KINY_DICDI
ID KINY_DICDI Reviewed; 579 AA.
AC Q54H05; Q9NFR9;
DT 25-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 03-AUG-2022, entry version 108.
DE RecName: Full=Probable serine/threonine-protein kinase kinY;
DE Short=DdKinY;
DE EC=2.7.11.1;
GN Name=kinY; ORFNames=DDB_G0289661;
OS Dictyostelium discoideum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=44689;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND DEVELOPMENTAL STAGE.
RC STRAIN=AX2;
RX PubMed=10899639; DOI=10.1016/s0167-4838(00)00070-4;
RA Wetterauer B.W.;
RT "Protein kinases from Dictyostelium discoideum with similarity to LIM
RT kinases.";
RL Biochim. Biophys. Acta 1480:377-383(2000).
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 -!- DEVELOPMENTAL STAGE: Weakly expressed in vegetative cells. Expression
CC increases during development until culmination. Higher levels detected
CC during aggregation and culmination. Enriched in prespore cells.
CC {ECO:0000269|PubMed:10899639}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. TKL Ser/Thr
CC protein kinase family. {ECO:0000305}.
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DR EMBL; AJ271978; CAB85705.1; -; mRNA.
DR EMBL; AAFI02000148; EAL62542.1; -; Genomic_DNA.
DR RefSeq; XP_636113.1; XM_631021.1.
DR AlphaFoldDB; Q54H05; -.
DR SMR; Q54H05; -.
DR STRING; 44689.DDB0191400; -.
DR PaxDb; Q54H05; -.
DR EnsemblProtists; EAL62542; EAL62542; DDB_G0289661.
DR GeneID; 8627327; -.
DR KEGG; ddi:DDB_G0289661; -.
DR dictyBase; DDB_G0289661; kinY.
DR eggNOG; KOG0192; Eukaryota.
DR HOGENOM; CLU_471291_0_0_1; -.
DR InParanoid; Q54H05; -.
DR OMA; FIGVYYE; -.
DR PhylomeDB; Q54H05; -.
DR PRO; PR:Q54H05; -.
DR Proteomes; UP000002195; Chromosome 5.
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 Pfam; PF00069; Pkinase; 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.
PE 2: Evidence at transcript level;
KW ATP-binding; Kinase; Nucleotide-binding; Reference proteome;
KW Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..579
FT /note="Probable serine/threonine-protein kinase kinY"
FT /id="PRO_0000355201"
FT DOMAIN 32..309
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 167
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 38..46
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 59
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT CONFLICT 87
FT /note="H -> Q (in Ref. 1; CAB85705)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 579 AA; 65629 MW; 18C900012B739745 CRC64;
MINGEQTMVE DELPDQGKPM SDESADIDIK DLKVGESIGS GAYGIVYRGT LFNSDVAIKK
IQNEKSEKNE FIKYLKREVA VLKNIQHPNI VQFIGVYYEP LASPSLVNRL LNSSSTWIVT
EYIGGGNLHE RIKDTKKDFP IELRIKLSLD IALAMAYLHS RDIIFRDLKS KNILIDDSSS
PIRGKVCDFG FARILNKKQQ GNRHLSICGT DSIMAPELIL GMEYDESVDI FSFGVVLLEM
ILRKKVSKVL ERGPQSAFEI DQDSARQLIP DDIPVLYSDL ALDCIKYQPE ERPNFSHIIH
VLKQLTSLFP VVHTFDNPLS PTSSPITPRK NSLNSPFTKS MRMNSFDFNL SNIVSSTSVQ
NNLKSQNLNF TLLNLNQINN QDLNENNNNN ISNNINNINN NNNNLNDCNS NLSSSTSTIY
NDSQQTIIDE DELDKEEEEN RNKVNNLKEK MLLVMGEFDI YINKVGKELL LVSEEDHISQ
KYDECRKVIE IKKVLGEVIE SDMSNSQQSN TPRKNSNVTN SRVALFLKSM ERSLNEIYSS
SDVLKQRIVK EDDLVESLLL ARVVSKIKKI HLSSLDINN
