MAK5_YEAST
ID MAK5_YEAST Reviewed; 773 AA.
AC P38112; D6VQD8;
DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1994, sequence version 1.
DT 03-AUG-2022, entry version 190.
DE RecName: Full=ATP-dependent RNA helicase MAK5;
DE EC=3.6.4.13;
DE AltName: Full=Maintenance of killer protein 5;
GN Name=MAK5; OrderedLocusNames=YBR142W; ORFNames=YBR1119;
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 204508 / S288c;
RX PubMed=7754712; DOI=10.1002/yea.320100911;
RA Zagulski M., Becam A.-M., Grzybowska E., Lacroute F., Migdalski A.,
RA Slonimski P.P., Sokolowska B., Herbert C.J.;
RT "The sequence of 12.5 kb from the right arm of chromosome II predicts a new
RT N-terminal sequence for the IRA1 protein and reveals two new genes, one of
RT which is a DEAD-box helicase.";
RL Yeast 10:1227-1234(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=7813418; DOI=10.1002/j.1460-2075.1994.tb06923.x;
RA Feldmann H., Aigle M., Aljinovic G., Andre B., Baclet M.C., Barthe C.,
RA Baur A., Becam A.-M., Biteau N., Boles E., Brandt T., Brendel M.,
RA Brueckner M., Bussereau F., Christiansen C., Contreras R., Crouzet M.,
RA Cziepluch C., Demolis N., Delaveau T., Doignon F., Domdey H.,
RA Duesterhus S., Dubois E., Dujon B., El Bakkoury M., Entian K.-D.,
RA Feuermann M., Fiers W., Fobo G.M., Fritz C., Gassenhuber J., Glansdorff N.,
RA Goffeau A., Grivell L.A., de Haan M., Hein C., Herbert C.J.,
RA Hollenberg C.P., Holmstroem K., Jacq C., Jacquet M., Jauniaux J.-C.,
RA Jonniaux J.-L., Kallesoee T., Kiesau P., Kirchrath L., Koetter P.,
RA Korol S., Liebl S., Logghe M., Lohan A.J.E., Louis E.J., Li Z.Y.,
RA Maat M.J., Mallet L., Mannhaupt G., Messenguy F., Miosga T., Molemans F.,
RA Mueller S., Nasr F., Obermaier B., Perea J., Pierard A., Piravandi E.,
RA Pohl F.M., Pohl T.M., Potier S., Proft M., Purnelle B., Ramezani Rad M.,
RA Rieger M., Rose M., Schaaff-Gerstenschlaeger I., Scherens B.,
RA Schwarzlose C., Skala J., Slonimski P.P., Smits P.H.M., Souciet J.-L.,
RA Steensma H.Y., Stucka R., Urrestarazu L.A., van der Aart Q.J.M.,
RA Van Dyck L., Vassarotti A., Vetter I., Vierendeels F., Vissers S.,
RA Wagner G., de Wergifosse P., Wolfe K.H., Zagulski M., Zimmermann F.K.,
RA Mewes H.-W., Kleine K.;
RT "Complete DNA sequence of yeast chromosome II.";
RL EMBO J. 13:5795-5809(1994).
RN [3]
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 [4]
RP FUNCTION.
RX PubMed=787537; DOI=10.1016/0022-2836(76)90102-9;
RA Wickner R.B., Leibowitz M.J.;
RT "Chromosomal genes essential for replication of a double-stranded RNA
RT plasmid of Saccharomyces cerevisiae: the killer character of yeast.";
RL J. Mol. Biol. 105:427-443(1976).
RN [5]
RP FUNCTION, SUBCELLULAR LOCATION, AND MUTAGENESIS OF GLY-218.
RX PubMed=13680366; DOI=10.1007/s00438-003-0913-4;
RA Zagulski M., Kressler D., Becam A.-M., Rytka J., Herbert C.J.;
RT "Mak5p, which is required for the maintenance of the M1 dsRNA virus, is
RT encoded by the yeast ORF YBR142w and is involved in the biogenesis of the
RT 60S subunit of the ribosome.";
RL Mol. Genet. Genomics 270:216-224(2003).
RN [6]
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 [7]
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 [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-135 AND SER-678, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ADR376;
RX PubMed=17330950; DOI=10.1021/pr060559j;
RA Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,
RA Elias J.E., Gygi S.P.;
RT "Large-scale phosphorylation analysis of alpha-factor-arrested
RT Saccharomyces cerevisiae.";
RL J. Proteome Res. 6:1190-1197(2007).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-138 AND SER-678, AND
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 [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-135; SER-138 AND SER-678, AND
RP IDENTIFICATION BY 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).
CC -!- FUNCTION: ATP-binding RNA helicase involved in the biogenesis of 60S
CC ribosomal subunits and is required for the normal formation of 25S and
CC 5.8S rRNAs. Required for the maintenance of dsRNA killer plasmid.
CC {ECO:0000269|PubMed:13680366, ECO:0000269|PubMed:787537}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.13;
CC -!- INTERACTION:
CC P38112; Q12389: DBP10; NbExp=3; IntAct=EBI-10394, EBI-5644;
CC P38112; Q03532: HAS1; NbExp=4; IntAct=EBI-10394, EBI-8170;
CC P38112; P43586: LOC1; NbExp=3; IntAct=EBI-10394, EBI-22906;
CC P38112; Q08208: NOP12; NbExp=3; IntAct=EBI-10394, EBI-35895;
CC P38112; P37838: NOP4; NbExp=4; IntAct=EBI-10394, EBI-12122;
CC P38112; P40693: RLP7; NbExp=3; IntAct=EBI-10394, EBI-15415;
CC P38112; P38805: RPF1; NbExp=3; IntAct=EBI-10394, EBI-24614;
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000269|PubMed:13680366,
CC ECO:0000269|PubMed:14562095}.
