RT103_YEAST
ID RT103_YEAST Reviewed; 409 AA.
AC Q05543; D6VSR9;
DT 12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 147.
DE RecName: Full=Regulator of Ty1 transposition protein 103;
GN Name=RTT103; OrderedLocusNames=YDR289C;
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=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 [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 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).
RN [4]
RP FUNCTION.
RX PubMed=11779788; DOI=10.1093/genetics/159.4.1449;
RA Scholes D.T., Banerjee M., Bowen B., Curcio M.J.;
RT "Multiple regulators of Ty1 transposition in Saccharomyces cerevisiae have
RT conserved roles in genome maintenance.";
RL Genetics 159:1449-1465(2001).
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 PCF11; RAI1; RAT1; RPO21 AND RBP2.
RX PubMed=15565157; DOI=10.1038/nature03041;
RA Kim M., Krogan N.J., Vasiljeva L., Rando O.J., Nedea E., Greenblatt J.F.,
RA Buratowski S.;
RT "The yeast Rat1 exonuclease promotes transcription termination by RNA
RT polymerase II.";
RL Nature 432:517-522(2004).
RN [8]
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).
CC -!- FUNCTION: Involved in transcription termination by RNA polymerase II
CC and in regulation of Ty1 transposition. {ECO:0000269|PubMed:11779788,
CC ECO:0000269|PubMed:15565157}.
CC -!- SUBUNIT: Interacts with PCF11, RAI1, RAT1, RPO21 AND RBP2.
CC {ECO:0000269|PubMed:15565157}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:14562095}.
CC -!- MISCELLANEOUS: Present with 3930 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the UPF0400 (RTT103) family. {ECO:0000305}.
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DR EMBL; U51031; AAB64467.1; -; Genomic_DNA.
DR EMBL; AY557793; AAS56119.1; -; Genomic_DNA.
DR EMBL; BK006938; DAA12129.1; -; Genomic_DNA.
DR PIR; S70119; S70119.
DR RefSeq; NP_010575.1; NM_001180597.1.
DR PDB; 2KM4; NMR; -; A=1-131.
DR PDB; 2L0I; NMR; -; A=3-131.
DR PDB; 5M48; X-ray; 2.59 A; A=141-246.
DR PDB; 5WOZ; NMR; -; A=5-131.
DR PDBsum; 2KM4; -.
DR PDBsum; 2L0I; -.
DR PDBsum; 5M48; -.
DR PDBsum; 5WOZ; -.
DR AlphaFoldDB; Q05543; -.
DR BMRB; Q05543; -.
DR SASBDB; Q05543; -.
DR SMR; Q05543; -.
DR BioGRID; 32342; 534.
DR DIP; DIP-2583N; -.
DR IntAct; Q05543; 6.
DR MINT; Q05543; -.
DR STRING; 4932.YDR289C; -.
DR iPTMnet; Q05543; -.
DR MaxQB; Q05543; -.
DR PaxDb; Q05543; -.
DR PRIDE; Q05543; -.
DR EnsemblFungi; YDR289C_mRNA; YDR289C; YDR289C.
DR GeneID; 851884; -.
DR KEGG; sce:YDR289C; -.
DR SGD; S000002697; RTT103.
DR VEuPathDB; FungiDB:YDR289C; -.
DR eggNOG; KOG2669; Eukaryota.
DR GeneTree; ENSGT00950000183094; -.
DR HOGENOM; CLU_053395_0_0_1; -.
DR InParanoid; Q05543; -.
DR OMA; KWLLSQY; -.
DR BioCyc; YEAST:G3O-29853-MON; -.
DR Reactome; R-SCE-6807505; RNA polymerase II transcribes snRNA genes.
DR EvolutionaryTrace; Q05543; -.
DR PRO; PR:Q05543; -.
DR Proteomes; UP000002311; Chromosome IV.
DR RNAct; Q05543; protein.
DR GO; GO:0000785; C:chromatin; IDA:SGD.
DR GO; GO:0016591; C:RNA polymerase II, holoenzyme; IBA:GO_Central.
DR GO; GO:0035861; C:site of double-strand break; IDA:SGD.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0000993; F:RNA polymerase II complex binding; IDA:SGD.
DR GO; GO:0031124; P:mRNA 3'-end processing; IMP:SGD.
DR GO; GO:0010526; P:negative regulation of transposition, RNA-mediated; IMP:SGD.
DR Gene3D; 1.25.40.90; -; 1.
DR InterPro; IPR006569; CID_dom.
DR InterPro; IPR008942; ENTH_VHS.
DR Pfam; PF04818; CID; 1.
DR SMART; SM00582; RPR; 1.
DR SUPFAM; SSF48464; SSF48464; 1.
DR PROSITE; PS51391; CID; 1.
PE 1: Evidence at protein level;
KW 3D-structure; DNA-binding; Nucleus; Reference proteome; Transcription;
KW Transcription regulation.
FT CHAIN 1..409
FT /note="Regulator of Ty1 transposition protein 103"
FT /id="PRO_0000268707"
FT DOMAIN 1..135
FT /note="CID"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00724"
FT REGION 249..409
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 262..290
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 309..325
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 337..384
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 390..409
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT HELIX 5..13
FT /evidence="ECO:0007829|PDB:2KM4"
FT HELIX 19..30
FT /evidence="ECO:0007829|PDB:2KM4"
FT HELIX 33..35
FT /evidence="ECO:0007829|PDB:2KM4"
FT HELIX 36..47
FT /evidence="ECO:0007829|PDB:2KM4"
FT STRAND 49..52
FT /evidence="ECO:0007829|PDB:2KM4"
FT HELIX 54..71
FT /evidence="ECO:0007829|PDB:2KM4"
FT HELIX 72..74
FT /evidence="ECO:0007829|PDB:2KM4"
FT HELIX 78..85
FT /evidence="ECO:0007829|PDB:2KM4"
FT HELIX 87..97
FT /evidence="ECO:0007829|PDB:2KM4"
FT HELIX 100..116
FT /evidence="ECO:0007829|PDB:2KM4"
FT HELIX 121..131
FT /evidence="ECO:0007829|PDB:2KM4"
FT HELIX 145..177
FT /evidence="ECO:0007829|PDB:5M48"
FT STRAND 182..184
FT /evidence="ECO:0007829|PDB:5M48"
FT HELIX 185..246
FT /evidence="ECO:0007829|PDB:5M48"
SQ SEQUENCE 409 AA; 46488 MW; 08D37739466E3010 CRC64;
MPFSSEQFTT KLNTLEDSQE SISSASKWLL LQYRDAPKVA EMWKEYMLRP SVNTRRKLLG
LYLMNHVVQQ AKGQKIIQFQ DSFGKVAAEV LGRINQEFPR DLKKKLSRVV NILKERNIFS
KQVVNDIERS LKTESSPVEA LVLPQKLKDF AKDYEKLVKM HHNVCAMKMR FDKSSDELDP
SSSVYEENFK TISKIGNMAK DIINESILKR ESGIHKLQST LDDEKRHLDE EQNMLSEIEF
VLSAKDPSRL NKNVDEDNII PTYEVGDGDD DDDDGDNDDD DDDDDDDKNY DDRSNDSNYG
VTNISTTDKK NEVVEKTDSE HKNSTHNPSD NQFGMKRTHD MIGHDDANDI PEKKVHLDSK
TSEDGTFNSE DGHYELDIEG HVGAQTDEGV ENSGGVSSSI QDLLSKLAN
