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MRH4_ASHGO
ID   MRH4_ASHGO              Reviewed;         554 AA.
AC   Q755C5;
DT   21-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 102.
DE   RecName: Full=ATP-dependent RNA helicase MRH4, mitochondrial;
DE            EC=3.6.4.13;
DE   Flags: Precursor;
GN   Name=MRH4; OrderedLocusNames=AFL102W;
OS   Ashbya gossypii (strain ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056)
OS   (Yeast) (Eremothecium gossypii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Eremothecium.
OX   NCBI_TaxID=284811;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX   PubMed=15001715; DOI=10.1126/science.1095781;
RA   Dietrich F.S., Voegeli S., Brachat S., Lerch A., Gates K., Steiner S.,
RA   Mohr C., Poehlmann R., Luedi P., Choi S., Wing R.A., Flavier A.,
RA   Gaffney T.D., Philippsen P.;
RT   "The Ashbya gossypii genome as a tool for mapping the ancient Saccharomyces
RT   cerevisiae genome.";
RL   Science 304:304-307(2004).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX   PubMed=23749448; DOI=10.1534/g3.112.002881;
RA   Dietrich F.S., Voegeli S., Kuo S., Philippsen P.;
RT   "Genomes of Ashbya fungi isolated from insects reveal four mating-type
RT   loci, numerous translocations, lack of transposons, and distinct gene
RT   duplications.";
RL   G3 (Bethesda) 3:1225-1239(2013).
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; AE016819; AAS53272.1; -; Genomic_DNA.
DR   RefSeq; NP_985448.1; NM_210802.1.
DR   AlphaFoldDB; Q755C5; -.
DR   SMR; Q755C5; -.
DR   STRING; 33169.AAS53272; -.
DR   EnsemblFungi; AAS53272; AAS53272; AGOS_AFL102W.
DR   GeneID; 4621675; -.
DR   KEGG; ago:AGOS_AFL102W; -.
DR   eggNOG; KOG0335; Eukaryota.
DR   HOGENOM; CLU_003041_18_0_1; -.
DR   InParanoid; Q755C5; -.
DR   OMA; FHALKMQ; -.
DR   Proteomes; UP000000591; Chromosome VI.
DR   GO; GO:0005759; C:mitochondrial matrix; IEA:EnsemblFungi.
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; IEA:EnsemblFungi.
DR   GO; GO:0003724; F:RNA helicase activity; IEA:UniProtKB-EC.
DR   GO; GO:1902775; P:mitochondrial large ribosomal subunit assembly; IEA:EnsemblFungi.
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..54
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255"
FT   CHAIN           55..554
FT                   /note="ATP-dependent RNA helicase MRH4, mitochondrial"
FT                   /id="PRO_0000227962"
FT   DOMAIN          150..337
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT   DOMAIN          368..554
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT   REGION          439..474
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           119..140
FT                   /note="Q motif"
FT   MOTIF           285..288
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   554 AA;  62151 MW;  EEF0D3E178D690E7 CRC64;
     MSSVGIASAS LWLRGPVKSA LKGRWLSCEQ MRRYGTKSAP AVRKGGHSKK ARQAPSLPFV
     FGRHKQLTGP EFTRRTRIGN LSDKITKFEQ LKLLPEVREV MMKVIASESV LNKSLDDEDC
     GLDDKRVAAF LGQVQPTPIQ TAVIKKMAKT LMEPQLQVHM VAAETGSGKT MSYLMPLVDY
     LKQEEQAAGT EEGRARLGAL RSLILVPTHE LVEQVYMTLE KLQEPLQLKT FKLDRDTPYK
     DIVEAFKGRV DIMVTTPGKL RGLFKIRMLH RPDRILSQVR FAVVDEADTL MDQSWVQETY
     SCIKSLRDAN HLVFCSASVP MEFEKAMNKL FPNLQVVASE KLHRINKHSN IKIINVALRP
     YNGSKMKALA QALYAIMKDG TSEGYEKRCV VFVNEADSVN SIVDTLRDKF GHDVHGLTGE
     HSLDDRLATI APFMRSPPRI QDQVRPSELK KPQERRLPNS NIKVADSKDN GQRSVSSPLK
     VLVTTDVLSR GINFKGVKHV ILYDVPAKSI DLVHRVGRTS RMNERGHVYI FVGKKGSAQA
     KGLNPVVKKN RPIQ
 
 
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