NSI1_YEAST
ID NSI1_YEAST Reviewed; 570 AA.
AC Q12457; D6VS11;
DT 27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 170.
DE RecName: Full=RNA polymerase I termination factor {ECO:0000303|PubMed:22805593};
DE AltName: Full=NTS1 silencing protein 1 {ECO:0000303|PubMed:22362748};
GN Name=NSI1 {ECO:0000303|PubMed:22362748};
GN OrderedLocusNames=YDR026C {ECO:0000312|SGD:S000002433}; ORFNames=PZE570;
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].
RX PubMed=8896275;
RX DOI=10.1002/(sici)1097-0061(199609)12:10b<1085::aid-yea9>3.3.co;2-s;
RA Eide L.G., Sander C., Prydz H.;
RT "Sequencing and analysis of a 35.4 kb region on the right arm of chromosome
RT IV from Saccharomyces cerevisiae reveal 23 open reading frames.";
RL Yeast 12:1085-1090(1996).
RN [2]
RP ERRATUM OF PUBMED:8896275.
RA Eide L.G., Sander C., Prydz H.;
RL Yeast 13:189-189(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169867;
RA Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G.,
RA Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C.,
RA Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F.,
RA Delaveau T., del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M.,
RA Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T.,
RA Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C.,
RA Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S.,
RA Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L.,
RA Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H.,
RA Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M.,
RA Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M.,
RA Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A.,
RA Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G.,
RA Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E.,
RA Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S.,
RA Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D.,
RA Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V.,
RA Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E.,
RA Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M.,
RA Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D.,
RA Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X.,
RA Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A.,
RA Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R.,
RA Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T.,
RA Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L.,
RA Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E.,
RA Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L.,
RA Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M.,
RA Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K.,
RA Mewes H.-W., Zollner A., Zaccaria P.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV.";
RL Nature 387:75-78(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 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 [6]
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 [7]
RP FUNCTION, AND INTERACTION WITH FOB1.
RX PubMed=14576157; DOI=10.1074/jbc.m309078200;
RA Mohanty B.K., Bastia D.;
RT "Binding of the replication terminator protein Fob1p to the Ter sites of
RT yeast causes polar fork arrest.";
RL J. Biol. Chem. 279:1932-1941(2004).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-64, 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 [9]
RP FUNCTION.
RX PubMed=22805593; DOI=10.1038/emboj.2012.185;
RA Reiter A., Hamperl S., Seitz H., Merkl P., Perez-Fernandez J., Williams L.,
RA Gerber J., Nemeth A., Leger I., Gadal O., Milkereit P., Griesenbeck J.,
RA Tschochner H.;
RT "The Reb1-homologue Ydr026c/Nsi1 is required for efficient RNA polymerase I
RT termination in yeast.";
RL EMBO J. 31:3480-3493(2012).
RN [10]
RP FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH FOB1; NET1 AND SIR2, AND
RP DISRUPTION PHENOTYPE.
RX PubMed=22362748; DOI=10.1093/nar/gks188;
RA Ha C.W., Sung M.K., Huh W.K.;
RT "Nsi1 plays a significant role in the silencing of ribosomal DNA in
RT Saccharomyces cerevisiae.";
RL Nucleic Acids Res. 40:4892-4903(2012).
CC -!- FUNCTION: DNA-binding protein that recognizes sequence-specific
CC replication termini (Ter sites) within rDNA (PubMed:14576157). Binds to
CC rDNA terminator elements and mediates efficient RNA polymerase I
CC transcription termination (PubMed:22805593). Required for rDNA
CC silencing at the non-transcribed spacer 1 (NTS1). Promotes the
CC association of SIR2 with NTS1 and contributes to maintenance of rDNA
CC stability (PubMed:22362748). {ECO:0000269|PubMed:14576157,
CC ECO:0000269|PubMed:22362748, ECO:0000269|PubMed:22805593}.
CC -!- SUBUNIT: Interacts with FOB1 (PubMed:14576157, PubMed:22362748).
CC Interacts with the RENT complex subunits NET1 and SIR2
CC (PubMed:22362748). {ECO:0000269|PubMed:14576157,
CC ECO:0000269|PubMed:22362748}.
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000269|PubMed:14562095,
CC ECO:0000269|PubMed:22362748}.
CC -!- DISRUPTION PHENOTYPE: Decreases the association of SIR2 with NTS1,
CC decreases rDNA stability and shortens replicative lifespan.
CC {ECO:0000269|PubMed:22362748}.
CC -!- MISCELLANEOUS: Present with 432 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
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; X95966; CAA65219.1; -; Genomic_DNA.
DR EMBL; Z47814; CAA87805.1; -; Genomic_DNA.
