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 02-NOV-2016, entry version 111.
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;
OC Saccharomycetes; 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.,
RA Paulin L., Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M.,
RA Prydz H., Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L.,
RA Rieger M., Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M.,
RA Scharfe M., Schmidt E.R., Schneider C., Scholler P., Schwarz S.,
RA Soler-Mira A., Urrestarazu L.A., Verhasselt P., Vissers S., Voet M.,
RA Volckaert G., Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S.,
RA Harris D.E., Bowman S., Brown D., Churcher C.M., Connor R., Dedman K.,
RA Gentles S., Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D.,
RA Niblett D., Odell C., Oliver K., Rajandream M.A., Richards C.,
RA Shore L., Walsh S.V., Barrell B.G., Dietrich F.S., Mulligan J.T.,
RA Allen E., Araujo R., Aviles E., Berno A., Carpenter J., Chen E.,
RA Cherry J.M., Chung E., Duncan M., Hunicke-Smith S., Hyman R.W.,
RA Komp C., Lashkari D., Lew H., Lin D., Mosedale D., Nakahara K.,
RA Namath A., Oefner P., Oh C., Petel F.X., Roberts D., Schramm S.,
RA Schroeder M., Shogren T., Shroff N., Winant A., Yelton M.A.,
RA Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R.,
RA Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S.,
RA Greco T., Hallsworth K., Hawkins J., Hillier L.W., Jier M.,
RA Johnson D., Johnston L., Kirsten J., Kucaba T., Langston Y.,
RA Latreille P., Le T., Mardis E., Menezes S., Miller N., Nhan M.,
RA Pauley A., Peluso D., Rifkin L., Riles L., Taich A., Trevaskis E.,
RA Vignati D., Wilcox L., Wohldman P., Vaudin M., Wilson R.,
RA 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.,
RA Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and
RT 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.,
RA Raphael J., Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F.,
RA Williamson J., Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G.,
RA Kolodner R.D., LaBaer J.;
RT "Approaching a complete repository of sequence-verified protein-
RT encoding clones for Saccharomyces cerevisiae.";
RL Genome Res. 17:536-543(2007).
RN [4]
RP FUNCTION.
RX PubMed=11779788;
RA Scholes D.T., Banerjee M., Bowen B., Curcio M.J.;
RT "Multiple regulators of Ty1 transposition in Saccharomyces cerevisiae
RT have 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.,
RA Dephoure N., 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.,
RA Greenblatt J.F., 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
RT phosphoproteome analysis.";
RL Mol. Cell. Proteomics 7:1389-1396(2008).
CC -!- FUNCTION: Involved in transcription termination by RNA polymerase
CC II and in regulation of Ty1 transposition.
CC {ECO:0000269|PubMed:11779788, 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
CC medium. {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the UPF0400 (RTT103) family. {ECO:0000305}.
CC -!- SIMILARITY: Contains 1 CID domain. {ECO:0000255|PROSITE-
CC ProRule:PRU00724}.
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 PDBsum; 2KM4; -.
DR PDBsum; 2L0I; -.
DR ProteinModelPortal; Q05543; -.
DR SMR; Q05543; -.
DR BioGrid; 32342; 307.
DR DIP; DIP-2583N; -.
DR IntAct; Q05543; 5.
DR MINT; MINT-425860; -.
DR iPTMnet; Q05543; -.
DR MaxQB; Q05543; -.
DR PRIDE; Q05543; -.
DR EnsemblFungi; YDR289C; YDR289C; YDR289C.
DR GeneID; 851884; -.
DR KEGG; sce:YDR289C; -.
DR EuPathDB; FungiDB:YDR289C; -.
DR SGD; S000002697; RTT103.
DR GeneTree; ENSGT00400000022016; -.
DR HOGENOM; HOG000141975; -.
DR InParanoid; Q05543; -.
DR KO; K15559; -.
DR OMA; HYELDIE; -.
DR OrthoDB; EOG092C38EY; -.
DR BioCyc; YEAST:G3O-29853-MONOMER; -.
DR EvolutionaryTrace; Q05543; -.
DR PRO; PR:Q05543; -.
DR Proteomes; UP000002311; Chromosome IV.
DR GO; GO:0000790; C:nuclear chromatin; IDA:SGD.
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 core binding; IDA:SGD.
DR GO; GO:0042769; P:DNA damage response, detection of DNA damage; IMP: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 GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:UniProtKB-KW.
DR GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
DR Gene3D; 1.25.40.90; -; 1.
DR InterPro; IPR006569; CID_dom.
DR InterPro; IPR008942; ENTH_VHS.
DR InterPro; IPR006903; RNA_pol_II-bd.
DR Pfam; PF04818; CTD_bind; 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; Complete proteome; DNA-binding; Nucleus;
KW Reference proteome; Transcription; Transcription regulation.
FT CHAIN 1 409 Regulator of Ty1 transposition protein
FT 103.
FT /FTId=PRO_0000268707.
FT DOMAIN 1 135 CID. {ECO:0000255|PROSITE-
FT ProRule:PRU00724}.
FT COMPBIAS 267 296 Asp-rich.
FT HELIX 5 13 {ECO:0000244|PDB:2KM4}.
FT HELIX 19 30 {ECO:0000244|PDB:2KM4}.
FT HELIX 33 35 {ECO:0000244|PDB:2KM4}.
FT HELIX 36 47 {ECO:0000244|PDB:2KM4}.
FT STRAND 49 52 {ECO:0000244|PDB:2KM4}.
FT HELIX 54 71 {ECO:0000244|PDB:2KM4}.
FT HELIX 72 74 {ECO:0000244|PDB:2KM4}.
FT HELIX 78 85 {ECO:0000244|PDB:2KM4}.
FT HELIX 87 97 {ECO:0000244|PDB:2KM4}.
FT HELIX 100 116 {ECO:0000244|PDB:2KM4}.
FT HELIX 121 131 {ECO:0000244|PDB:2KM4}.
CC --------------------------------------------------------------------------
CC The following FT lines are automated annotations from the MyHits database.
CC --------------------------------------------------------------------------
FT MYHIT 1 135 iprf:CID [T]
FT MYHIT 7 132 ismart:RPR [T]
FT MYHIT 57 119 ipfam:CTD_bind [T]
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
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