0291664; -.
DR dictyBase; DDB_G0291664; -.
DR eggNOG; KOG4721; Eukaryota.
DR HOGENOM; CLU_306845_0_0_1; -.
DR InParanoid; Q54EM1; -.
DR PhylomeDB; Q54EM1; -.
DR PRO; PR:Q54EM1; -.
DR Proteomes; UP000002195; Chromosome 6.
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 Gene3D; 1.25.40.20; -; 1.
DR InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR Pfam; PF00069; Pkinase; 1.
DR SUPFAM; SSF48403; SSF48403; 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 ANK repeat; ATP-binding; Kinase; Nucleotide-binding; Reference proteome;
KW Repeat; Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..959
FT /note="Probable serine/threonine-protein kinase
FT DDB_G0291664"
FT /id="PRO_0000362044"
FT REPEAT 294..324
FT /note="ANK 1"
FT REPEAT 333..362
FT /note="ANK 2"
FT DOMAIN 482..762
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 154..213
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 904..959
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 161..175
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 195..213
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 610
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 488..496
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 509
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
SQ SEQUENCE 959 AA; 111306 MW; 732A025F33F96BA9 CRC64;
MESKKNSYYK NVMDKIYAKE KDVLSINKDF QENNLTRISL ILNYKDFYLK FDESLHGYSF
GYVTNLFGLK LYSPFTETVR FDDTEKYMKT ILGVPSNEAL PQLCSDQHQN FEEKDPQIEI
LPSPQQQQQQ QQQQQQQQQQ QQQQQQQQQQ QQQQQQQQQQ LTPPPSPPLL PIPQPPAQNE
EQQLTQPPSI PPPQQKQIKI QKSDRGTQVK SITNPVNSLS KYINNSSLDY SIKKNYTLEE
IYENNKNYMD KTNNFLHFLF TFIDKTTIKD LEHFEKEISR VHNIEKLINE QNVKGETPLH
SLILYNSESC LKKLVIAKIN CMGIFDYSKC DNLNKNLLTH AIEKGDFEII KLVLIGGCPL
KMSPRSKLFK QNFKLYRQQI YRVFEIKEFL TELGFNQFIP MFLEYEFKNI NIYYQIKSFI
MVLTLNADEI LRWKSLLEPN KNLDLDSFCI EYQIKDQNGS ESQLMADHFK KVCQLNSLFG
YIDFHTQIGS AGNASVFEGT YKGMPIACKE MPVSGTYEQR VDSIKEIAAV GQIEDLGGCT
VVKTVGVLKY NEKLFLVMVK EKCNLLSFLS NKSEILKMQR GGIWTSIFKI SKEILKGLIS
LREVGMYHRD FKTANFLVSN TGKILISDFG TSRDENEKRF NTFAKTIGTL WYRCPRLGDC
SGDEKTLNHY NEKSEIYSLG IILWELICIA MTGTYVSPKI ALFQNEVDFS IWIHKDYRFS
FPIGTPQSLV KLITSMCLPC RDRRPTVHQI LDEVGIIETE FLSNRGIKGE QTYSGLECWR
EFNFSKQNVF GISISNLHDT EYKAVNKYNY TSYNNKNSLL MKRYLDNSNF VVELINPNGI
FKFKSFFEKE KLLYLKLKST YKGEYYFDMG KFLTTIIQIH QITEIYYKML QKYRELGLLR
NNNNNINNNN NNNNNCNNSK KFKTTSESTS ALGSDASSSS SPSSSSPSPK YSASIYHHQ
