Y6627_DICDI
ID Y6627_DICDI Reviewed; 671 AA.
AC Q54LH8; Q23852; Q23853;
DT 05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 03-AUG-2022, entry version 93.
DE RecName: Full=Probable serine/threonine-protein kinase DDB_G0286627;
DE EC=2.7.11.1;
GN ORFNames=DDB_G0286627;
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).
RN [2] {ECO:0000305, ECO:0000312|EMBL:AAB54076.1}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 253-671.
RC STRAIN=AX3 / DH1 {ECO:0000312|EMBL:AAB54076.1};
RX PubMed=1976383; DOI=10.1021/bi00483a015;
RA Giorda R., Ohmachi T., Shaw D.R., Ennis H.L.;
RT "A shared internal threonine-glutamic acid-threonine-proline repeat defines
RT a family of Dictyostelium discoideum spore germination specific proteins.";
RL Biochemistry 29:7264-7269(1990).
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 Evidence={ECO:0000250|UniProtKB:Q869N2};
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; Evidence={ECO:0000250|UniProtKB:Q869N2};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:Q869N2};
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Single-pass membrane
CC protein {ECO:0000255}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. STE Ser/Thr
CC protein kinase family. {ECO:0000250|UniProtKB:Q869N2}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB54076.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=AAB54079.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AAFI02000089; EAL64069.1; -; Genomic_DNA.
DR EMBL; U20661; AAB54076.1; ALT_SEQ; Genomic_DNA.
DR EMBL; U20661; AAB54079.1; ALT_SEQ; Genomic_DNA.
DR RefSeq; XP_637583.1; XM_632491.1.
DR AlphaFoldDB; Q54LH8; -.
DR SMR; Q54LH8; -.
DR STRING; 44689.DDB0229378; -.
DR PaxDb; Q54LH8; -.
DR EnsemblProtists; EAL64069; EAL64069; DDB_G0286627.
DR GeneID; 8625723; -.
DR KEGG; ddi:DDB_G0286627; -.
DR dictyBase; DDB_G0286627; -.
DR eggNOG; KOG0201; Eukaryota.
DR HOGENOM; CLU_409639_0_0_1; -.
DR InParanoid; Q54LH8; -.
DR PhylomeDB; Q54LH8; -.
DR PRO; PR:Q54LH8; -.
DR Proteomes; UP000002195; Chromosome 4.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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:0007228; P:positive regulation of hh target transcription factor activity; IBA:GO_Central.
DR GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR InterPro; IPR045193; Fused-like.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR PANTHER; PTHR22983; PTHR22983; 1.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; SSF56112; 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; Membrane; Metal-binding;
KW Nucleotide-binding; Reference proteome; Serine/threonine-protein kinase;
KW Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..671
FT /note="Probable serine/threonine-protein kinase
FT DDB_G0286627"
FT /id="PRO_0000371252"
FT TRANSMEM 369..389
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 31..283
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 410..523
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 410..491
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 492..521
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 148
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:P28523,
FT ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-
FT ProRule:PRU10027"
FT BINDING 37..45
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P28523,
FT ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 61
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P28523,
FT ECO:0000255|PROSITE-ProRule:PRU00159"
FT CONFLICT 669..671
FT /note="GPN -> LMV (in Ref. 2; AAB54079)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 671 AA; 77102 MW; 8BD0180EC35051A7 CRC64;
MTDKYNDWVK NKKHNNYNMA EDPLYYIKSN WVIERQLSKG SFGQVYKAHK KLDPNFVCAI
KVIQYCKFTM KEVDYLKKLN DPKFVKYYSL EFNNSKTYAY IIMEFIEGES MKSIIENKKF
SDIEIKEIIK ELLKALVYLN DKGIMHRDLK PENIMFQNQN QNQNQNNKIN LKLIDFGLSK
AINENIINKT VKLQTISSVG TTLYMAPEIL LNNKGSNSSL DIWSLGCIIV EMKWGLNQLC
LQRPNNIPVF PVNSLFTEIL NLCFQTEPSK RIKSHQLIKH PFFNDENEQF YNDNKEYFDF
LKENERDSYI EIHNTESIGS NSTCSINEIR FENLYLIQST YENQYPIKTI TLHEKYTGIS
KLSHLNSKFK IIYLFLILLF LMTILVNLNR HVQTKFSIIQ RDNIFLSITP ESNPIKKPSP
TQSSDYNQYS EGSQSSYESS SSSESSSESS SSESSSSESS SSSESQSSEI NYSSNSNDLQ
PTDSSTTDPP VTDPPITDPP ITDPPVTDPP ITEPPVTETP KPTINPFFNT PVFICSQKID
QCLTVLNSQD LEFIDKKGRD QSMVLEYDGN AEQTFSIREK GGMYICLSGE HYHFSEKLKG
RLNANKDGRD CTFNLITQFN IDKQANLYSF RSPNDQYIQS DETTRFISTK PGGLGSQSQF
FIYFSHSLGP N
