ID   MRH4_MAGO7              Reviewed;         651 AA.
AC   A4QTC6; G4N4G3;
DT   10-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT   15-MAY-2007, sequence version 1.
DT   03-AUG-2022, entry version 84.
DE   RecName: Full=ATP-dependent RNA helicase MRH4, mitochondrial;
DE            EC=3.6.4.13;
DE   Flags: Precursor;
GN   Name=MRH4; ORFNames=MGG_05112;
OS   Magnaporthe oryzae (strain 70-15 / ATCC MYA-4617 / FGSC 8958) (Rice blast
OS   fungus) (Pyricularia oryzae).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Sordariomycetidae; Magnaporthales; Pyriculariaceae; Pyricularia.
OX   NCBI_TaxID=242507;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=70-15 / ATCC MYA-4617 / FGSC 8958;
RX   PubMed=15846337; DOI=10.1038/nature03449;
RA   Dean R.A., Talbot N.J., Ebbole D.J., Farman M.L., Mitchell T.K.,
RA   Orbach M.J., Thon M.R., Kulkarni R., Xu J.-R., Pan H., Read N.D.,
RA   Lee Y.-H., Carbone I., Brown D., Oh Y.Y., Donofrio N., Jeong J.S.,
RA   Soanes D.M., Djonovic S., Kolomiets E., Rehmeyer C., Li W., Harding M.,
RA   Kim S., Lebrun M.-H., Bohnert H., Coughlan S., Butler J., Calvo S.E.,
RA   Ma L.-J., Nicol R., Purcell S., Nusbaum C., Galagan J.E., Birren B.W.;
RT   "The genome sequence of the rice blast fungus Magnaporthe grisea.";
RL   Nature 434:980-986(2005).
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; CM001233; EHA52831.1; -; Genomic_DNA.
DR   RefSeq; XP_003712638.1; XM_003712590.1.
DR   AlphaFoldDB; A4QTC6; -.
DR   SMR; A4QTC6; -.
DR   STRING; 318829.MGG_05112T0; -.
DR   PRIDE; A4QTC6; -.
DR   EnsemblFungi; MGG_05112T0; MGG_05112T0; MGG_05112.
DR   GeneID; 2675568; -.
DR   KEGG; mgr:MGG_05112; -.
DR   VEuPathDB; FungiDB:MGG_05112; -.
DR   eggNOG; KOG0335; Eukaryota.
DR   HOGENOM; CLU_003041_18_0_1; -.
DR   InParanoid; A4QTC6; -.
DR   OMA; FHALKMQ; -.
DR   OrthoDB; 1223767at2759; -.
DR   Proteomes; UP000009058; Chromosome 3.
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.
DR   PROSITE; PS51195; Q_MOTIF; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Helicase; Hydrolase; Mitochondrion; Nucleotide-binding;
KW   Reference proteome; RNA-binding; Transit peptide.
FT   TRANSIT         1..61
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255"
FT   CHAIN           62..651
FT                   /note="ATP-dependent RNA helicase MRH4, mitochondrial"
FT                   /id="PRO_0000294674"
FT   DOMAIN          234..445
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT   DOMAIN          494..651
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT   REGION          45..137
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          210..241
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           167..200
FT                   /note="Q motif"
FT   MOTIF           392..395
FT                   /note="DEAD box"
FT   COMPBIAS        59..91
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         247..254
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ   SEQUENCE   651 AA;  71018 MW;  BFC3AB6B8A8503DD CRC64;
     MLRSSLGSVC LACRISGNAG AAPGAVAYRP QLSTAIRGST IQLQSSLSFS TSNARQATRR
     ERTPSRMVLS DRVGRSTARD GDKKPRRRVD GPFAGMNRTV ANFDPETRSK LSRDNSNNNR
     SSKNGREGGK KLGRDGKGFK ALNMQRSLAS IGYGHRTTVK AKMQEVDSFD QFDLLPQVKD
     AVLNEALKGM LDIKPTPVQR LAIPALLGQT TGARSRWRTK SKPADSGSEA ASPDAPPPPR
     EEFLLAAETG SGKTLAYLVP AFNALKEAEA SDPDIIAYNQ RRAEERALLA KNPGSKIKTR
     PEPHPTMSRP RVVILVPTAE LVDQVGRVAK SLSHVAKART RMISANMSAT MIENDVFSPA
     GIDILISTPH LLASIAESHP NILSRVSHLV VDEADSLLDR SFSEVTTPII DRALPSIRQL
     VLCSATIPRR LDNYLASRFP NMRRITTPNL HAIPRRVQLG VIDVARDPYR GNKNIACADA
     IWSIGKEAGR HEGPVKGQVD VRRIMVFVNE REKTQEVAEY LKSKGIDAVA LHRDTSEERQ
     SEMLASFTSN ETMSIPTPEG GVAGSPRSSR TLPNTKVIVA TDLASRGIDT LAVRHVVLYD
     VPHTTIDFIH RLGRAGRMGR RGRGIVLVGN DDRKDIVAEV KESMFMGQAL V