Y8901_DICDI
ID Y8901_DICDI Reviewed; 1495 AA.
AC Q54XJ4;
DT 05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 03-AUG-2022, entry version 105.
DE RecName: Full=Probable serine/threonine-protein kinase DDB_G0278901 {ECO:0000312|dictyBase:DDB_G0278901};
DE EC=2.7.11.1;
GN ORFNames=DDB_G0278901;
OS Dictyostelium discoideum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=44689;
RN [1] {ECO:0000312|EMBL:EAL68052.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4 {ECO:0000312|EMBL:EAL68052.1};
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 Evidence={ECO:0000250|UniProtKB:Q869N2};
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; Evidence={ECO:0000250|UniProtKB:Q869N2};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:Q869N2};
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. {ECO:0000250|UniProtKB:Q869N2, ECO:0000255|PROSITE-
CC ProRule:PRU00159}.
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DR EMBL; AAFI02000024; EAL68052.1; -; Genomic_DNA.
DR RefSeq; XP_647809.1; XM_642717.1.
DR AlphaFoldDB; Q54XJ4; -.
DR SMR; Q54XJ4; -.
DR STRING; 44689.DDB0231212; -.
DR PaxDb; Q54XJ4; -.
DR EnsemblProtists; EAL68052; EAL68052; DDB_G0278901.
DR GeneID; 8621769; -.
DR KEGG; ddi:DDB_G0278901; -.
DR dictyBase; DDB_G0278901; -.
DR eggNOG; KOG0198; Eukaryota.
DR HOGENOM; CLU_001872_1_1_1; -.
DR InParanoid; Q54XJ4; -.
DR OMA; WFADAIE; -.
DR PRO; PR:Q54XJ4; -.
DR Proteomes; UP000002195; Chromosome 3.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion 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:0018105; P:peptidyl-serine phosphorylation; IBA:GO_Central.
DR Gene3D; 1.25.10.10; -; 1.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF48371; SSF48371; 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; Magnesium; Metal-binding; Nucleotide-binding;
KW Reference proteome; Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..1495
FT /note="Probable serine/threonine-protein kinase
FT DDB_G0278901"
FT /id="PRO_0000374050"
FT DOMAIN 22..279
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 315..419
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 476..519
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 593..646
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 693..712
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1325..1373
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 315..329
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 336..419
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 476..513
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 147
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:P28523,
FT ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-
FT ProRule:PRU10027"
FT BINDING 28..36
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P28523,
FT ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 51
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P28523,
FT ECO:0000255|PROSITE-ProRule:PRU00159"
SQ SEQUENCE 1495 AA; 166223 MW; 490ABFB69D3E4638 CRC64;
MSQPSLLNQL NNIVDKESCG DYLLIDIIGK GGFGVVYKGL HKTKGYFSAI KKIKIMKKKK
LQSESQISLM AEINLLKVLS HHNIVRYYEH IPSSSHSYIV MEFIENGSLE KIIKRHGLLP
ESLVTVYIAQ VLNGLEYLHR QGVIHRDIKA ANLLISTDGS IKLADFGVAT KVSDLSSDNP
DDTFAGTPYW MAPEVIQMQG ISTACDVWSL GCTIIELLTG TPPYFGLAPA AALYKIVQED
HPPIPPGISA ALKDFLLNCF KKDENIRSSA KQLLHHPWVK SVQIRNPETQ APKNARQEIL
SYNAQLQDII QDNNSNITRP RSSAVVQPPS PSQLVPPLTN MNISSSNDNN NNNNNSSATN
NSPNISSTTT KNNSSTTNNN NNKLTSPSLS SSLLPIPATS TSTVNQNKAS PTLNSSWSAV
PSNKISQTVN SIDKSSLNKI NNGSGQHVQI ASPRKLSAGQ KQSIQPNIIA AAATTTTTTT
TTTTTNAATN TTTTTTPSST NTGSNVTSPV VSAISTPPPI PTTPLSPMMK SQEQLNQEKE
KINLHLRKFS EKESDDEFDN IVLPNSTICL QKLQPILSHK PPIQLQRQQS FNANNNISNS
NSNNNNNNNN NNNNNNNNNN NNNNSNNNNS SNNSNNNSNS NSINSSNSHK LKLLKFNKFT
EKDNEDDETD LVFDQKVSDT SRFKVRNQKK DWDDEFDNFG SSGDESESST ATTNAAINSN
IAKKILPSNR IIRYSSSGQL KQQQQQLLLQ QQQQQQQQHL QQPLSPSEMK LKVKETSEEW
DTEFEESFDT ISWSEADNQR TINIQDKYRE QVVKTIVEFI LQLKPNQPND VLIDTCQKLT
DLFQTYPDER KLLISNGEGG VYFRLPIITI LEILEDNCCC NSDTPSDVIT TTYHHNNNSD
TFSEDFSNVE LVINLLKLLN QSIIKEKDIQ ETICLMNGIS IITKLATKQF DELIREEVSK
FVLQLCSYST YSLNMFITGS RGCKVLVDLL DSDYFNGFTL IHNSLDAISL IFKMNTASPK
TALCHLFAKT ALMYRISYLL NQIFNSSDKS ATSKSQQFQQ KQIQQQQQLL LQQQQQQQQQ
QQLLPSSSSP NLKFPVLSKS SSVKNLSKDQ FDKVLAYSVK AADILLFFST GDSLVKEEMS
QSNVIKYIVN VLDEIYTWKT IGNNIRSFLL KILKVIKNLS MDPNVRSRLD DAGVIPPLIN
YLKKHGGIDK ITEIHNQALH SLYYLLLLDR SRQEKALKSS ILEPLLTIIE ERGPLKELAL
PILFDLVRSC NNRSLLWKCN TIDKLLDLIE DRNWFADAIE SISTWATLES KLVFEKLNSG
GTISPLTSTS TSTSTSKSSP SSSSSSSSSS LSTSTSTSSS SLQLPTSSSS TSFENHNIPL
RLIGILNINH IKHPSFQKSI IPLFNLINGS QQLLKSLINE GLVNSLVECL RVDSSPVSKI
TLLKITASIV QSPSLLLVDK EQTNSLYQIL NEISKQDESE IVKKIAENLV LELNK
