ID   MRH4_YEAS7              Reviewed;         561 AA.
AC   A6ZUB2;
DT   13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT   11-SEP-2007, sequence version 1.
DT   03-AUG-2022, entry version 57.
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; ORFNames=SCY_1995;
OS   Saccharomyces cerevisiae (strain YJM789) (Baker's yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX   NCBI_TaxID=307796;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=YJM789;
RX   PubMed=17652520; DOI=10.1073/pnas.0701291104;
RA   Wei W., McCusker J.H., Hyman R.W., Jones T., Ning Y., Cao Z., Gu Z.,
RA   Bruno D., Miranda M., Nguyen M., Wilhelmy J., Komp C., Tamse R., Wang X.,
RA   Jia P., Luedi P., Oefner P.J., David L., Dietrich F.S., Li Y., Davis R.W.,
RA   Steinmetz L.M.;
RT   "Genome sequencing and comparative analysis of Saccharomyces cerevisiae
RT   strain YJM789.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:12825-12830(2007).
CC   -!- FUNCTION: ATP-binding RNA helicase involved in mitochondrial RNA
CC       metabolism. Required for maintenance of mitochondrial DNA (By
CC       similarity). {ECO:0000250}.
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:0000250}.
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   -!- SIMILARITY: Belongs to the DEAD box helicase family. MRH4 subfamily.
CC       {ECO:0000305}.
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DR   EMBL; AAFW02000099; EDN62050.1; -; Genomic_DNA.
DR   AlphaFoldDB; A6ZUB2; -.
DR   SMR; A6ZUB2; -.
DR   PRIDE; A6ZUB2; -.
DR   EnsemblFungi; EDN62050; EDN62050; SCY_1995.
DR   HOGENOM; CLU_003041_18_0_1; -.
DR   Proteomes; UP000007060; Unassembled WGS sequence.
DR   GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0003724; F:RNA helicase activity; IEA:UniProtKB-EC.
DR   GO; GO:0034641; P:cellular nitrogen compound metabolic process; IEA:UniProt.
DR   GO; GO:0043170; P:macromolecule metabolic process; IEA:UniProt.
DR   GO; GO:0044238; P:primary metabolic process; IEA:UniProt.
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   3: Inferred from homology;
KW   ATP-binding; Helicase; Hydrolase; Mitochondrion; Nucleotide-binding;
KW   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_0000310262"
FT   DOMAIN          131..319
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT   DOMAIN          350..539
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           98..129
FT                   /note="Q motif"
FT   MOTIF           267..270
FT                   /note="DEAD box"
FT   BINDING         144..151
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
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