SAMKB_DICDI
ID SAMKB_DICDI Reviewed; 593 AA.
AC Q54P26;
DT 10-FEB-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 samkB;
DE EC=2.7.11.1;
DE AltName: Full=SAM domain-containing protein kinase B;
GN Name=samkB; Synonyms=SAMK-B, smkB; ORFNames=DDB_G0284859;
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. Ser/Thr protein
CC kinase family. {ECO:0000255|PROSITE-ProRule:PRU00159}.
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DR EMBL; AAFI02000072; EAL65019.1; -; Genomic_DNA.
DR RefSeq; XP_638369.1; XM_633277.1.
DR AlphaFoldDB; Q54P26; -.
DR SMR; Q54P26; -.
DR STRING; 44689.DDB0229884; -.
DR PaxDb; Q54P26; -.
DR EnsemblProtists; EAL65019; EAL65019; DDB_G0284859.
DR GeneID; 8624802; -.
DR KEGG; ddi:DDB_G0284859; -.
DR dictyBase; DDB_G0284859; samkB.
DR eggNOG; KOG0198; Eukaryota.
DR HOGENOM; CLU_492983_0_0_1; -.
DR InParanoid; Q54P26; -.
DR PhylomeDB; Q54P26; -.
DR PRO; PR:Q54P26; -.
DR Proteomes; UP000002195; Chromosome 4.
DR GO; GO:0005524; F:ATP 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:0006468; P:protein phosphorylation; IEA:InterPro.
DR Gene3D; 1.10.150.50; -; 1.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR001660; SAM.
DR InterPro; IPR013761; SAM/pointed_sf.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF47769; SSF47769; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
DR PROSITE; PS50105; SAM_DOMAIN; 1.
PE 3: Inferred from homology;
KW ATP-binding; Kinase; Nucleotide-binding; Reference proteome;
KW Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..593
FT /note="Probable serine/threonine-protein kinase samkB"
FT /id="PRO_0000362031"
FT DOMAIN 29..93
FT /note="SAM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00184"
FT DOMAIN 186..438
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 108..157
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 313
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 192..200
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 216
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
SQ SEQUENCE 593 AA; 68549 MW; DB09FFADC78181A2 CRC64;
MDSTFDARAS NKSYLGSNSI ALTKNFEDWN NEAVCEWLSE NNFKMSDIEK FQENKIKGDH
LEFIGDKILI QMGLSIYERL SFKSIFKKLK NNNKIKIDST DNYKNECESN SINNSNNNNN
NNNNNNNNNN NNNNNNNNNN NNNNNNNNNN NNNKIDTFNS SIKQLNFSQE ANDPNIKAPI
LDINQYKLIE EIGRGAFSIV EKYENKLKPN EFISIKRINV LASEKEMIVK EINMLYSINH
PNIIKIIGYY KDEHYYYIAT PYYKKGSIAK IVKSIKSKNN SGFSESNVRN ISKKILNAID
YLHSSNPPIV HRDIKGDNIL LNDSDEPILA DFGLSYLAIE NNTNFKTACC SPFWAAPEIL
NKSTSDFSRK CDIYSFGCTI LEMIVGSDPW GGKRNHQSHS PPIPTYLTLE CKEVLNETLK
YNQNFRADSK QLLEAQWFKE TSLRNSSNGE IIFSSEDIMK EFKKNGSTIQ IGPVKQEYKY
KEQFDIENIS KWPREPSFID PKHKNYKEVL NLYDHYINHS PFMAKIGPYV LDLKEELNEK
TFYKSLAISS ILGKIDKYEP TTNQNLIPSL FFGFINFVLY QTIKHYPSKF RIL
