Y0133_DICDI
ID Y0133_DICDI Reviewed; 1090 AA.
AC Q54Y90;
DT 25-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 03-AUG-2022, entry version 92.
DE RecName: Full=Probable serine/threonine-protein kinase DDB_G0278665;
DE EC=2.7.11.1;
GN ORFNames=DDB_G0278665;
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. TKL Ser/Thr
CC protein kinase family. {ECO:0000305}.
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DR EMBL; AAFI02000023; EAL68505.1; -; Genomic_DNA.
DR RefSeq; XP_642312.1; XM_637220.1.
DR AlphaFoldDB; Q54Y90; -.
DR SMR; Q54Y90; -.
DR STRING; 44689.DDB0230133; -.
DR PaxDb; Q54Y90; -.
DR PRIDE; Q54Y90; -.
DR EnsemblProtists; EAL68505; EAL68505; DDB_G0278665.
DR GeneID; 8621518; -.
DR KEGG; ddi:DDB_G0278665; -.
DR dictyBase; DDB_G0278665; -.
DR eggNOG; KOG0192; Eukaryota.
DR HOGENOM; CLU_284761_0_0_1; -.
DR InParanoid; Q54Y90; -.
DR OMA; IKIDSKM; -.
DR PRO; PR:Q54Y90; -.
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: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 InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR PRINTS; PR00109; TYRKINASE.
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; Nucleotide-binding; Reference proteome;
KW Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..1090
FT /note="Probable serine/threonine-protein kinase
FT DDB_G0278665"
FT /id="PRO_0000355152"
FT DOMAIN 192..443
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 462..705
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 747..881
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 462..599
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 613..705
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 747..767
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 775..874
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 308
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 198..206
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 219
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
SQ SEQUENCE 1090 AA; 120397 MW; 36F9778CB24364AF CRC64;
MIYTSSDGDW FNPNEIDQDT DCDEELHHLL KFGIIEGKQI ESLKTLFFEQ TIEDRTKSQY
RARHSIFPNE DQPKYSVQFS KYHFDFNLKE GEKCKVGVTL KDKIKINSTG SGKTTFNFCN
IPVHSPNIKL TFTPSGGVIK KGQSVEILVE MVVLCTTRVR ELIAVDIANS GRHLFTIKID
SKMSQVLDYK ELEIGNVIGG GGYGAIYKAK WRGLSVAVKV ISELSDGSEF EKELEMHKEL
LHHPNIVHFV GFCVSPKCLV LEYIEGGSLD KYLHNPNYTF SPQLRLKMAN DIAKGMCFLH
RNEILHLDLK PQNFLVVSIS PEAPVSIKLA DFGLATSSSR SFYGPTVEGS FLYMSPEVFT
QKKFSRAADV WSYGACLIEI LTNKRPYQEY DQLGYLELAR VREEGLPPMI PPEIEGDLRK
IIEACFHRDH TKRPNFENIE QFLDAMTDSL FNVQSSIDSS SSLISSSPST INNNGSSSGS
SSTSTSPINT NNNNNNNNNN NINNINNNYN SNNSNNNSNN SNLIIQSANN VSSGSLMPSS
PGKTTPPLKH SGSFLFSRLQ QQQQYQQPAP VLSSHHPSSS SSSSSSSSSS SSSPSPPTTP
RKATGVPIPP FSLPSSLLQQ YQQNQLDKQL SSSPSNSSLT MSSSTPNQPP TPTQSNLNIV
STSPTSKPIV PLRTFLSSSN DSTCNNNNNN NNNNNNNNNN NNSNETLVKT SRAMTDLTLS
DTQKSGAVPS RSVTISGSSF IKPISIENNN VNSNNNNNNN IEATSPEKYN SHRPLPVLPT
SNSSNNLNGS IISTSNPSVS SSISQMSQLI SKQQQSQQQQ QQQQQNTPSR NVIIPNSSTA
NSSSSNLNIT TPTRPKPISS STSSSSTPQL PIGGNQHSHR PLPIRAASSF EIKNNHLNLS
SSPGDLFSSS PSTFEITMME RDTEDLTKLI ELRSRTLKCL KVLYYSFLDS IKSFSEIKEL
KDCIELGQKI RNFKKDVELQ CIEHLKLGWE TIHDASKKFN TNGKHLQTCP SPHPSNFDGE
TYNKVVQFRD AAVIVGESAL DGLFYLMLQL LPSHNNYRVP ILDITVSSTD KIPEKDLIVK
IAKIARSLKS
