ID   MRH4_VANPO              Reviewed;         539 AA.
AC   A7TE77;
DT   13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT   02-OCT-2007, sequence version 1.
DT   03-AUG-2022, entry version 64.
DE   RecName: Full=ATP-dependent RNA helicase MRH4, mitochondrial;
DE            EC=3.6.4.13;
DE   Flags: Precursor;
GN   Name=MRH4; ORFNames=Kpol_1002p46;
OS   Vanderwaltozyma polyspora (strain ATCC 22028 / DSM 70294 / BCRC 21397 / CBS
OS   2163 / NBRC 10782 / NRRL Y-8283 / UCD 57-17) (Kluyveromyces polysporus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Vanderwaltozyma.
OX   NCBI_TaxID=436907;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 22028 / DSM 70294 / BCRC 21397 / CBS 2163 / NBRC 10782 / NRRL
RC   Y-8283 / UCD 57-17;
RX   PubMed=17494770; DOI=10.1073/pnas.0608218104;
RA   Scannell D.R., Frank A.C., Conant G.C., Byrne K.P., Woolfit M., Wolfe K.H.;
RT   "Independent sorting-out of thousands of duplicated gene pairs in two yeast
RT   species descended from a whole-genome duplication.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:8397-8402(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; DS480379; EDO19399.1; -; Genomic_DNA.
DR   RefSeq; XP_001647257.1; XM_001647207.1.
DR   AlphaFoldDB; A7TE77; -.
DR   SMR; A7TE77; -.
DR   STRING; 436907.A7TE77; -.
DR   EnsemblFungi; EDO19399; EDO19399; Kpol_1002p46.
DR   GeneID; 5547749; -.
DR   KEGG; vpo:Kpol_1002p46; -.
DR   eggNOG; KOG0335; Eukaryota.
DR   HOGENOM; CLU_003041_18_0_1; -.
DR   InParanoid; A7TE77; -.
DR   OMA; FHALKMQ; -.
DR   OrthoDB; 1223767at2759; -.
DR   PhylomeDB; A7TE77; -.
DR   Proteomes; UP000000267; 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   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   Reference proteome; RNA-binding; Transit peptide.
FT   TRANSIT         1..24
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255"
FT   CHAIN           25..539
FT                   /note="ATP-dependent RNA helicase MRH4, mitochondrial"
FT                   /id="PRO_0000310261"
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   MOTIF           81..109
FT                   /note="Q motif"
FT                   /evidence="ECO:0000250"
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   539 AA;  61264 MW;  AC828F72ADAD48A0 CRC64;
     MMTSRLPSCF GLRFYAKRAA TIRAKPSKLA SSVGIGAKRS KKTVKKKGKE VDIFNYGKYV
     GLKERDPGSE TKGKELLDKL SSFDQLKILP EVRNSIKNII KDETLSKKAK ESEDVIPSPI
     QLIAMKKLSR TLMDPKLQHH AIAAETGSGK TMAYLIPLFD YLKRQETEFP EDWEFMQDKA
     IIRSVIFLPT HELVDQVYNT VKKTENDLKF HVYKWDSGTK YPEIVEKLKN RIDILITTPA
     KLLNLFNIRM ISRADRLLSE VKFVVLDEAD TLLDKSWVED THRAIRSLPN TNHLLFCSAT
     IPNDFNDTLE RLFPNTIPIT TPRLHKLPKS VDFKIIDSSI NPFKGSKIKA LAQTLYAIAN
     DSSEPGFEKR CIVFTNEKKD VPYIVEKLKV TYGHDCIGLT SNDSVEERLE KIHDFITPPK
     PITMKKETPK IENEDSVEVE GSNITIGDFS SKTSVKNSNS ESSLKVLVST DLMARGLNFQ
     GVRNLVLYDV PQTSIDLIHR VGRTARMQQR GRVFMITDKK TKSWAKALPK VIKKNMTLK