RCK1_YEAST
ID RCK1_YEAST Reviewed; 512 AA.
AC P38622; D6VTZ3;
DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1994, sequence version 1.
DT 03-AUG-2022, entry version 178.
DE RecName: Full=Serine/threonine-protein kinase RCK1;
DE EC=2.7.11.1;
GN Name=RCK1; OrderedLocusNames=YGL158W; ORFNames=G1854;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204510 / AB320;
RX PubMed=8112585; DOI=10.1016/0378-1119(94)90519-3;
RA Dahlkvist A., Sunnerhagen P.;
RT "Two novel deduced serine/threonine protein kinases from Saccharomyces
RT cerevisiae.";
RL Gene 139:27-33(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8585324; DOI=10.1002/yea.320111409;
RA James C.M., Indge K.J., Oliver S.G.;
RT "DNA sequence analysis of a 35 kb segment from Saccharomyces cerevisiae
RT chromosome VII reveals 19 open reading frames including RAD54, ACE1/CUP2,
RT PMR1, RCK1, AMS1 and CAL1/CDC43.";
RL Yeast 11:1413-1419(1995).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169869;
RA Tettelin H., Agostoni-Carbone M.L., Albermann K., Albers M., Arroyo J.,
RA Backes U., Barreiros T., Bertani I., Bjourson A.J., Brueckner M.,
RA Bruschi C.V., Carignani G., Castagnoli L., Cerdan E., Clemente M.L.,
RA Coblenz A., Coglievina M., Coissac E., Defoor E., Del Bino S., Delius H.,
RA Delneri D., de Wergifosse P., Dujon B., Durand P., Entian K.-D., Eraso P.,
RA Escribano V., Fabiani L., Fartmann B., Feroli F., Feuermann M.,
RA Frontali L., Garcia-Gonzalez M., Garcia-Saez M.I., Goffeau A.,
RA Guerreiro P., Hani J., Hansen M., Hebling U., Hernandez K., Heumann K.,
RA Hilger F., Hofmann B., Indge K.J., James C.M., Klima R., Koetter P.,
RA Kramer B., Kramer W., Lauquin G., Leuther H., Louis E.J., Maillier E.,
RA Marconi A., Martegani E., Mazon M.J., Mazzoni C., McReynolds A.D.K.,
RA Melchioretto P., Mewes H.-W., Minenkova O., Mueller-Auer S., Nawrocki A.,
RA Netter P., Neu R., Nombela C., Oliver S.G., Panzeri L., Paoluzi S.,
RA Plevani P., Portetelle D., Portillo F., Potier S., Purnelle B., Rieger M.,
RA Riles L., Rinaldi T., Robben J., Rodrigues-Pousada C.,
RA Rodriguez-Belmonte E., Rodriguez-Torres A.M., Rose M., Ruzzi M.,
RA Saliola M., Sanchez-Perez M., Schaefer B., Schaefer M., Scharfe M.,
RA Schmidheini T., Schreer A., Skala J., Souciet J.-L., Steensma H.Y.,
RA Talla E., Thierry A., Vandenbol M., van der Aart Q.J.M., Van Dyck L.,
RA Vanoni M., Verhasselt P., Voet M., Volckaert G., Wambutt R., Watson M.D.,
RA Weber N., Wedler E., Wedler H., Wipfli P., Wolf K., Wright L.F.,
RA Zaccaria P., Zimmermann M., Zollner A., Kleine K.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome VII.";
RL Nature 387:81-84(1997).
RN [4]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=17322287; DOI=10.1101/gr.6037607;
RA Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
RA Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J.,
RA Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J.,
RA Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D.,
RA LaBaer J.;
RT "Approaching a complete repository of sequence-verified protein-encoding
RT clones for Saccharomyces cerevisiae.";
RL Genome Res. 17:536-543(2007).
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 -!- INTERACTION:
CC P38622; P25379: CHA1; NbExp=2; IntAct=EBI-14880, EBI-3804607;
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; X71064; CAA50388.1; -; Genomic_DNA.
