SAMKA_DICDI
ID SAMKA_DICDI Reviewed; 640 AA.
AC Q55CW3;
DT 10-FEB-2009, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 03-AUG-2022, entry version 90.
DE RecName: Full=Probable serine/threonine-protein kinase samkA;
DE EC=2.7.11.1;
DE AltName: Full=SAM domain-containing protein kinase A;
GN Name=samkA; Synonyms=SAMK-A, smkA; ORFNames=DDB_G0269876;
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AAFI02000005; EAL72288.1; -; Genomic_DNA.
DR RefSeq; XP_646368.1; XM_641276.1.
DR AlphaFoldDB; Q55CW3; -.
DR SMR; Q55CW3; -.
DR STRING; 44689.DDB0231307; -.
DR PaxDb; Q55CW3; -.
DR EnsemblProtists; EAL72288; EAL72288; DDB_G0269876.
DR GeneID; 8617323; -.
DR KEGG; ddi:DDB_G0269876; -.
DR dictyBase; DDB_G0269876; samkA.
DR eggNOG; KOG0198; Eukaryota.
DR HOGENOM; CLU_492983_0_0_1; -.
DR InParanoid; Q55CW3; -.
DR OMA; IIRSESC; -.
DR PhylomeDB; Q55CW3; -.
DR PRO; PR:Q55CW3; -.
DR Proteomes; UP000002195; Chromosome 1.
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 InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
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.
PE 3: Inferred from homology;
KW ATP-binding; Coiled coil; Kinase; Nucleotide-binding; Reference proteome;
KW Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..640
FT /note="Probable serine/threonine-protein kinase samkA"
FT /id="PRO_0000362030"
FT DOMAIN 21..84
FT /note="SAM"
FT DOMAIN 191..437
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 84..165
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 448..482
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 73..100
FT /evidence="ECO:0000255"
FT COMPBIAS 448..463
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 312
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 197..205
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 221
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
SQ SEQUENCE 640 AA; 73515 MW; F7AA97AD2D9B54CD CRC64;
MDTSAVSYLS SIVLNNNYKE WNNEKIIKWL SDTKKIQKVI VFKIYEITGR DLEFLSDKIL
FKMGVGIRDL LSFKSEFEIL KNNYDNNNNN NNNNNNNNNN NNNNNNNNNN NNNNNNNNNN
NNNNNNNNNK NNNNSNSNST NINNNCSNNN SNNNHINFNS NSNITNIKNN DSKIKNKKEE
NKVPIIDLNQ YEYVESISLG VFSVVGKYKR KGQENEFIAI KKIDILSLNE EKIIKEINKL
YSINHPNIIK IIGYCKDQKN YYIASKYYPK GSIKKNTKQS PYSEMNAKRI SVKILSGIDY
LHSLNPPIIH RDIKCDNILL DENDDPILID FGLSYKTIDD STNLKTLCKK PFWASPDVNN
QEIQIFSEKT DIYSFGCTIF EMIVGWESYS KKENNQPNLQ KLPDNLTISC RLALGDIIGL
EQNFKPDSKD LQKLSWFNES LPPIFQSQEL TKSTTNTTTT TTTTTTPPPP PSPSSSSPSM
NENKKIVTSD CLINSFKESG CLIFLNGELM YDNPFDKDCY QYNIVIPFGT PHLREVIHKD
KNKSKHLDKI ELFIDDHLAK GLVIKLGNFK LDLSKEFKKT PTFIDSIIEY LLDLLQKDND
DDDDDDVPES IILNIAVGFY KYISNFITYQ YVLNQPSHFC
