ID   MRH4_YARLI              Reviewed;         514 AA.
AC   Q6C3J3;
DT   04-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT   16-AUG-2004, sequence version 1.
DT   03-AUG-2022, entry version 96.
DE   RecName: Full=ATP-dependent RNA helicase MRH4, mitochondrial;
DE            EC=3.6.4.13;
DE   Flags: Precursor;
GN   Name=MRH4; OrderedLocusNames=YALI0E34353g;
OS   Yarrowia lipolytica (strain CLIB 122 / E 150) (Yeast) (Candida lipolytica).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Dipodascaceae; Yarrowia.
OX   NCBI_TaxID=284591;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CLIB 122 / E 150;
RX   PubMed=15229592; DOI=10.1038/nature02579;
RA   Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA   de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA   Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA   Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA   Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA   Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA   Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA   Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA   Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA   Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA   Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA   Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA   Weissenbach J., Wincker P., Souciet J.-L.;
RT   "Genome evolution in yeasts.";
RL   Nature 430:35-44(2004).
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; CR382131; CAG80376.1; -; Genomic_DNA.
DR   RefSeq; XP_504769.1; XM_504769.1.
DR   AlphaFoldDB; Q6C3J3; -.
DR   SMR; Q6C3J3; -.
DR   STRING; 4952.CAG80376; -.
DR   EnsemblFungi; CAG80376; CAG80376; YALI0_E34353g.
DR   GeneID; 2912236; -.
DR   KEGG; yli:YALI0E34353g; -.
DR   VEuPathDB; FungiDB:YALI0_E34353g; -.
DR   HOGENOM; CLU_003041_18_0_1; -.
DR   InParanoid; Q6C3J3; -.
DR   OMA; FHALKMQ; -.
DR   Proteomes; UP000001300; Chromosome E.
DR   GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
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:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0003724; F:RNA helicase activity; IEA:UniProtKB-EC.
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   3: Inferred from homology;
KW   ATP-binding; Helicase; Hydrolase; Mitochondrion; Nucleotide-binding;
KW   Reference proteome; RNA-binding; Transit peptide.
FT   TRANSIT         1..55
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255"
FT   CHAIN           56..514
FT                   /note="ATP-dependent RNA helicase MRH4, mitochondrial"
FT                   /id="PRO_0000232356"
FT   DOMAIN          150..328
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT   DOMAIN          359..514
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT   REGION          26..64
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           115..122
FT                   /note="Q motif"
FT   MOTIF           276..279
FT                   /note="DEAD box"
FT   BINDING         163..170
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ   SEQUENCE   514 AA;  58199 MW;  CAB1D4DBE58DA650 CRC64;
     MFANSLRRIT KPCLGVPDMA VRHIAMRPKP KVKVNSREGG GKGKPRPSTG VRRKPPGAQK
     QQPASIAING DAARRLLESK FAANISSFNE LKLHPDVRAV LPDVIQLPEH KQDQDIKPSI
     IQSLAVKIMR QSYTYKQRVK NEGEEPTVEK IPVDRQKTFV LAAQTGSGKT LAYLLPLLSD
     LKDQEKFPSW QLEKHYKTVR SVILVPTLEL SQQVGQVLKQ FEEPLGIKTF ASAFGQSHQE
     IAKAFNNRLD VLVTTPQKLQ QTREKNLGGA THLVVDEADT LFDTNFIDST TDVISQMPKL
     KCAAFVAATV SKSFLRKLRS FYPHVVVIAA PRLHAIPDHI RFSVVDVNKA PYYNNKKVAL
     LQALYAISHS QKQKNYVRRV VVFRNRKEHI PELKKFLEEN GYPVDTLHGK QDLHERNEVV
     EKYTNMPDAA DQTENARNVR VLLTTDIASR GMDMKNLRFV VLYDVPFDKT DFIHRVGRTG
     RFGREGEVYM FTDNQDKKAQ TNQLLHTSRN GLSL