ID   MRH4_ASPTN              Reviewed;         631 AA.
AC   Q0C9E8;
DT   03-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT   03-APR-2007, sequence version 2.
DT   03-AUG-2022, entry version 69.
DE   RecName: Full=ATP-dependent RNA helicase mrh4, mitochondrial;
DE            EC=3.6.4.13;
DE   Flags: Precursor;
GN   Name=mrh4; ORFNames=ATEG_09686;
OS   Aspergillus terreus (strain NIH 2624 / FGSC A1156).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Circumdati.
OX   NCBI_TaxID=341663;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NIH 2624 / FGSC A1156;
RA   Birren B.W., Lander E.S., Galagan J.E., Nusbaum C., Devon K., Henn M.,
RA   Ma L.-J., Jaffe D.B., Butler J., Alvarez P., Gnerre S., Grabherr M.,
RA   Kleber M., Mauceli E.W., Brockman W., Rounsley S., Young S.K., LaButti K.,
RA   Pushparaj V., DeCaprio D., Crawford M., Koehrsen M., Engels R.,
RA   Montgomery P., Pearson M., Howarth C., Larson L., Luoma S., White J.,
RA   Alvarado L., Kodira C.D., Zeng Q., Oleary S., Yandava C., Denning D.W.,
RA   Nierman W.C., Milne T., Madden K.;
RT   "Annotation of the Aspergillus terreus NIH2624 genome.";
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=EAU29877.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; CH476608; EAU29877.1; ALT_SEQ; Genomic_DNA.
DR   RefSeq; XP_001218308.1; XM_001218307.1.
DR   AlphaFoldDB; Q0C9E8; -.
DR   SMR; Q0C9E8; -.
DR   STRING; 341663.Q0C9E8; -.
DR   PRIDE; Q0C9E8; -.
DR   GeneID; 4354373; -.
DR   eggNOG; KOG0335; Eukaryota.
DR   OrthoDB; 1223767at2759; -.
DR   Proteomes; UP000007963; 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.
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..39
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255"
FT   CHAIN           40..631
FT                   /note="ATP-dependent RNA helicase mrh4, mitochondrial"
FT                   /id="PRO_0000282710"
FT   DOMAIN          196..408
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT   DOMAIN          442..631
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT   REGION          55..111
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          181..200
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           143..176
FT                   /note="Q motif"
FT   MOTIF           355..358
FT                   /note="DEAD box"
FT   COMPBIAS        182..200
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         209..216
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ   SEQUENCE   631 AA;  70349 MW;  BE5D4C3152B796F8 CRC64;
     MYPLGRVSLP VRSPVCLFCQ NRTSSLLPSA YVWQSARTMA SGRLRRKAAR MALSPNVAKT
     SLKKKRNDTD RFGPFAGMNQ TEARIRDDPR SRSPASLKRS KAPSDESGRK DSELYKALKM
     QTALAPIPYG RRSAIKAKIA EITSFDQFPL LPVVRHSIFS QALPGLHDVT PTPIQRVAIP
     RLLDDTNKDK KPKKRAEGEP EYDQYLLAAE TGSGKTLAYL IPLVNTVKQQ EAIEKEEQKR
     EEEEKAKERE EKLKNQAFDV EPELPPLSNA GRPRVIILVP TAELVAQVGA KVKTLSHTIK
     YRSGMISSNL TPRRIKNTLF NPDGIDILVT TPHLLASIAK TEPYVLSRVS HLVLDEADSL
     LDRSFQPITT EIIEKTSGSL QKLILCSATI PRSLDNFLRK KYPDIQRLTT PNLHAIPRRV
     QLGVVDIQKD PYRGNRNLAC ADVIWSIGKA GDSEPAGPFA SYQGPSVKKI LVFVNEREEA
     DEVAQFLRSK GIDAHSLSRD SSARRQEEIL AEFTEAGAPP SSEEIMLAQK KGRQDDAIPF
     EAPSKPHEPH KLPNTKVLVT TDIASRGIDT LAVKTVILYH VPHTTIDFIH RLGRLGRMNK
     RGRGIVLVGK KDRKDVVKEV REGMFRGQAL I