LIMKB_DICDI
ID LIMKB_DICDI Reviewed; 966 AA.
AC P0CD62;
DT 09-FEB-2010, integrated into UniProtKB/Swiss-Prot.
DT 09-FEB-2010, sequence version 1.
DT 03-AUG-2022, entry version 48.
DE RecName: Full=Probable LIM domain-containing serine/threonine-protein kinase DDB_G0286997;
DE EC=2.7.11.1;
GN ORFNames=DDB_G0286997;
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; AAFI02000094; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AAFI02000095; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; P0CD62; -.
DR SMR; P0CD62; -.
DR dictyBase; DDB_G0286997; -.
DR InParanoid; P0CD62; -.
DR PRO; PR:P0CD62; -.
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; 1.
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; 1.
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..966
FT /note="Probable LIM domain-containing serine/threonine-
FT protein kinase DDB_G0286997"
FT /id="PRO_0000391335"
FT DOMAIN 3..62
FT /note="LIM zinc-binding 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00125"
FT DOMAIN 63..120
FT /note="LIM zinc-binding 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00125"
FT DOMAIN 702..959
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 208..291
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 331..588
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 208..287
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 331..411
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 416..430
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 431..447
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 448..476
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 488..512
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 513..532
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 556..576
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 825
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 708..716
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 729
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
SQ SEQUENCE 966 AA; 107219 MW; 8BFFAFEA68EA4E4E CRC64;
MDSRCGVCKY IISDCERYVS DNTFYHVKCF ICKICKCELP PCFRGKHASL MCGDCEIKLN
APKCFKSHFP IHSVSVVARN KEFHNNCFTC ISCNEIIKGG FQYSDELFYC SKCDIIKPPP
LPPPLIYKAP IATSKATTSI TSPLPTKIPI LSTANLIPPL SSSSPLATQI SPKTSTIATT
TVETTTAETT LPSPFKISQL KNSGDNIYSL SSPSSSSSSS SSSSSSSSSP PNTFNKSSDF
LRNPLNNNVK SSSSSIGGNF VNKSQQQQQP IDSCSKSSIS ISPSSPRPTE DDIKEQVFLL
QKQSVQLQIQ QQLQQRQIEQ LNKNQLGVQK PLNQQPQQQQ QQFKPQSPNL SNNDTLDSFS
NLNQSLPPPP LINTTTFSNP LLKTKNQSFP TPPTSHIIKE NQSQQIPKPS SIDEVDQLPL
PPPPITPIPS PSSSSIIINN QQQQQQESQL PPPPPTSIII DQSILLPPPP PSTEILPQQQ
SPKLYKPRPK PIVLPPPPLD MEQLPLPPPP LLSSQINQSL KSTQHNQTTS PTIEIPIPPP
LPIQKQSIPT RKPQLPQSSN PSPPSPPSPQ PSSNIPPLSP KQQQEQQVEP IFSPTGSIIP
TPPPPPPIFK MKPLRPQKFR APTNYIPSLS LHRANKLSNS TEDHIKPPES LVLESSRIEK
FEPTINGRKL TELLKHQTFD DIVGEVLNKR ISIYKQLVKD DVIFGDVIAA GASGKVYKGI
YKGRDVAIKV YSSENFCFNI DEFDREVTIM SLIDSDHPNF TRFYGANKQN KKYLFHVSEL
VKSGSLRDLL LDKEKPLLYF TQLSIASDIA NAMKHLHSIG VIHRDLKSLN VLITEDFTAK
VIDFGTSRNV DLAKHMTMNL GTSCYMSPEL FKGNGYDETC DVYAFGIVLW EIIARKEPYE
NINSWSIPVM VAKGDRPTIP ADCPSEYSKL IKACWTDKPK KRPSFKEICD TLKKISESLT
LKRNKK
