MRH4_YEAST
ID MRH4_YEAST Reviewed; 561 AA.
AC P53166; D6VU77;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 186.
DE RecName: Full=ATP-dependent RNA helicase MRH4, mitochondrial;
DE EC=3.6.4.13;
DE AltName: Full=Mitochondrial RNA helicase 4;
DE Flags: Precursor;
GN Name=MRH4; OrderedLocusNames=YGL064C;
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=9234674;
RX DOI=10.1002/(sici)1097-0061(199707)13:9<861::aid-yea125>3.0.co;2-9;
RA Feuermann M., de Montigny J., Potier S., Souciet J.-L.;
RT "The characterization of two new clusters of duplicated genes suggests a
RT 'Lego' organization of the yeast Saccharomyces cerevisiae chromosomes.";
RL Yeast 13:861-869(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169869;
RA Tettelin H., Agostoni-Carbone M.L., Albermann K., Albers M., Arroyo J.,
RA Backes U., Barreiros T., Bertani I., Bjourson A.J., Brueckner M.,
RA Bruschi C.V., Carignani G., Castagnoli L., Cerdan E., Clemente M.L.,
RA Coblenz A., Coglievina M., Coissac E., Defoor E., Del Bino S., Delius H.,
RA Delneri D., de Wergifosse P., Dujon B., Durand P., Entian K.-D., Eraso P.,
RA Escribano V., Fabiani L., Fartmann B., Feroli F., Feuermann M.,
RA Frontali L., Garcia-Gonzalez M., Garcia-Saez M.I., Goffeau A.,
RA Guerreiro P., Hani J., Hansen M., Hebling U., Hernandez K., Heumann K.,
RA Hilger F., Hofmann B., Indge K.J., James C.M., Klima R., Koetter P.,
RA Kramer B., Kramer W., Lauquin G., Leuther H., Louis E.J., Maillier E.,
RA Marconi A., Martegani E., Mazon M.J., Mazzoni C., McReynolds A.D.K.,
RA Melchioretto P., Mewes H.-W., Minenkova O., Mueller-Auer S., Nawrocki A.,
RA Netter P., Neu R., Nombela C., Oliver S.G., Panzeri L., Paoluzi S.,
RA Plevani P., Portetelle D., Portillo F., Potier S., Purnelle B., Rieger M.,
RA Riles L., Rinaldi T., Robben J., Rodrigues-Pousada C.,
RA Rodriguez-Belmonte E., Rodriguez-Torres A.M., Rose M., Ruzzi M.,
RA Saliola M., Sanchez-Perez M., Schaefer B., Schaefer M., Scharfe M.,
RA Schmidheini T., Schreer A., Skala J., Souciet J.-L., Steensma H.Y.,
RA Talla E., Thierry A., Vandenbol M., van der Aart Q.J.M., Van Dyck L.,
RA Vanoni M., Verhasselt P., Voet M., Volckaert G., Wambutt R., Watson M.D.,
RA Weber N., Wedler E., Wedler H., Wipfli P., Wolf K., Wright L.F.,
RA Zaccaria P., Zimmermann M., Zollner A., Kleine K.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome VII.";
RL Nature 387:81-84(1997).
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=10077188;
RX DOI=10.1002/(sici)1097-0061(199902)15:3<219::aid-yea349>3.0.co;2-3;
RA Shiratori A., Shibata T., Arisawa M., Hanaoka F., Murakami Y., Eki T.;
RT "Systematic identification, classification, and characterization of the
RT open reading frames which encode novel helicase-related proteins in
RT Saccharomyces cerevisiae by gene disruption and Northern analysis.";
RL Yeast 15:219-253(1999).
RN [5]
RP FUNCTION, SUBCELLULAR LOCATION, AND VARIANTS SER-67 AND SER-438.
RC STRAIN=DBY947;
RX PubMed=12702275; DOI=10.1111/j.1567-1364.2002.tb00094.x;
RA Schmidt U., Lehmann K., Stahl U.;
RT "A novel mitochondrial DEAD box protein (Mrh4) required for maintenance of
RT mtDNA in Saccharomyces cerevisiae.";
RL FEMS Yeast Res. 2:267-276(2002).
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 SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RC STRAIN=ATCC 76625 / YPH499;
RX PubMed=14576278; DOI=10.1073/pnas.2135385100;
RA Sickmann A., Reinders J., Wagner Y., Joppich C., Zahedi R.P., Meyer H.E.,
RA Schoenfisch B., Perschil I., Chacinska A., Guiard B., Rehling P.,
RA Pfanner N., Meisinger C.;
RT "The proteome of Saccharomyces cerevisiae mitochondria.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:13207-13212(2003).
