FRK1_YEAST
ID FRK1_YEAST Reviewed; 865 AA.
AC Q03002; D6W3M7;
DT 16-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 170.
DE RecName: Full=Fatty acyl-CoA synthetase and RNA processing-associated kinase 1;
DE EC=2.7.11.1;
GN Name=FRK1; OrderedLocusNames=YPL141C;
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169875;
RA Bussey H., Storms R.K., Ahmed A., Albermann K., Allen E., Ansorge W.,
RA Araujo R., Aparicio A., Barrell B.G., Badcock K., Benes V., Botstein D.,
RA Bowman S., Brueckner M., Carpenter J., Cherry J.M., Chung E.,
RA Churcher C.M., Coster F., Davis K., Davis R.W., Dietrich F.S., Delius H.,
RA DiPaolo T., Dubois E., Duesterhoeft A., Duncan M., Floeth M., Fortin N.,
RA Friesen J.D., Fritz C., Goffeau A., Hall J., Hebling U., Heumann K.,
RA Hilbert H., Hillier L.W., Hunicke-Smith S., Hyman R.W., Johnston M.,
RA Kalman S., Kleine K., Komp C., Kurdi O., Lashkari D., Lew H., Lin A.,
RA Lin D., Louis E.J., Marathe R., Messenguy F., Mewes H.-W., Mirtipati S.,
RA Moestl D., Mueller-Auer S., Namath A., Nentwich U., Oefner P., Pearson D.,
RA Petel F.X., Pohl T.M., Purnelle B., Rajandream M.A., Rechmann S.,
RA Rieger M., Riles L., Roberts D., Schaefer M., Scharfe M., Scherens B.,
RA Schramm S., Schroeder M., Sdicu A.-M., Tettelin H., Urrestarazu L.A.,
RA Ushinsky S., Vierendeels F., Vissers S., Voss H., Walsh S.V., Wambutt R.,
RA Wang Y., Wedler E., Wedler H., Winnett E., Zhong W.-W., Zollner A.,
RA Vo D.H., Hani J.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XVI.";
RL Nature 387:103-105(1997).
RN [2]
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 [3]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=14562095; DOI=10.1038/nature02026;
RA Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA Weissman J.S., O'Shea E.K.;
RT "Global analysis of protein localization in budding yeast.";
RL Nature 425:686-691(2003).
RN [4]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
RA Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT "A multidimensional chromatography technology for in-depth phosphoproteome
RT analysis.";
RL Mol. Cell. Proteomics 7:1389-1396(2008).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-441, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19779198; DOI=10.1126/science.1172867;
RA Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
RT "Global analysis of Cdk1 substrate phosphorylation sites provides insights
RT into evolution.";
RL Science 325:1682-1686(2009).
RN [7]
RP INTERACTION WITH FAA3; POL5 AND TPA1.
RX PubMed=20489023; DOI=10.1126/science.1176495;
RA Breitkreutz A., Choi H., Sharom J.R., Boucher L., Neduva V., Larsen B.,
RA Lin Z.Y., Breitkreutz B.J., Stark C., Liu G., Ahn J., Dewar-Darch D.,
RA Reguly T., Tang X., Almeida R., Qin Z.S., Pawson T., Gingras A.C.,
RA Nesvizhskii A.I., Tyers M.;
RT "A global protein kinase and phosphatase interaction network in yeast.";
RL Science 328:1043-1046(2010).
CC -!- FUNCTION: Putative serine/threonine-protein kinase that may be involved
CC in rRNA transcription and ribosome biogenesis. {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 -!- SUBUNIT: Interacts with FAA3, POL5 and TPA1.
CC {ECO:0000269|PubMed:20489023}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14562095}.
CC -!- MISCELLANEOUS: Present with 556 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
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; U43703; AAB68219.1; -; Genomic_DNA.
DR EMBL; BK006949; DAA11293.1; -; Genomic_DNA.
DR PIR; S69044; S69044.
DR RefSeq; NP_015184.1; NM_001183955.1.
DR AlphaFoldDB; Q03002; -.
DR SMR; Q03002; -.