DR EMBL; Z48618; CAA88535.1; -; Genomic_DNA.
DR EMBL; Z72680; CAA96870.1; -; Genomic_DNA.
DR EMBL; AY723813; AAU09730.1; -; Genomic_DNA.
DR EMBL; BK006941; DAA07954.1; -; Genomic_DNA.
DR PIR; S47900; S47900.
DR RefSeq; NP_011357.1; NM_001181023.1.
DR AlphaFoldDB; P38622; -.
DR SMR; P38622; -.
DR BioGRID; 33096; 192.
DR DIP; DIP-1557N; -.
DR IntAct; P38622; 36.
DR MINT; P38622; -.
DR STRING; 4932.YGL158W; -.
DR iPTMnet; P38622; -.
DR PaxDb; P38622; -.
DR PRIDE; P38622; -.
DR EnsemblFungi; YGL158W_mRNA; YGL158W; YGL158W.
DR GeneID; 852719; -.
DR KEGG; sce:YGL158W; -.
DR SGD; S000003126; RCK1.
DR VEuPathDB; FungiDB:YGL158W; -.
DR eggNOG; KOG0032; Eukaryota.
DR GeneTree; ENSGT00940000176587; -.
DR HOGENOM; CLU_532266_0_0_1; -.
DR InParanoid; P38622; -.
DR OMA; MHYMGIV; -.
DR BioCyc; YEAST:G3O-30647-MON; -.
DR BRENDA; 2.7.11.1; 984.
DR PRO; PR:P38622; -.
DR Proteomes; UP000002311; Chromosome VII.
DR RNAct; P38622; protein.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0005516; F:calmodulin binding; IEA:UniProtKB-KW.
DR GO; GO:0004672; F:protein kinase activity; HDA:SGD.
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:0044773; P:mitotic DNA damage checkpoint signaling; IBA:GO_Central.
DR GO; GO:0006468; P:protein phosphorylation; HDA:SGD.
DR GO; GO:0040020; P:regulation of meiotic nuclear division; IMP:SGD.
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 1: Evidence at protein level;
KW ATP-binding; Calmodulin-binding; Kinase; Nucleotide-binding;
KW Reference proteome; Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..512
FT /note="Serine/threonine-protein kinase RCK1"
FT /id="PRO_0000086603"
FT DOMAIN 121..414
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 502..512
FT /note="Calmodulin-binding"
FT /evidence="ECO:0000255"
FT ACT_SITE 259
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 127..135
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 152
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
SQ SEQUENCE 512 AA; 57981 MW; 82053F80D5CE4B13 CRC64;
MSVNPEFIAD GIDFYPTTPD AAYFNAADGK NKVNRINGNS ENLHHSFASG CRRSSLSVDF
NVTSSDSEKS EQSCLENNSQ EDEYFCDIFS TELKLDETSN KSTDYSSSNH QYPEQLELHN
YKLLNKIGEG AFSRVFKAVG INTDDQAPVA IKAIIKKGIS SDAILKGNDR IQGSSRKKVL
NEVAIHKLVS KNNPHCTKFI AFQESANYYY LVTELVTGGE IFDRIVQLTC FSEDLARHVI
TQVAIAIKHM HYMGIVHRDV KPENLLFEPI PFYGLDGDMQ KEDEFTLGVG GGGIGLVKLM
DFGLAKKLRN NTAKTPCGTI EYVASEVFTS KRYSMKVDMW SIGCVLFTLL CGYPPFYEKN
EKTLLKKISR GDYEFLAPWW DNISSGAKNA VTHLLEVDPN KRYDIDDFLN DPWLNSYDCL
KDSNSNSYAS VQSILNDSFD ERAETLHCAL SCQSEKQDDT EFSRSESSEY IFMTEEDRNL
RGSWIGEPKE CFTLDLATSS IYRRRKNKIF FW
