ID Y0701_DICDI Reviewed; 2102 AA.
AC Q559T8; Q75JU5;
DT 10-FEB-2009, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 27-MAR-2024, entry version 116.
DE RecName: Full=Probable serine/threonine-protein kinase DDB_G0272282;
DE EC=2.7.11.1;
GN ORFNames=DDB_G0272282;
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. AGC Ser/Thr
CC protein kinase family. {ECO:0000305}.
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DR EMBL; AAFI02000008; EAL71293.1; -; Genomic_DNA.
DR RefSeq; XP_645246.1; XM_640154.1.
DR AlphaFoldDB; Q559T8; -.
DR SMR; Q559T8; -.
DR PaxDb; 44689-DDB0220701; -.
DR EnsemblProtists; EAL71293; EAL71293; DDB_G0272282.
DR GeneID; 8618413; -.
DR KEGG; ddi:DDB_G0272282; -.
DR dictyBase; DDB_G0272282; -.
DR eggNOG; KOG0606; Eukaryota.
DR HOGENOM; CLU_232370_0_0_1; -.
DR InParanoid; Q559T8; -.
DR OMA; VCRICED; -.
DR PRO; PR:Q559T8; -.
DR Proteomes; UP000002195; Chromosome 2.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0035091; F:phosphatidylinositol binding; IEA:InterPro.
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 CDD; cd06093; PX_domain; 1.
DR CDD; cd05579; STKc_MAST_like; 1.
DR Gene3D; 3.30.1520.10; Phox-like domain; 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; IPR000961; AGC-kinase_C.
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; IPR001683; PX_dom.
DR InterPro; IPR036871; PX_dom_sf.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR PANTHER; PTHR24356; SERINE/THREONINE-PROTEIN KINASE; 1.
DR PANTHER; PTHR24356:SF1; SERINE_THREONINE-PROTEIN KINASE GREATWALL; 1.
DR Pfam; PF00169; PH; 1.
DR Pfam; PF00069; Pkinase; 2.
DR Pfam; PF00787; PX; 1.
DR SMART; SM00233; PH; 1.
DR SMART; SM00312; PX; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF50729; PH domain-like; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR SUPFAM; SSF64268; PX domain; 1.
DR PROSITE; PS51285; AGC_KINASE_CTER; 1.
DR PROSITE; PS50003; PH_DOMAIN; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
DR PROSITE; PS50195; PX; 1.
PE 3: Inferred from homology;
KW ATP-binding; Kinase; Nucleotide-binding; Reference proteome;
KW Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..2102
FT /note="Probable serine/threonine-protein kinase
FT DDB_G0272282"
FT /id="PRO_0000362041"
FT DOMAIN 1..118
FT /note="PX"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00147"
FT DOMAIN 124..222
FT /note="PH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT DOMAIN 1527..1851
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT DOMAIN 1852..1911
FT /note="AGC-kinase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00618"
FT REGION 225..289
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 302..390
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 426..558
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 574..665
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 685..768
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 804..842
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1029..1051
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1106..1224
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1476..1514
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1687..1741
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1902..2070
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 225..244
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 249..289
