Y0004_DICDI
ID Y0004_DICDI Reviewed; 998 AA.
AC Q54ZN3; Q8MN47;
DT 10-FEB-2009, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 03-AUG-2022, entry version 104.
DE RecName: Full=Probable protein kinase DDB_G0277539;
DE EC=2.7.11.1;
GN ORFNames=DDB_G0277539;
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=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. Ser/Thr protein
CC kinase family. WEE1 subfamily. {ECO:0000255|PROSITE-ProRule:PRU00159}.
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DR EMBL; AAFI02000020; EAL68732.1; -; Genomic_DNA.
DR RefSeq; XP_642609.1; XM_637517.1.
DR AlphaFoldDB; Q54ZN3; -.
DR SMR; Q54ZN3; -.
DR STRING; 44689.DDB0220004; -.
DR PaxDb; Q54ZN3; -.
DR PRIDE; Q54ZN3; -.
DR EnsemblProtists; EAL68732; EAL68732; DDB_G0277539.
DR GeneID; 8621026; -.
DR KEGG; ddi:DDB_G0277539; -.
DR dictyBase; DDB_G0277539; -.
DR eggNOG; KOG0601; Eukaryota.
DR HOGENOM; CLU_300254_0_0_1; -.
DR InParanoid; Q54ZN3; -.
DR OMA; YELARCK; -.
DR Reactome; R-DDI-156711; Polo-like kinase mediated events.
DR Reactome; R-DDI-69202; Cyclin E associated events during G1/S transition.
DR Reactome; R-DDI-69656; Cyclin A:Cdk2-associated events at S phase entry.
DR PRO; PR:Q54ZN3; -.
DR Proteomes; UP000002195; Chromosome 2.
DR GO; GO:0005634; C:nucleus; 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: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:0004713; F:protein tyrosine kinase activity; 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; IPR008271; Ser/Thr_kinase_AS.
DR Pfam; PF00069; Pkinase; 2.
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; Magnesium; Metal-binding; Nucleotide-binding;
KW Reference proteome; Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..998
FT /note="Probable protein kinase DDB_G0277539"
FT /id="PRO_0000362036"
FT DOMAIN 508..849
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 1..34
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 65..207
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 265..284
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 316..367
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 380..420
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 435..489
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..23
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 65..139
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 162..207
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 387..420
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 631
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 514..522
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 537
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 636
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 677
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
SQ SEQUENCE 998 AA; 114845 MW; E08989F8630D235C CRC64;
MDFPSQSEKK KYITKKRTTL FSYDDDDDDD DFDQNREFIH MSSYEESKDQ QNSFNTLLLS
ELSNCEDQKQ QQQQQSSSPT QSDCDSSPTN NNNNNNTNNN IVHHLNNSNS IPISGSNNNN
NNNNNNNNNN NNNNNNNNNS HHHHLRKGRR LFHDDNDDQP IYPASASLSS TKTNMFPSSP
ILYSSPSSQQ QQQQQQQQSQ SQQTNEFKVP SFTPLSFINN SSTNSMNIRP INNNRIYNNL
NNNNNNNNNN NNNINNINNN NINNINNNYN NNNNNEEDQI FSSSLPTSPV SWSANGSMMN
GHNINNITGN HSRFLSNGSY NKGNTFPSTE VKRVRPDQRA FNENSFSMSP TPSPPPTPSL
KRNNYSSPKF EPVFIRLAEE RTNRKRSTSM TSNVNNNNNN NANNNNVNNN NNNNNGPNSI
SSLIANVNPF TEEGRLQSLN KPCPSFQLVN NNNNNNNASN NNNDNNNNNN NNNNNNNNND
DTCNNNNNNS QNIDNNLITK FSLYKHTFQE LDLIGEGSFG HVYKVRHRID GCLYAIKKTK
KPLKGQKDRD IVLREVYGLS AIKDHTNIVR YFNAWEEDSH IFIQMEHCNG GNIYKWVTEH
IKQSESNLLL LAKQILTGIV YIHSLGLVHL DIKPENIYII YKCNQNQIIT NNNNTCSINN
SSNGSDSYFK SKIKTTENDL DNFITTTNSV NNNNCNNNNN NNVDNQNNNN QNNYLIIDGN
KINFNSITFK IGDLGLLNEA TNTKIYSEGD SRYLSRELLH DDMSALKKSD IFSLGCTLYE
LARCKPLPKS GMEWDSIRNG ILSFEKEDSI YDDNKNDFST EFWQLIKSMI HPDPSVRPSA
EQLLEHPLIK YGVIEIDDFE NEIETLKNLL AEKEKVLIIQ KEKQKLRQNQ LQQKMQQPNF
IELKQQPQQQ QEKQQMLHQQ KQQYLEQHNN NNDNNNNEFD ESEKEYQIQL EQFKIQKMQF
QLQQEQLQYQ HQHKHQNFFT KQICTASQIE GGIKNMAL