DR EMBL; Z74322; CAA98848.1; -; Genomic_DNA.
DR EMBL; BK006938; DAA11871.1; -; Genomic_DNA.
DR PIR; S50933; S50933.
DR RefSeq; NP_010309.3; NM_001180334.3.
DR AlphaFoldDB; Q12457; -.
DR SMR; Q12457; -.
DR BioGRID; 32076; 117.
DR DIP; DIP-1814N; -.
DR IntAct; Q12457; 10.
DR MINT; Q12457; -.
DR STRING; 4932.YDR026C; -.
DR iPTMnet; Q12457; -.
DR MaxQB; Q12457; -.
DR PaxDb; Q12457; -.
DR PRIDE; Q12457; -.
DR EnsemblFungi; YDR026C_mRNA; YDR026C; YDR026C.
DR GeneID; 851590; -.
DR KEGG; sce:YDR026C; -.
DR SGD; S000002433; NSI1.
DR VEuPathDB; FungiDB:YDR026C; -.
DR eggNOG; KOG0051; Eukaryota.
DR GeneTree; ENSGT00940000176744; -.
DR HOGENOM; CLU_016706_0_0_1; -.
DR InParanoid; Q12457; -.
DR OMA; FWANISK; -.
DR BioCyc; YEAST:G3O-29642-MON; -.
DR PRO; PR:Q12457; -.
DR Proteomes; UP000002311; Chromosome IV.
DR RNAct; Q12457; protein.
DR GO; GO:0005730; C:nucleolus; IDA:SGD.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0033553; C:rDNA heterochromatin; IDA:SGD.
DR GO; GO:0003677; F:DNA binding; IDA:SGD.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IBA:GO_Central.
DR GO; GO:0000976; F:transcription cis-regulatory region binding; IBA:GO_Central.
DR GO; GO:0000183; P:rDNA heterochromatin assembly; IMP:SGD.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IBA:GO_Central.
DR GO; GO:0006363; P:termination of RNA polymerase I transcription; IDA:SGD.
DR CDD; cd00167; SANT; 3.
DR InterPro; IPR009057; Homeobox-like_sf.
DR InterPro; IPR017930; Myb_dom.
DR InterPro; IPR001005; SANT/Myb.
DR SMART; SM00717; SANT; 4.
DR SUPFAM; SSF46689; SSF46689; 1.
DR PROSITE; PS51294; HTH_MYB; 1.
DR PROSITE; PS50090; MYB_LIKE; 2.
PE 1: Evidence at protein level;
KW DNA-binding; Nucleus; Phosphoprotein; Reference proteome; Repeat.
FT CHAIN 1..570
FT /note="RNA polymerase I termination factor"
FT /id="PRO_0000242620"
FT DOMAIN 273..339
FT /note="Myb-like 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00133"
FT DOMAIN 340..391
FT /note="HTH myb-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00625"
FT DOMAIN 392..486
FT /note="Myb-like 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00133"
FT DOMAIN 493..549
FT /note="Myb-like 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00133"
FT DNA_BIND 367..389
FT /note="H-T-H motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00625"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 37..68
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 100..138
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..20
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 37..54
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 114..134
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 64
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:19779198"
SQ SEQUENCE 570 AA; 66352 MW; 48F42C8F428D989D CRC64;
MDSVSNLKST NFQNNNDPKE SVEEAVLRYV GVDLKNHIKK TKKKLKKQKK RKHGSKMSHE
DEDTDMDWYL KTSGSKDLRK VDDIEPNSVA VAAVAAAYNS SMREKDKRSC HKKSSNSRSE
RKKHRKRKSS KERKAKIKMV LDPQLTTLDD GITTTAFLPD DLIAETAFDK YVDTEKAYLA
KHPSKSLEVN EDDKENNFNN NSSTLVRIYT DLEGIPNDGS YIKRTPKIPE KDVKSDDLIL
APEENNGDTA LLRSDIVKAS VIDGAITKSI GKKFTPSEEN ALDQFIEEYM KIRGLDRRQM
CERIWSTDGV IRDGFWANIS KVLPYRTRSS IYKHIRRKYH IFEQRGKWTP EEDQELARLC
LEKEGHWTEV GKLLGRMPED CRDRWRNYMK CGSKRGSKRW SKEEEELLTT VVNEMIEEAH
QYQRMKALEA ANKNDRYNQM YSRGPKGKRI SDNPTFKDMI NWTVVSERMS GTRSRIQCRY
KWNKLVTDEA ARSMLSIPVS ERKWLLERLK QLPKTSYSNI DWNSIATYKP GYPRTGLELR
LCYEQMREKI HDFKGRSTAE IIDSLLEQIN