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 302..332
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 333..349
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 350..390
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 454..492
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 501..558
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 574..663
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 804..825
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 826..842
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1476..1490
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1491..1509
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1687..1739
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1902..2065
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 1650
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 1533..1541
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 1556
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
SQ SEQUENCE 2102 AA; 234519 MW; 48D5278ABAA957F7 CRC64;
MKYQLSILGD ESRLDPTTFN AFTVYMVNVT NLMTNRQWNI YRRYSQFHEL DSEIKSAFPK
IKLPKLPKKY IFKNSTNREL VEERKLLLQK YLKDLVKHEQ IEDSDCLINW LVPQNEPAFT
SLNNPDKSGY LIKEGHVIRS WKKRYFVLKD GLIYYFKHQS DQEPTGMIPV IGSQIKRIGE
TERKFSFQII PKNETFFPTF SIQARDEQDC NDWIKAIELS QQHFQDQEQY RKQEEEERQK
KNNGARIKKS GSFEFSTLTS ASAPTSPVQS SSSTSNMLPS SYQFSSDGSN NNSVCSSIGA
LGPNNSNNNN NNNNNSYYYS HSSNNHNHYN HHNNNHNNSH HHHHHHNGLN RGSSQVSLSV
NTTSSNSSGS SSSTSLSRRH PPQKSKSDLN LSSVLHSNIR IGIDESDELY ILNNSISNEN
LSSMLEQPGS YQQPQHQQGG GGGGGGGGGN IVNNLPPLSL TQRHISNLSS RSNSNSSGSS
SGSGSSSGSG PIGSGGVGGG LNQPVKTSSQ QPHHRKSNSS NNPSYISHLH YLQPSNSSSS
ISSSSSSSSA SSASSASPFS SLFTTINQYF NPKSNLPYSP PSSPILNANN NNNNNNNNNN
NNNNNNNNDF NLNNNNNNNN NNNNGNTASG SSCNTTPNLL PAPTNVSPIQ NRARSSPMTS
LPLPNNLLIP IPVFSLNDEY NNINNNNSNI ESNNNNNNNN NNNNNNNNNN NNNNNNNNNN
NNNNNNNNNN NNNNNTTELV NNNIESNDND NNNSNNNNNN NNNSNNSLDL INKPLVKIIE
PKKKEKKSKS KSKVASISDF ITSKKKEKDK EKEKDKEKEK EKEIGGNIST STTPNKKNGT
LRSRALTLPV KPNDSILGTT PHHNHQNNHH HHGDISSINI IREKFISKTT RFSSDGKPRF
DINQKLVSTK LSVDKKIRNF IEVVIDDIDH EATSGGNLQK QQHTQLIAND IKKLANTVLN
MSVYDQREKN TQIVQSIQTL FATAISNKEM TSLVSKFLFI FSEFSRVVDV LNPVEKNLTN
VINKQLQSQQ QQQKQNETTG TTTGTAGSSV NPLSFSSNSI LVQQKRLSRS LQSFNEINHH
YSSSYHEPII YSSSLNQYNG INIGSGTPTT TSGDNTPLTN TATSSTVSSY SEPSLISSQN
QLPLSQQPQP QPQQQQQLND SSSFPTSPIS SRNDLISSNS SIYEPPLSDV ASQLIEQQQE
QQQQQHQEQP LQPQQQQQQQ PQPQPISTLV FDKANQRSSS PILEKKSILT DLLKENYQKE
TTNNNGIGNM IILSEYDKKL QKQQLYPNQH VIITEEMRNK PERSFVCRIC EDTYTQSQLA
KHTPFCALTN KHDFKNHSSH DERLYSILNL VKGIICDSFA SPNNSEQYSY LIDDEIISQL
GQQLEYLFNI PYGPVESPKQ CQDVINRVQA IIDENSTDMA LHVFGKRICK IIEEKKALFV
QYSKFQNAAQ TTTSKGKKWS MWGIIPFIKD IIPSPSSKVD SSSSSQISSP ILSSPPPPMK
QPPPQVIVPP SSLTTSSNTT SISIADFEII KPISRGAFGR VYLAQKKKTG DLYAIKVLKK
LDTIRKNMVN HVIVERNILA MVQNEFVVKL FYAFQSTDKL YLVMEYLIGG DCASLLRALG
CFEEHMAKHY IAETVLCLEY LHKSAIVHRD LKPDNMLIDG LGHIKLTDFG LSKIGIIDDK
KMEDSGNTNT NTHFNFSTSP TNTSMMDDSS TTGNPNGNGN TSLNSSQTNI LSPYPQRKNT
LKTPLKKPVK KVVGTPDYLS PEILLGTGHG QTVDWWALGI ILYEFLTGSP PFNDDTPELI
FQHILHRDRE MEWPEEISSE AKDLILKLLN PDPYKRLGAN GAYEVKTHPF FANVNWDTLI
DQEMDNIFLP KPENNYDTDY FWDRQSMYDD EAEDDFLTIN QSQPQHQSQH QSQPQSQPQP
QSQNLGQNNN NSESNNNNNN SNSNVSGQNI NNSVSSSSNN NGSGNLNNIC NNSNVNANNN
NSNGNLGNNN NNKNNNINND NDKNKNNNSN VQNNNNNNNN NILQQSSSPS STSSSLSNSS
NNNHNGGRQI NNSKDSDNSI GGGKNNSKIE DIEKDPITFG NFSFTNINHL KDMNNFFLKN
KS
//