CC -!- FUNCTION: ATP-binding RNA helicase involved in mitochondrial RNA
CC metabolism. Required for maintenance of mitochondrial DNA.
CC {ECO:0000269|PubMed:10077188, ECO:0000269|PubMed:12702275}.
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 -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:12702275,
CC ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:14576278}.
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 736 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the DEAD box helicase family. MRH4 subfamily.
CC {ECO:0000305}.
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DR EMBL; Z72586; CAA96767.1; -; Genomic_DNA.
DR EMBL; BK006941; DAA08038.1; -; Genomic_DNA.
DR PIR; S64068; S64068.
DR RefSeq; NP_011451.1; NM_001180929.1.
DR AlphaFoldDB; P53166; -.
DR SMR; P53166; -.
DR BioGRID; 33183; 104.
DR DIP; DIP-6672N; -.
DR IntAct; P53166; 4.
DR MINT; P53166; -.
DR STRING; 4932.YGL064C; -.
DR iPTMnet; P53166; -.
DR MaxQB; P53166; -.
DR PaxDb; P53166; -.
DR PRIDE; P53166; -.
DR EnsemblFungi; YGL064C_mRNA; YGL064C; YGL064C.
DR GeneID; 852816; -.
DR KEGG; sce:YGL064C; -.
DR SGD; S000003032; MRH4.
DR VEuPathDB; FungiDB:YGL064C; -.
DR eggNOG; KOG0335; Eukaryota.
DR GeneTree; ENSGT00940000161738; -.
DR HOGENOM; CLU_003041_18_0_1; -.
DR InParanoid; P53166; -.
DR OMA; FHALKMQ; -.
DR BioCyc; YEAST:G3O-30570-MON; -.
DR PRO; PR:P53166; -.
DR Proteomes; UP000002311; Chromosome VII.
DR RNAct; P53166; protein.
DR GO; GO:0005759; C:mitochondrial matrix; IDA:SGD.
DR GO; GO:0005739; C:mitochondrion; IDA:SGD.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR GO; GO:1990400; F:mitochondrial ribosomal large subunit rRNA binding; IDA:SGD.
DR GO; GO:0003724; F:RNA helicase activity; IMP:SGD.
DR GO; GO:1902775; P:mitochondrial large ribosomal subunit assembly; IMP:SGD.
DR GO; GO:0016070; P:RNA metabolic process; IMP:SGD.
DR GO; GO:0006364; P:rRNA processing; IBA:GO_Central.
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 Pfam; PF00270; DEAD; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Helicase; Hydrolase; Mitochondrion; Nucleotide-binding;
KW Reference proteome; RNA-binding; Transit peptide.
FT TRANSIT 1..26
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 27..561
FT /note="ATP-dependent RNA helicase MRH4, mitochondrial"
FT /id="PRO_0000041929"
FT DOMAIN 151..339
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 370..561
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT REGION 29..72
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 117..141
FT /note="Q motif"
FT MOTIF 287..290
FT /note="DEAD box"
FT BINDING 164..171
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT VARIANT 67
FT /note="P -> S (in strain: DBY947)"
FT /evidence="ECO:0000269|PubMed:12702275"
FT VARIANT 438
FT /note="P -> S (in strain: DBY947)"
FT /evidence="ECO:0000269|PubMed:12702275"
SQ SEQUENCE 561 AA; 63058 MW; A8CEE92D461DB6EC CRC64;
MSLFFKPVIS PQWSFPVLLK IGVRSYAGGP RTKHKGNSPL ASVPTGSSNK NRKQKAKGKK
GNKKNDPDQA FNFGEYGGLK KDVEMNMDST NKLIQKISNF DQLLILPPVR DAVKEIISKE
SLKLQDSRKK TSENIIPSPI QTVAIKRISK NLMDPKLQIH AIAAETGSGK TMAYLIPLID
YLKRQELETP ELWETLRKNV LIRSIILVPT HELVDQVYET VSKTKTLLGL NSFKWDKATS
YRDLLENIKN RIDILVTTPG KLLNLFSIRM ITRPDKVLSK VGFVVLDEAD TLLDRSWLEE
THSAIKRIPN INHLIFCSAT IPQEFNKTMQ RLFPTVVPIM TPRLHKLPFA LDFKVINSAL
SPFKGSKIKA LAQTLYAISN DDTEPGFEKR CIIFVNEKKN VPEIVNLLNK KFGHNAIGLT
GEDTFEERSE KIMPFLSPPR PLSEVVAQST SPPTSLKKFE IPDSNIVIGK LKNTNSNGTA
PSNKSLHVLV TTDLMARGLN FKGVRNVVLY DVPKTSIDLI HRVGRTARMK QGGRVFMLTD
SKTKSWAKAL PKIIKKHQRL S
