STK11_DICDI
ID STK11_DICDI Reviewed; 586 AA.
AC Q54WJ0;
DT 20-JAN-2009, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 03-AUG-2022, entry version 107.
DE RecName: Full=Serine/threonine-protein kinase stk11 homolog;
DE EC=2.7.11.1;
DE AltName: Full=Liver kinase B1 homolog;
DE Short=lkb1;
GN Name=lkb1; ORFNames=DDB_G0279629;
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 -!- FUNCTION: Serine/threonine-protein kinase that controls the activity of
CC AMP-activated protein kinase (AMPK) family members, thereby playing a
CC role in various processes such as cell metabolism, cell polarity,
CC apoptosis and DNA damage response. Acts by phosphorylating the T-loop
CC of AMPK family proteins, leading to promote their activity (By
CC similarity). {ECO:0000250}.
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 -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. CAMK Ser/Thr
CC protein kinase family. LKB1 subfamily. {ECO:0000305}.
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DR EMBL; AAFI02000032; EAL67589.1; -; Genomic_DNA.
DR RefSeq; XP_641563.1; XM_636471.1.
DR AlphaFoldDB; Q54WJ0; -.
DR SMR; Q54WJ0; -.
DR STRING; 44689.DDB0229349; -.
DR PaxDb; Q54WJ0; -.
DR EnsemblProtists; EAL67589; EAL67589; DDB_G0279629.
DR GeneID; 8622138; -.
DR KEGG; ddi:DDB_G0279629; -.
DR dictyBase; DDB_G0279629; lkb1.
DR eggNOG; KOG0583; Eukaryota.
DR HOGENOM; CLU_465740_0_0_1; -.
DR InParanoid; Q54WJ0; -.
DR OMA; KIDIWAM; -.
DR PhylomeDB; Q54WJ0; -.
DR PRO; PR:Q54WJ0; -.
DR Proteomes; UP000002195; Chromosome 3.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0030295; F:protein kinase activator activity; IMP:dictyBase.
DR GO; GO:0004672; F:protein kinase activity; IDA:dictyBase.
DR GO; GO:0019887; F:protein kinase regulator activity; IMP:dictyBase.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; ISS:dictyBase.
DR GO; GO:0035556; P:intracellular signal transduction; IBA:GO_Central.
DR GO; GO:0010629; P:negative regulation of gene expression; IMP:dictyBase.
DR GO; GO:0010628; P:positive regulation of gene expression; IMP:dictyBase.
DR GO; GO:1901263; P:positive regulation of sorocarp spore cell differentiation; IMP:dictyBase.
DR GO; GO:0046777; P:protein autophosphorylation; IDA:dictyBase.
DR GO; GO:0006468; P:protein phosphorylation; IBA:GO_Central.
DR GO; GO:0031098; P:stress-activated protein kinase signaling cascade; IMP:dictyBase.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR Pfam; PF00069; Pkinase; 1.
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.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 3: Inferred from homology;
KW ATP-binding; Kinase; Magnesium; Manganese; Metal-binding;
KW Nucleotide-binding; Reference proteome; Serine/threonine-protein kinase;
KW Transferase.
FT CHAIN 1..586
FT /note="Serine/threonine-protein kinase stk11 homolog"
FT /id="PRO_0000358899"
FT DOMAIN 40..301
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 326..418
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 484..586
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 397..418
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 488..502
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 505..531
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 532..572
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 168
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 46..54
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 69
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
SQ SEQUENCE 586 AA; 66252 MW; C615B9E3911AF22D CRC64;
MEVEQQPSYT SNFIIHLNEN EDNGISYRSR KSTPKLVKHY ILGEVLGEGA YGKVKDGMDS
FTQKRVAVKI LKRARLKKIP GGEASVLKEI NITKKLHNKH IIKLIDHFII EEKGKLYIVY
EYVGGGTSQN ILENAPNGRL PPHQSQFIFR QLIEACEYIH SQKILHRDIK PDNILFTHAN
VLKLSDFGVA EDSSQLEDFE CLSRSYGSPA FQPPELTQFQ TTFSPFKIDI WAMGVTLYLM
TIGKFPFSGA NMFVLFENIS KCKIEFPNDL DKDLVNLIKG ILQVDHIQRF SLGQIKNHPW
CIKYIPEVEP FVPLLEESKF LPLEMAYGDD EGDDGGGGRG GGGDDELIFG YENDGNTIDL
QDPEYIPSIS VGDQPPSTPI LHSSDHHHHH HHNNQHQHQQ QQQQLQQSQQ FHGNGDNNLL
FDSNNNLIFD SNNNLLFNTN NNEHLINGLP VHPIELDPVN IKKSSIGTNI SDVALIRENY
ICSDNDASSG QDDEDYSDDN EISGEDLNPT NHHHHRADRV GSRDKSSRSS KRKNSSSNNN
NNNSTSPKVE FNPNRSSPQP PLRNSSNRRP KITFESPHNK SKCIIN
