MRX8_YEAST
ID MRX8_YEAST Reviewed; 314 AA.
AC Q05473; D6VSW8;
DT 17-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 143.
DE RecName: Full=MIOREX complex component 8 {ECO:0000305|PubMed:25683707};
DE AltName: Full=Mitochondrial organization of gene expression protein 8 {ECO:0000303|PubMed:25683707};
GN Name=MRX8 {ECO:0000303|PubMed:25683707};
GN OrderedLocusNames=YDR336W {ECO:0000312|SGD:S000002744};
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 SUMOYLATION [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RX PubMed=15166219; DOI=10.1074/jbc.m404173200;
RA Zhou W., Ryan J.J., Zhou H.;
RT "Global analyses of sumoylated proteins in Saccharomyces cerevisiae.
RT Induction of protein sumoylation by cellular stresses.";
RL J. Biol. Chem. 279:32262-32268(2004).
RN [4]
RP FUNCTION, AND SUBUNIT.
RX PubMed=25683707; DOI=10.1016/j.celrep.2015.01.012;
RA Kehrein K., Schilling R., Moller-Hergt B.V., Wurm C.A., Jakobs S.,
RA Lamkemeyer T., Langer T., Ott M.;
RT "Organization of mitochondrial gene expression in two distinct ribosome-
RT containing assemblies.";
RL Cell Rep. 10:843-853(2015).
CC -!- FUNCTION: Component of MIOREX complexes, large expressome-like
CC assemblies of ribosomes with factors involved in all the steps of post-
CC transcriptional gene expression. {ECO:0000269|PubMed:25683707}.
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU01043};
CC -!- SUBUNIT: Associates with the mitochondrial ribosome.
CC {ECO:0000269|PubMed:25683707}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000305|PubMed:25683707}.
CC -!- PTM: Sumoylated upon ethanol stress. {ECO:0000269|PubMed:15166219}.
CC -!- SIMILARITY: Belongs to the TRAFAC class TrmE-Era-EngA-EngB-Septin-like
CC GTPase superfamily. EngB GTPase family. {ECO:0000255|PROSITE-
CC ProRule:PRU01043}.
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DR EMBL; U51032; AAB64772.1; -; Genomic_DNA.
DR EMBL; BK006938; DAA12178.1; -; Genomic_DNA.
DR PIR; S70101; S70101.
DR RefSeq; NP_010623.3; NM_001180644.3.
DR AlphaFoldDB; Q05473; -.
DR SMR; Q05473; -.
DR BioGRID; 32393; 77.
DR STRING; 4932.YDR336W; -.
DR PaxDb; Q05473; -.
DR PRIDE; Q05473; -.
DR EnsemblFungi; YDR336W_mRNA; YDR336W; YDR336W.
DR GeneID; 851936; -.
DR KEGG; sce:YDR336W; -.
DR SGD; S000002744; MRX8.
DR VEuPathDB; FungiDB:YDR336W; -.
DR eggNOG; KOG2486; Eukaryota.
DR HOGENOM; CLU_062874_0_0_1; -.
DR InParanoid; Q05473; -.
DR OMA; FTKTINC; -.
DR BioCyc; YEAST:G3O-29892-MON; -.
DR PRO; PR:Q05473; -.
DR Proteomes; UP000002311; Chromosome IV.
DR RNAct; Q05473; protein.
DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR CDD; cd01876; YihA_EngB; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR030393; G_ENGB_dom.
DR InterPro; IPR006073; GTP-bd.
DR InterPro; IPR027417; P-loop_NTPase.
DR Pfam; PF01926; MMR_HSR1; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS51706; G_ENGB; 1.
PE 1: Evidence at protein level;
KW GTP-binding; Magnesium; Metal-binding; Mitochondrion; Nucleotide-binding;
KW Reference proteome; Ubl conjugation.
FT CHAIN 1..314
FT /note="MIOREX complex component 8"
FT /id="PRO_0000253817"
FT DOMAIN 132..312
FT /note="EngB-type G"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01043"
FT BINDING 140..147
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01043"
FT BINDING 147
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01043"
FT BINDING 173..177
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01043"
FT BINDING 175
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01043"
FT BINDING 191..194
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01043"
FT BINDING 253..256
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01043"
FT BINDING 290..292
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01043"
SQ SEQUENCE 314 AA; 35614 MW; 244A044799B87406 CRC64;
MEQLCKRYVH TPAAFIQNIV ANTKRTTLAT QLSVEKAKKK VPKTALKKKL NSRPKERLPN
WLKLNDVFNI HYEKPSNSDI NKVNRFFNKA KVEFEWCAAS FDDIPENPFL NKKSHKDILK
DHGECGTTLI DTLPEVIFLG GTNVGKSSIL NNITTSHVSR DLGSLARVSK TTGFTKTLNC
YNVGNRLRMI DSPGYGFNSS KEQGKVTLQY LLERKQLVRC FLLLAGDKEI NNTDNMIIQY
IHEHGVPFEV VFTKMDKVKD LNKFKKKVMS SGLMDLPTLP RLVLTNSLTS STSPKRFGID
LLRYVIFQSC GLIL
