ID Y1558_DICDI Reviewed; 1350 AA.
AC Q1ZXI5;
DT 20-JAN-2009, integrated into UniProtKB/Swiss-Prot.
DT 02-MAY-2006, sequence version 1.
DT 27-MAR-2024, entry version 90.
DE RecName: Full=Probable serine/threonine-protein kinase DDB_G0278845;
DE EC=2.7.11.1;
GN ORFNames=DDB_G0278845;
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=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. AGC Ser/Thr
CC protein kinase family. {ECO:0000305}.
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DR EMBL; AAFI02000024; EAS66888.1; -; Genomic_DNA.
DR RefSeq; XP_001134572.1; XM_001134572.1.
DR AlphaFoldDB; Q1ZXI5; -.
DR SMR; Q1ZXI5; -.
DR STRING; 44689.Q1ZXI5; -.
DR PaxDb; 44689-DDB0231558; -.
DR EnsemblProtists; EAS66888; EAS66888; DDB_G0278845.
DR GeneID; 8621734; -.
DR KEGG; ddi:DDB_G0278845; -.
DR dictyBase; DDB_G0278845; -.
DR eggNOG; KOG0605; Eukaryota.
DR HOGENOM; CLU_257764_0_0_1; -.
DR InParanoid; Q1ZXI5; -.
DR OMA; IDYLQIN; -.
DR PRO; PR:Q1ZXI5; -.
DR Proteomes; UP000002195; Chromosome 3.
DR GO; GO:0005815; C:microtubule organizing center; IEA:UniProt.
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:0035556; P:intracellular signal transduction; IBA:GO_Central.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 2.
DR InterPro; IPR000961; AGC-kinase_C.
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 PANTHER; PTHR24356:SF417; CELL CYCLE PROTEIN KINASE DBF2-RELATED; 1.
DR PANTHER; PTHR24356; SERINE/THREONINE-PROTEIN KINASE; 1.
DR Pfam; PF00069; Pkinase; 2.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS51285; AGC_KINASE_CTER; 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; Phosphoprotein;
KW Reference proteome; Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..1350
FT /note="Probable serine/threonine-protein kinase
FT DDB_G0278845"
FT /id="PRO_0000358901"
FT DOMAIN 756..1082
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT DOMAIN 1083..1203
FT /note="AGC-kinase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00618"
FT REGION 66..109
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 121..159
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 179..249
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 270..296
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 337..396
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 431..506
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 525..596
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 612..701
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1129..1159
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1190..1219
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1232..1285
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1300..1350
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 121..142
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 179..235
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 270..293
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 337..393
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 431..447
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 458..480
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 481..495
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 525..553
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 565..596
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 612..634
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 641..678
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1130..1152
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1199..1219
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 880
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 762..770
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 785
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
SQ SEQUENCE 1350 AA; 150420 MW; A2F1C846751BBDE7 CRC64;
MVFSLKESSD SISKPSSLKN STIIENPEIL NNNNNNNNSN NIIKSPNFLL SQKQRSINIS
NEQTQRELNN NGGNLDHRDP NSPKYLTSSH SSVVIPQDNS NNNNNNNIRI STSPILTEIS
ENGLLESPTS PIRTSSTPTT PTSPPFITSP PFITSPKGLN SPRRLVGFFS KSTSYQSLLA
NNNNNNNNSN NSNNNSNSSN SNISCSNNSN KISRLINNSN TTDSNASIRS SNNNNDDFDN
NDDEDLNSIN NSSGIGIGVS SDYSLMGSSS SINGNTTTTT TNTYSYNDND NVNEYSPKGK
RLIRHEKSKS SPPLSPITPY YENLVIKGNY TNSNNYNNYN NYYYNNNSSG NNNNNNNNNN
NNNNNNNNNN NNNNNNNNNN NNISGNSGYN NSRDDLFKRP FEMNKESSPT NSLIPNVSAL
KLNRVIKSSN GSTIFTSTSS DIASENDNNK NNENENENEN ENENENENEN DNDSDSENEN
ENDNSIGNKS NKSNSELSIE EQEKKKEKDL ENYINMINNS GFITNDSNNN NNNNNSGNNN
SFISNGSPFS PIKEESPQPS PTFSPKPTLQ RQRSNSKNVL YSPNASPSNS CKIPTPPLLH
NISIIDTSNN NNNNSNNIEN QNNNNNNIDN NIDNNIDSID KKLKNNNNNN NNNNNNNNNN
NNNNNNNNNN NNNNNNNNNN DDDDDDNNIK KTPNNKINTN ENPMIITNSV LKRSGNIDYL
QINNNYVIPS PSPGTQLSEC TNQQMKYNPP VSIVDFTLIE KIGEGGFGQV FLAKKKDTGE
IVAIKRMSKE LIWSKNKVSH IKNERDILAQ GKNHRWIVSL VYSFQDDQYL YLAMEYVPGG
DLRSLLSALN SLDEDSARFY MAEMVEAVDS CHRLGYCHRD LKPENFLISR DGHVKLADFG
LSKNVVTRYH LRSASADNTI NTTTSTPTTS SNINQLSSSM IEHTPMKFGA AANGNGPLNS
SVTDFGSFKD LSVAARLAYS VVGSPFYMAP EVLQATRGYG DEVDWWSLGC MFYEFIFGVP
PFDGDSPEEV METVLKWKTM LQRPDGVSDE LWDLISGLIN DGSTRLGSGE KGVENIKNHI
FFNGVPWGKL HDLDPPFVPL LQGDYDTTYF ENTEKLDNNF LLQQTQQLSL LPPPLPPPPQ
TPTQPQQPSL PPQTPNDKMI FDKIRSPVVY TNTHSGNIIT SRSRPRNILG FTYPRADDQP
LLWNNNNNNN NNNNNNNNNL LKNFEELTIL NNNNNKNKNK GNSNNNNNNN NNNNNNNNNN
NNNNNNNNNN NNSNNNKNNS NNKTVTIPIS TGRLLNEIDN CNNNNNNDEN NINTGNLTPP
NSSPFNSGEN LNFEKQEPTS PYGSYSKQQQ
//