CC -!- DOMAIN: The Q motif is unique to and characteristic of the DEAD box
CC family of RNA helicases and controls ATP binding and hydrolysis.
CC -!- MISCELLANEOUS: Present with 981 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the DEAD box helicase family. DDX24/MAK5
CC subfamily. {ECO:0000305}.
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DR EMBL; Z36011; CAA85100.1; -; Genomic_DNA.
DR EMBL; X78937; CAA55539.1; -; Genomic_DNA.
DR EMBL; BK006936; DAA07258.1; -; Genomic_DNA.
DR PIR; S46011; S46011.
DR RefSeq; NP_009700.1; NM_001178490.1.
DR AlphaFoldDB; P38112; -.
DR SMR; P38112; -.
DR BioGRID; 32842; 413.
DR DIP; DIP-6337N; -.
DR IntAct; P38112; 60.
DR MINT; P38112; -.
DR STRING; 4932.YBR142W; -.
DR iPTMnet; P38112; -.
DR MaxQB; P38112; -.
DR PaxDb; P38112; -.
DR PRIDE; P38112; -.
DR EnsemblFungi; YBR142W_mRNA; YBR142W; YBR142W.
DR GeneID; 852439; -.
DR KEGG; sce:YBR142W; -.
DR SGD; S000000346; MAK5.
DR VEuPathDB; FungiDB:YBR142W; -.
DR eggNOG; KOG0347; Eukaryota.
DR GeneTree; ENSGT00550000074847; -.
DR HOGENOM; CLU_003041_13_0_1; -.
DR InParanoid; P38112; -.
DR OMA; HYHVPRT; -.
DR BioCyc; YEAST:G3O-29096-MON; -.
DR PRO; PR:P38112; -.
DR Proteomes; UP000002311; Chromosome II.
DR RNAct; P38112; protein.
DR GO; GO:0005730; C:nucleolus; IDA:SGD.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003724; F:RNA helicase activity; ISS:SGD.
DR GO; GO:0000466; P:maturation of 5.8S rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA); IMP:SGD.
DR GO; GO:0000463; P:maturation of LSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA); IMP:SGD.
DR GO; GO:0042273; P:ribosomal large subunit biogenesis; IMP:SGD.
DR Gene3D; 3.40.50.300; -; 2.
DR InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR000629; RNA-helicase_DEAD-box_CS.
DR InterPro; IPR014014; RNA_helicase_DEAD_Q_motif.
DR Pfam; PF00270; DEAD; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SUPFAM; SSF52540; SSF52540; 2.
DR PROSITE; PS00039; DEAD_ATP_HELICASE; 1.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
DR PROSITE; PS51195; Q_MOTIF; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Helicase; Hydrolase; Nucleotide-binding; Nucleus;
KW Phosphoprotein; Reference proteome; Ribosome biogenesis; RNA-binding;
KW rRNA processing.
FT CHAIN 1..773
FT /note="ATP-dependent RNA helicase MAK5"
FT /id="PRO_0000055048"
FT DOMAIN 202..399
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 452..615
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT REGION 73..99
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 114..144
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 171..199
FT /note="Q motif"
FT MOTIF 333..336
FT /note="DEAD box"
FT BINDING 215..222
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT MOD_RES 135
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 138
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 678
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198"
FT MUTAGEN 218
FT /note="G->D: Delays the appearance and decreases the level
FT of 25S rRNA."
FT /evidence="ECO:0000269|PubMed:13680366"
SQ SEQUENCE 773 AA; 87048 MW; C4FF2FB5B04FFBF9 CRC64;
MGKKRAPQKG KTVTKPQEII VDESKLNWKP VDIPDTLDDF GGFYGLEEID GVDVKVVDGK
VTFVTKKDSK VLKDSNKEKV GDDQESVENE SGSDSESELL EFKNLDDIKE GELSAASYSS
SDEDEQGNIE SSKLTDPSED VDEDVDEDVL KENVFNKDIN IDDISPVNLP EWTNLAPLSM
TILQSLQNLN FLRPTEIQKK SIPVIMQGVD VMGKASTGSG KTLAYGIPIV EKLISNFSQK
NKKPISLIFT PTRELAHQVT DHLKKICEPV LAKSQYSILS LTGGLSIQKQ QRLLKYDNSG
QIVIATPGRF LELLEKDNTL IKRFSKVNTL ILDEADRLLQ DGHFDEFEKI IKHLLVERRK
NRENSEGSSK IWQTLIFSAT FSIDLFDKLS SSRQVKDRRF KNNEDELNAV IQHLMSKIHF
NSKPVIIDTN PESKVSSQIK ESLIECPPLE RDLYCYYFLT MFPGTTLIFC NAIDSVKKLT
VYLNNLGIPA FQIHSSMTQK NRLKSLERFK QQSAKQKTIN HSNPDSVQLS TVLIASDVAA
RGLDIPGVQH VIHYHLPRST DIYIHRSGRT ARAGSEGVSA MICSPQESMG PLRKLRKTLA
TKNSVSTDLN SRSTNRKPIK WQNTVPLLPI ETDILSQLRE RSRLAGELAD HEIASNSLRK
DDNWLKKAAD ELGIDVDSDE DDISKSNSDT FLLKNKNKKM QKTINKDKVK AMRATLNELL
SVPIRKDRRQ KYLTGGLVNL ADNLVKKRGH NSIIGHEKTN ALETLKKKKK RNN