DR BioGRID; 36041; 163.
DR IntAct; Q03002; 20.
DR MINT; Q03002; -.
DR STRING; 4932.YPL141C; -.
DR iPTMnet; Q03002; -.
DR MaxQB; Q03002; -.
DR PaxDb; Q03002; -.
DR PRIDE; Q03002; -.
DR EnsemblFungi; YPL141C_mRNA; YPL141C; YPL141C.
DR GeneID; 855962; -.
DR KEGG; sce:YPL141C; -.
DR SGD; S000006062; FRK1.
DR VEuPathDB; FungiDB:YPL141C; -.
DR eggNOG; KOG0583; Eukaryota.
DR GeneTree; ENSGT00940000176459; -.
DR HOGENOM; CLU_002888_1_2_1; -.
DR InParanoid; Q03002; -.
DR OMA; YRYITRT; -.
DR BioCyc; YEAST:G3O-34039-MON; -.
DR PRO; PR:Q03002; -.
DR Proteomes; UP000002311; Chromosome XVI.
DR RNAct; Q03002; protein.
DR GO; GO:0005938; C:cell cortex; IBA:GO_Central.
DR GO; GO:0005737; C:cytoplasm; IDA:SGD.
DR GO; GO:0005524; F:ATP 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:0035556; P:intracellular signal transduction; IBA:GO_Central.
DR GO; GO:0006468; P:protein phosphorylation; HDA: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; Cytoplasm; Kinase; Nucleotide-binding; Phosphoprotein;
KW Reference proteome; Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..865
FT /note="Fatty acyl-CoA synthetase and RNA processing-
FT associated kinase 1"
FT /id="PRO_0000234367"
FT DOMAIN 41..313
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 341..398
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 480..554
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 673..733
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 754..782
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 348..364
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 378..398
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 673..708
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 765..781
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 175
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 47..55
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 80
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 441
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
SQ SEQUENCE 865 AA; 97693 MW; 57FA180D63D74D98 CRC64;
MSYTNKRHTY YGGFTNDLSD TFQYPQRTDE QRRKHVTFGP YILGSTLGEG EFGKVKLGWP
KNFSNSSNST FDFPKQVAIK LIKRDSISND YRKEVKIYRE INALKHLSHP NIVKLEEVLQ
NSRYIGIVLE YACGGEFYKY IQKKRRLKEM NACRLFSQLI SGVHYIHSKG LVHRDLKLEN
LLLDKNENLV ITDFGFVNEF CSRNELMKTS CGSPCYAAPE LVISAEPYEA RKADIWSCGV
ILYAILAGYL PWDDDPNNPE GSDIGRLYNY INSTPLKFPD YILPIPRDLL RRMLVSDPKK
RINLKQIKKH EWLKPHSSFL SITPDEWDKL NNTQSVFRLA KPRRRYGSRP QSSCSTSSLG
SRSDKRDSLV IDSTLITFPA PPQESQNHII TRPASIASDQ RLSPIRRSNR HNRSNSAASV
ALQAVVNADR EYVLSHEQSL SPVQNIRQTT GNMTASLSPP PAISPGDIII ETTPIKRNTI
SGSSIVPSLE EESSTTMQTS KIQPNNMASS QNHQYNKNKT QNSLQSAKNF YRTSSSSHTK
PRPTSYHPGS YTTPPYNSNT LSIYEINEKA KSSASSQTLN QRDTSPFDST PYLALDTCIT
SSSSIESSPK LITHGQFSVA KPSVDLQSVS GDLIKYKRDA DVVTRIYDEK YKQKRKSLRY
SGIFSDISCD TVTEESDELR PPESPLQQHE GQESIDKAKT EDTSEKGSKS SNIAKATAQK
HVNNHLERSL NEAESTKKRF SFLSLYSYDT SKSSLYSSMD SKRKPSPPSQ RRPKKDDSYQ
TNSKNHYITA SNMQTSHQVS KDLPAPTMVQ NKCTLETKKA VRSNRSSIMV SEVNKASVDN
KAAQSPEHST AKRVLGFFKR RSMKI
