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Database: UniProt
Entry: A5E5F7
LinkDB: A5E5F7
Original site: A5E5F7 
ID   MRH4_LODEL              Reviewed;         603 AA.
AC   A5E5F7;
DT   10-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT   12-JUN-2007, sequence version 1.
DT   16-OCT-2019, entry version 60.
DE   RecName: Full=ATP-dependent RNA helicase MRH4, mitochondrial;
DE            EC=3.6.4.13;
DE   Flags: Precursor;
GN   Name=MRH4; ORFNames=LELG_04846;
OS   Lodderomyces elongisporus (strain ATCC 11503 / CBS 2605 / JCM 1781 /
OS   NBRC 1676 / NRRL YB-4239) (Yeast) (Saccharomyces elongisporus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
OC   Saccharomycetes; Saccharomycetales; Debaryomycetaceae;
OC   Candida/Lodderomyces clade; Lodderomyces.
OX   NCBI_TaxID=379508;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 11503 / CBS 2605 / JCM 1781 / NBRC 1676 / NRRL YB-4239;
RX   PubMed=19465905; DOI=10.1038/nature08064;
RA   Butler G., Rasmussen M.D., Lin M.F., Santos M.A.S., Sakthikumar S.,
RA   Munro C.A., Rheinbay E., Grabherr M., Forche A., Reedy J.L.,
RA   Agrafioti I., Arnaud M.B., Bates S., Brown A.J.P., Brunke S.,
RA   Costanzo M.C., Fitzpatrick D.A., de Groot P.W.J., Harris D.,
RA   Hoyer L.L., Hube B., Klis F.M., Kodira C., Lennard N., Logue M.E.,
RA   Martin R., Neiman A.M., Nikolaou E., Quail M.A., Quinn J.,
RA   Santos M.C., Schmitzberger F.F., Sherlock G., Shah P.,
RA   Silverstein K.A.T., Skrzypek M.S., Soll D., Staggs R., Stansfield I.,
RA   Stumpf M.P.H., Sudbery P.E., Srikantha T., Zeng Q., Berman J.,
RA   Berriman M., Heitman J., Gow N.A.R., Lorenz M.C., Birren B.W.,
RA   Kellis M., Cuomo C.A.;
RT   "Evolution of pathogenicity and sexual reproduction in eight Candida
RT   genomes.";
RL   Nature 459:657-662(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
CC       box family of RNA helicases and controls ATP binding and
CC       hydrolysis.
CC   -!- SIMILARITY: Belongs to the DEAD box helicase family. MRH4
CC       subfamily. {ECO:0000305}.
DR   EMBL; CH981530; EDK46665.1; -; Genomic_DNA.
DR   RefSeq; XP_001524033.1; XM_001523983.1.
DR   STRING; 36914.XP_001524033.1; -.
DR   PRIDE; A5E5F7; -.
DR   EnsemblFungi; EDK46665; EDK46665; LELG_04846.
DR   GeneID; 5231117; -.
DR   KEGG; lel:LELG_04846; -.
DR   eggNOG; KOG0335; Eukaryota.
DR   eggNOG; ENOG410XNTI; LUCA.
DR   InParanoid; A5E5F7; -.
DR   KO; K17678; -.
DR   OMA; WDLDSNF; -.
DR   OrthoDB; 1223767at2759; -.
DR   Proteomes; UP000001996; Unassembled WGS sequence.
DR   GO; GO:0005759; C:mitochondrial matrix; IEA:EnsemblFungi.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
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:0016070; P:RNA metabolic process; IEA:EnsemblFungi.
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; Complete proteome; Helicase; Hydrolase; Mitochondrion;
KW   Nucleotide-binding; Reference proteome; RNA-binding; Transit peptide.
FT   TRANSIT       1     71       Mitochondrion. {ECO:0000255}.
FT   CHAIN        72    603       ATP-dependent RNA helicase MRH4,
FT                                mitochondrial.
FT                                /FTId=PRO_0000294673.
FT   DOMAIN      193    409       Helicase ATP-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00541}.
FT   DOMAIN      443    603       Helicase C-terminal.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00542}.
FT   NP_BIND     206    213       ATP. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00541}.
FT   MOTIF       151    158       Q motif.
FT   MOTIF       357    360       DEAD box.
SQ   SEQUENCE   603 AA;  67375 MW;  24FC0A62B4CEFB59 CRC64;
     MISTGLPLFT LSKICHNCFF KQTRSLSRYS SKDKVKGRRR LLPRPNTEKF NSARSGVGVG
     VGNGAGAGAR VGVGAGAGSV AAKVFESGNF SQLHNNGLSK QAQTAGLDLK QKITSFDQLK
     VFPSVREAMI KEIKSQYNLK GPQHSSIDDV VIKPTPVQIA AIRKINQTRK IKVAKNLDEM
     SEGERIQIEL QTKNEEQKTK IFTVAAETGS GKTWAYLANI MSKLKEDDYK WFNQSPEAYN
     SFKSSEQVRS VILLPTHELV EQVYETLKRA NSFLLEYENV PLQYKEFLNL PEHHTLGLSI
     AKLSHGDAPI NVYKQLRNRG KIDILITTPG KITSFSKLES IDRPFKIFKS IRYCVIDEAD
     TLFDDSFLKD TTAVVKNFPK LLDLILVSAT IPKEFEKTLL RLFPDQKSLI RVATPSLHKI
     SKNIKVMTLD ADLAPYNGSK TRCLAQAIYA ISKDGTEHNH VKRIIIFVNE KAEVDGLVDL
     LQSKYHIRRE DICGISGSVN VGDRKDYLEP FLKPAQLLED DVDQSKIKIL VTTDLLARGM
     NFIGIKNVIL MGLPKSSVEL VHRLGRTGRM NQLGRVFIIV DKKSRKSWVK GLGSAIMKGS
     RIG
//
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