ID   MRH4_ASPCL              Reviewed;         632 AA.
AC   A1CSR1;
DT   03-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT   03-APR-2007, sequence version 2.
DT   03-AUG-2022, entry version 72.
DE   RecName: Full=ATP-dependent RNA helicase mrh4, mitochondrial;
DE            EC=3.6.4.13;
DE   Flags: Precursor;
GN   Name=mrh4; ORFNames=ACLA_080320;
OS   Aspergillus clavatus (strain ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 /
OS   NRRL 1 / QM 1276 / 107).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Fumigati.
OX   NCBI_TaxID=344612;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 / NRRL 1;
RX   PubMed=18404212; DOI=10.1371/journal.pgen.1000046;
RA   Fedorova N.D., Khaldi N., Joardar V.S., Maiti R., Amedeo P., Anderson M.J.,
RA   Crabtree J., Silva J.C., Badger J.H., Albarraq A., Angiuoli S., Bussey H.,
RA   Bowyer P., Cotty P.J., Dyer P.S., Egan A., Galens K., Fraser-Liggett C.M.,
RA   Haas B.J., Inman J.M., Kent R., Lemieux S., Malavazi I., Orvis J.,
RA   Roemer T., Ronning C.M., Sundaram J.P., Sutton G., Turner G., Venter J.C.,
RA   White O.R., Whitty B.R., Youngman P., Wolfe K.H., Goldman G.H.,
RA   Wortman J.R., Jiang B., Denning D.W., Nierman W.C.;
RT   "Genomic islands in the pathogenic filamentous fungus Aspergillus
RT   fumigatus.";
RL   PLoS Genet. 4:E1000046-E1000046(2008).
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=EAW06348.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; DS027060; EAW06348.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; XP_001267774.1; XM_001267773.1.
DR   AlphaFoldDB; A1CSR1; -.
DR   SMR; A1CSR1; -.
DR   STRING; 5057.CADACLAP00007514; -.
DR   EnsemblFungi; EAW06348; EAW06348; ACLA_080320.
DR   GeneID; 4700092; -.
DR   KEGG; act:ACLA_080320; -.
DR   eggNOG; KOG0335; Eukaryota.
DR   OrthoDB; 1223767at2759; -.
DR   Proteomes; UP000006701; 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..37
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255"
FT   CHAIN           38..632
FT                   /note="ATP-dependent RNA helicase mrh4, mitochondrial"
FT                   /id="PRO_0000282708"
FT   DOMAIN          194..406
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT   DOMAIN          460..632
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT   REGION          49..111
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           141..174
FT                   /note="Q motif"
FT   MOTIF           353..356
FT                   /note="DEAD box"
FT   COMPBIAS        83..111
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         207..214
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ   SEQUENCE   632 AA;  70489 MW;  3525ECB127D3ADD1 CRC64;
     MNRLGRMSLP LRSPACLICQ TRTTTLIPSS WQTARSMATA RLRRKVSRMA LSPDVAKPSL
     NKDRKKRERP GPFAAMNQTE ARIRDTPRTR SQAALKRSGD SKEEAQKKES PLYKALKMQT
     TLAPVPYGKR TAVKAKIADI TSFDQFPLLP VVRNSIVSQA LPGLMEVTPT PIQRLAIPKL
     LEESKPDKKP VKTDDDEPHY DQFLLAAETG SGKTLAYLLP VVDAVKRAEA VDKELEKKEE
     EEKAREREEK MKNKAFDIEP ELPPLSNAGR PRAIILVPTS ELVAQVGVKV KALSHTVKYR
     SGMISSNLTP RRIKNTLFHP DGIDILVATP HLLASIAKTE PYLLSRVSHL VLDEADSLLD
     RSFAPTTTEI ISKVAPSLQK LILCSATIPR SLDNLLRKRY PDIKRLTTPN LHAIPRRVQL
     GVVDIEKDPY RGNRSLACAD VIWSIGKAGD SEVSGPYSSF LEPKTKKILV FVNEREEADE
     VAQFLQSKGI DAHSLSRDSS ARKQEEILAE FTEAPPPPSP DEIMLAQKQR RHEDPIPFEM
     PKRTNSGGST RRLPNTKVLV TTDLTSRGID TLAVKTVILY HVPHTTIDFI HRLGRLGRMG
     KRGRGVVLVG KKDRKDVVKE VREGMFRGQA LI