LIMKA_DICDI
ID LIMKA_DICDI Reviewed; 650 AA.
AC Q54L00;
DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 03-AUG-2022, entry version 98.
DE RecName: Full=Probable LIM domain-containing serine/threonine-protein kinase DDB_G0287001;
DE EC=2.7.11.1;
GN ORFNames=DDB_G0287001;
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; AAFI02000095; EAL63927.1; -; Genomic_DNA.
DR RefSeq; XP_637432.1; XM_632340.1.
DR AlphaFoldDB; Q54L00; -.
DR SMR; Q54L00; -.
DR STRING; 44689.DDB0229940; -.
DR PaxDb; Q54L00; -.
DR EnsemblProtists; EAL63927; EAL63927; DDB_G0287001.
DR GeneID; 8625901; -.
DR KEGG; ddi:DDB_G0287001; -.
DR dictyBase; DDB_G0287001; -.
DR eggNOG; KOG0192; Eukaryota.
DR HOGENOM; CLU_421771_0_0_1; -.
DR InParanoid; Q54L00; -.
DR OMA; FDGQYLQ; -.
DR PRO; PR:Q54L00; -.
DR Proteomes; UP000002195; Chromosome 4.
DR GO; GO:0005737; C:cytoplasm; 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: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; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR InterPro; IPR001781; Znf_LIM.
DR Pfam; PF00412; LIM; 2.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR PRINTS; PR00109; TYRKINASE.
DR SMART; SM00132; LIM; 2.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS00478; LIM_DOMAIN_1; 2.
DR PROSITE; PS50023; LIM_DOMAIN_2; 2.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 3: Inferred from homology;
KW ATP-binding; Kinase; LIM domain; Metal-binding; Nucleotide-binding;
KW Reference proteome; Repeat; Serine/threonine-protein kinase; Transferase;
KW Zinc.
FT CHAIN 1..650
FT /note="Probable LIM domain-containing serine/threonine-
FT protein kinase DDB_G0287001"
FT /id="PRO_0000328052"
FT DOMAIN 4..63
FT /note="LIM zinc-binding 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00125"
FT DOMAIN 64..122
FT /note="LIM zinc-binding 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00125"
FT DOMAIN 386..643
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 118..138
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 171..197
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 293..320
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 509
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 392..400
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 413
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
SQ SEQUENCE 650 AA; 71668 MW; EF5350A4E003DB7A CRC64;
MDTNNCGVCK TIVNPGSERV KAGTSVFHAK CFVCKECKNE LESFIRSKDG SLICDECDIK
LNARKCFKCQ LPIQSTIVTA RGKSFHNDCF NCASCEKIIK GGFFFVEGEF YCSTCDAKPS
DKTKTTTPPP SEIPLPGKSG VSLANGVEIQ VPNNSTNIIY VLNTNESSNG LSSSGGSGNS
ISGSGGTNTG SSTSSFMIHK RNNSNELNVV TPTATTTVDL LTSSTTTTPT LSPSTLSPPI
STARFSNDYL ISLQDDIYAK QQQQLLLLQQ QQIQIQQQLQ QQQLEILQKN QSLLNSSSPS
PSTSSTSSTS SISQSQNLNT SQPNITQQLS NLNISNQKNG EIEKYIPKIN GKTLTELLKH
QSFDDILGEV LSKKISIYKE LSKEEVAFGD VIASGASGKV YKGIYKGRDV AIKVYSSENF
CFNIEEFDRE VTIMSLIDSD HPNFTRFYGA NKQNKKYLFH VSELVKSGSL RDLLLDKEKP
LAYFTQLSIA SDIANAMKHL HSIGVIHRDL KSLNVLITED FTAKVIDFGT SRNVDLAKQM
TLNLGTSCYM SPELFKGNGY DETCDVYAFG IVLWEIIARK EPYENINSWS IPVLVAKGER
PTIPADCPSE YSKLIKACWT DKPKKRPSFK EICDTLKKIS ESLTLKRNKK
