ID   MRH4_AJECN              Reviewed;         624 AA.
AC   A6RCJ9;
DT   13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT   21-AUG-2007, sequence version 1.
DT   03-AUG-2022, entry version 64.
DE   RecName: Full=ATP-dependent RNA helicase MRH4, mitochondrial;
DE            EC=3.6.4.13;
DE   Flags: Precursor;
GN   Name=MRH4; ORFNames=HCAG_07357;
OS   Ajellomyces capsulatus (strain NAm1 / WU24) (Darling's disease fungus)
OS   (Histoplasma capsulatum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Ajellomycetaceae; Histoplasma;
OC   unclassified Histoplasma.
OX   NCBI_TaxID=2059318;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NAm1 / WU24;
RX   PubMed=19717792; DOI=10.1101/gr.087551.108;
RA   Sharpton T.J., Stajich J.E., Rounsley S.D., Gardner M.J., Wortman J.R.,
RA   Jordar V.S., Maiti R., Kodira C.D., Neafsey D.E., Zeng Q., Hung C.-Y.,
RA   McMahan C., Muszewska A., Grynberg M., Mandel M.A., Kellner E.M.,
RA   Barker B.M., Galgiani J.N., Orbach M.J., Kirkland T.N., Cole G.T.,
RA   Henn M.R., Birren B.W., Taylor J.W.;
RT   "Comparative genomic analyses of the human fungal pathogens Coccidioides
RT   and their relatives.";
RL   Genome Res. 19:1722-1731(2009).
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; CH476662; EDN10896.1; -; Genomic_DNA.
DR   RefSeq; XP_001537935.1; XM_001537885.1.
DR   AlphaFoldDB; A6RCJ9; -.
DR   SMR; A6RCJ9; -.
DR   STRING; 339724.A6RCJ9; -.
DR   EnsemblFungi; EDN10896; EDN10896; HCAG_07357.
DR   GeneID; 5443994; -.
DR   KEGG; aje:HCAG_07357; -.
DR   VEuPathDB; FungiDB:HCAG_07357; -.
DR   HOGENOM; CLU_003041_18_0_1; -.
DR   OMA; FHALKMQ; -.
DR   OrthoDB; 1223767at2759; -.
DR   Proteomes; UP000009297; 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; 2.
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..43
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255"
FT   CHAIN           44..624
FT                   /note="ATP-dependent RNA helicase MRH4, mitochondrial"
FT                   /id="PRO_0000310259"
FT   DOMAIN          212..427
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT   DOMAIN          438..624
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT   REGION          41..120
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           151..184
FT                   /note="Q motif"
FT   MOTIF           374..377
FT                   /note="DEAD box"
FT   COMPBIAS        89..120
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         225..232
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ   SEQUENCE   624 AA;  69935 MW;  060237C08EC478E4 CRC64;
     MSPVASTCLL CEMRTVVWGW QPAVPQPWHF VRFASSARLA RRKPARMALS PNVARSSDRF
     KDSKKKKPPP TFKNNPFGGM NQTRARLPDR PIPRSDAELK RSSSDLNNKE KDAADKKQDG
     SLFRALKMQI ALSPIPYSRR NRIKEKIAAV TSFDQFPLLP QVREAVYANA FPTLTEISPT
     PIQRVAIPAL LRPPISETEK NKRKKKPQEE EEEELFHFDQ FLLAAETGTG KTLAYLLPII
     NWIKQAEMVE KDTELMDNGE KQQGVTEKSK ENLFELEAPE LATPEHSNVA RPRAIILVPT
     AELVEQVGKL AKQLSHTAKF RSATISSVYT PRRITNSLFN PAGIDILIST PHLLTSIAKT
     NPYILSRVAH LVIDEADSLL DKSFSPLTYS IMEKTAPSLT QLILCSATIP RSLDSVMEKK
     FPEMKRLVTP NLHAIPRRVQ LGVVDVDKDP SRGNKKLACA DIIWSLGKAG EVAAFLSQKG
     IHTAALSRDT PDQRKDEILA EFTHVKPLPT PQEVKDAQRN KRNWFSDPVP FATGENSHLG
     PQRNLRDTKV LVTTDLGSRG IDTVAVRNVI LFDVPHTTID FIHRLGRTGR MGRRGRGIVL
     VSKKDRKDVV KEVREAMFRG QALI