SAMKC_DICDI
ID SAMKC_DICDI Reviewed; 875 AA.
AC Q55CW2;
DT 10-FEB-2009, integrated into UniProtKB/Swiss-Prot.
DT 02-MAY-2006, sequence version 2.
DT 03-AUG-2022, entry version 100.
DE RecName: Full=Probable serine/threonine-protein kinase samkC;
DE EC=2.7.11.1;
DE AltName: Full=SAM domain-containing protein kinase C;
GN Name=samkC; Synonyms=SAMK-C, smkC; ORFNames=DDB_G0270678;
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 -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane
CC protein {ECO:0000305}.
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; AAFI02000005; EAL72689.2; -; Genomic_DNA.
DR RefSeq; XP_646369.2; XM_641277.2.
DR AlphaFoldDB; Q55CW2; -.
DR SMR; Q55CW2; -.
DR STRING; 44689.DDB0229990; -.
DR PaxDb; Q55CW2; -.
DR EnsemblProtists; EAL72689; EAL72689; DDB_G0270678.
DR GeneID; 8617324; -.
DR KEGG; ddi:DDB_G0270678; -.
DR dictyBase; DDB_G0270678; samkC.
DR eggNOG; KOG0586; Eukaryota.
DR HOGENOM; CLU_328583_0_0_1; -.
DR InParanoid; Q55CW2; -.
DR OMA; CERCHTW; -.
DR PRO; PR:Q55CW2; -.
DR Proteomes; UP000002195; Chromosome 1.
DR GO; GO:0005813; C:centrosome; IBA:GO_Central.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
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; IBA:GO_Central.
DR GO; GO:0007059; P:chromosome segregation; IBA:GO_Central.
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 Pfam; PF00069; Pkinase; 1.
DR Pfam; PF07647; SAM_2; 1.
DR SUPFAM; SSF47769; SSF47769; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS50105; SAM_DOMAIN; 1.
PE 3: Inferred from homology;
KW ATP-binding; Coiled coil; Kinase; Membrane; Nucleotide-binding;
KW Reference proteome; Serine/threonine-protein kinase; Transferase;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..875
FT /note="Probable serine/threonine-protein kinase samkC"
FT /id="PRO_0000362032"
FT TRANSMEM 842..862
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 51..116
FT /note="SAM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00184"
FT DOMAIN 181..452
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 1..47
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 136..170
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 331..362
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 461..718
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 135..162
FT /evidence="ECO:0000255"
FT COILED 626..655
FT /evidence="ECO:0000255"
FT COMPBIAS 331..361
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 478..538
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 551..568
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 578..592
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 593..656
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 683..718
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 301
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 187..195
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 210
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
SQ SEQUENCE 875 AA; 99725 MW; D0DEAB7E425A45DB CRC64;
METTTITSIL DDNNNNNNNN NNNNNNNNNN NNNNNNNNNN NNNNNYNYKE WDNEMVCKWL
HDTKRIQKVS IEIFKANEIT GNYLESLTDK MLLKMGLTIR DLLSFRSEFD DLKNIFNETN
LYNNIQKNSI DYSIDNNNLN NLNNNNNNNN NNNNNNNNNN NNNNNNNNKT IKAPTIDISQ
YVFIKQMKGS VNCSLEKYIN KKTKERILIK RIGKSNINEE TIINEISILC SIDHPNIIKT
YGYYKDENYY YVASKFYPKG SIKTKSKSTP YNEINAKKVF GKVLKAIDYL HSLDPPIIHR
DINSDNILFD ENDEPILIDF GLSYKELKDD NNNDDDNYDN HNHNHNHNHN HNHDNDNDND
TNVKIKTQCM EPRWPSPEIH REPPHFSKES DIFSFGCTLF EILGYIITTP IIILPSIPSG
MSLECQILFN ETTKIDSCFR PTSKQLLNFS WFKETALLTS SEPQPLEPQP QPKPQTSQSK
PKPSSSLSSS ELPPQPPLES QSKPKPSQSK TQPTQPQSKL NPSSPPSSSS SSLSEPPKPQ
PSQSKPKPSS SLSSEPPPLE PQPKPQTSQS KPKPSSSLSS SEPPPLEPQP TQSSKPQPSQ
SKPQPIQSQP TQPQPTQPKS SKQQPQSKQQ QQQQQQQQQQ QQQQQQQQQQ QQKSKPEQSK
SKPEQSQSKP QPGQPLQSPS KPQPIPSTTK TTTTTTTTTT PNNNNNNNNN NNNNNNNNNN
NIITSINLIE CFKKNNSKII ISKDMEFDNP YEKTLHEKHL LKLGISDCKQ ININHKYFKK
VLSFLNSHLT SALQMKMGPY QVDIAPEFDN IFKTLFISLV LEKIDKDTLL KGGKDLGDTS
STLILYTFYY FLSNTLIYQI ILHKPTSFKL VGKLK
