Y9956_DICDI
ID Y9956_DICDI Reviewed; 1385 AA.
AC Q55EI8;
DT 25-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 03-AUG-2022, entry version 96.
DE RecName: Full=Probable serine/threonine-protein kinase DDB_G0268876;
DE EC=2.7.11.1;
GN ORFNames=DDB_G0268876;
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; AAFI02000004; EAL73027.1; -; Genomic_DNA.
DR RefSeq; XP_647032.1; XM_641940.1.
DR AlphaFoldDB; Q55EI8; -.
DR STRING; 44689.DDB0229956; -.
DR PaxDb; Q55EI8; -.
DR EnsemblProtists; EAL73027; EAL73027; DDB_G0268876.
DR GeneID; 8616727; -.
DR KEGG; ddi:DDB_G0268876; -.
DR dictyBase; DDB_G0268876; -.
DR eggNOG; KOG0192; Eukaryota.
DR HOGENOM; CLU_255347_0_0_1; -.
DR InParanoid; Q55EI8; -.
DR OMA; CTIIDEL; -.
DR PRO; PR:Q55EI8; -.
DR Proteomes; UP000002195; Chromosome 1.
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 Gene3D; 1.25.10.10; -; 2.
DR Gene3D; 2.60.40.10; -; 1.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR017868; Filamin/ABP280_repeat-like.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR014756; Ig_E-set.
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 InterPro; IPR029071; Ubiquitin-like_domsf.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR PRINTS; PR00109; TYRKINASE.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF48371; SSF48371; 1.
DR SUPFAM; SSF54236; SSF54236; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR SUPFAM; SSF81296; SSF81296; 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..1385
FT /note="Probable serine/threonine-protein kinase
FT DDB_G0268876"
FT /id="PRO_0000355168"
FT DOMAIN 758..1008
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 1040..1074
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1091..1266
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1287..1339
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1052..1074
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1102..1148
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1149..1166
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1182..1266
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 878
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 764..772
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 1385 AA; 155503 MW; 2115E30FC55E17AF CRC64;
MRVLVHVNNA KQSGDGANNS NGTLINYNSN NKLFLEIHPN QSIWMIKTLL FNLFQIPPAR
QQLYLKVVDE INPRETSKAY SKLLQSYRLV KDYKIYEGTE LQMVALEKEI PSEFLVPPKK
TQSNSMEKLP HFTNLSMSSM SNMDEILSGS GGGRIHVLSS KKGEECPALC FAVGKGLYRG
ISGVIYEIKL YRVDSKGMLI VNTSLNFQID VIKKDSISVE DRKMAFTYEQ RKSDYSLLKL
QPIIYGEYSI SIKIDDTPIC GSPFHCTIID ELNPNLKELA FSNEWIEEVV QLITLMSNKP
STIDKLFSFG IEGLMNLMFY PDPTIQIHII GIFAKLIEKD KNKERVLKEF GMDFIFKLVS
LDNWSNFMEL RKLVASSLCI LSCYKPFLNR FFKEVGIDVI SLIARSDFID CPRSCAIFLS
RVSEISFELN EYLISDSIKE TLIYLLSIQD NITVNCTLKT ISNLSSSFDL KKESNIKLLS
NLLEYCKEFQ EISKKVLIFK SFSNFCVNES LCTFLISNGI LDLITPTHDK SGYFGIPMFC
QWESNTINYI ISNNNEINLK QYGYEFNQIF KEETDYVFFL SLTISNMLVS TTSLKIHDHF
SRGNGLNLLK QFIICHECSV RSEAFRSFMI ISNSPNDQCK KHLIQSGIIP YLVSSLFDSL
SVETPFIVNT LANLCKYDPT CVENMGVDDI DKFIELLHRD STSSLSKSIS YILSHLIRHD
KYKQRIVNGG GKLFLQYLIE FVRQGEISVL KYISQSDLEL TKEIGRGVSG VVKRGKWKGY
EIAVKQFNEE ELGFSEREFH SEATIMSVLR HDNIVHCVGG SAQPGKMYLV CDYYSRGSLY
SVITANICPL SNARIVHLAL QVAKGMNYLH SLGIIHRDLK PGNLLIDQDW NIRISDFGLS
RVVDNRMTKT VGTPCYMAVE VLKGLTDYSQ QADVYSFAFV LWECISRQIP YKDFAQIQWI
SMVLEDSFRP PIPDSCLPEF RDLITMCWTS NPDDRPSFQQ IITYLENLRL KMQDQGIYQI
LTGGSSVGIG GVGVVGVGSG GNSDEHESNI DIDTVSGSNN NESSTAVSLN ENKINIDMSM
HPTEELKNLV EVSKDDNPTN SDYDIRSSST SSSPSTLSAP QSPVGSTSPM GSTSTSPISN
NNNRPTHDHQ QPHQVKWERI VPDKPNPNLK SKRLSAFRNK AVPISITDNN NNNNSANNNN
NNNSMKNNSN ASRNTFSSVS SPSSSADLSS GIESSNNRDD SFLSSGSSLS EQHRSVSNSV
SNSVGGFSLP PPPLAPSFYA SMINEKISSS TPTDNNNNNN NNNNNNNNNN NNNNNNNNNN
NNNNNNNNSN NSINNNNNNG IAINYTNSIN NNKNSNNNTS NTKYPISKCK SNPSFEALKS
KFDKD
