GenomeNet

Database: UniProt
Entry: Q7SBR1
LinkDB: Q7SBR1
Original site: Q7SBR1 
ID   MRH4_NEUCR              Reviewed;         625 AA.
AC   Q7SBR1;
DT   04-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT   15-DEC-2003, sequence version 1.
DT   16-OCT-2019, entry version 94.
DE   RecName: Full=ATP-dependent RNA helicase mrh4, mitochondrial;
DE            EC=3.6.4.13;
DE   AltName: Full=DEAD box RNA helicase 15;
DE   Flags: Precursor;
GN   Name=drh-15; Synonyms=mrh4; ORFNames=NCU06246;
OS   Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM
OS   1257 / FGSC 987).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina;
OC   Sordariomycetes; Sordariomycetidae; Sordariales; Sordariaceae;
OC   Neurospora.
OX   NCBI_TaxID=367110;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987;
RX   PubMed=12712197; DOI=10.1038/nature01554;
RA   Galagan J.E., Calvo S.E., Borkovich K.A., Selker E.U., Read N.D.,
RA   Jaffe D.B., FitzHugh W., Ma L.-J., Smirnov S., Purcell S., Rehman B.,
RA   Elkins T., Engels R., Wang S., Nielsen C.B., Butler J., Endrizzi M.,
RA   Qui D., Ianakiev P., Bell-Pedersen D., Nelson M.A.,
RA   Werner-Washburne M., Selitrennikoff C.P., Kinsey J.A., Braun E.L.,
RA   Zelter A., Schulte U., Kothe G.O., Jedd G., Mewes H.-W., Staben C.,
RA   Marcotte E., Greenberg D., Roy A., Foley K., Naylor J.,
RA   Stange-Thomann N., Barrett R., Gnerre S., Kamal M., Kamvysselis M.,
RA   Mauceli E.W., Bielke C., Rudd S., Frishman D., Krystofova S.,
RA   Rasmussen C., Metzenberg R.L., Perkins D.D., Kroken S., Cogoni C.,
RA   Macino G., Catcheside D.E.A., Li W., Pratt R.J., Osmani S.A.,
RA   DeSouza C.P.C., Glass N.L., Orbach M.J., Berglund J.A., Voelker R.,
RA   Yarden O., Plamann M., Seiler S., Dunlap J.C., Radford A., Aramayo R.,
RA   Natvig D.O., Alex L.A., Mannhaupt G., Ebbole D.J., Freitag M.,
RA   Paulsen I., Sachs M.S., Lander E.S., Nusbaum C., Birren B.W.;
RT   "The genome sequence of the filamentous fungus Neurospora crassa.";
RL   Nature 422:859-868(2003).
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; CM002238; EAA33861.3; -; Genomic_DNA.
DR   RefSeq; XP_963097.3; XM_958004.3.
DR   EnsemblFungi; EAA33861; EAA33861; NCU06246.
DR   GeneID; 3879220; -.
DR   KEGG; ncr:NCU06246; -.
DR   EuPathDB; FungiDB:NCU06246; -.
DR   HOGENOM; HOG000268797; -.
DR   InParanoid; Q7SBR1; -.
DR   KO; K17678; -.
DR   Proteomes; UP000001805; Chromosome 3, Linkage Group III.
DR   GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003723; F:RNA binding; IBA:GO_Central.
DR   GO; GO:0003724; F:RNA helicase activity; IEA:UniProtKB-EC.
DR   GO; GO:0030490; P:maturation of SSU-rRNA; IBA:GO_Central.
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   InterPro; IPR014014; RNA_helicase_DEAD_Q_motif.
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; Complete proteome; Helicase; Hydrolase; Mitochondrion;
KW   Nucleotide-binding; Reference proteome; RNA-binding; Transit peptide.
FT   TRANSIT       1     16       Mitochondrion. {ECO:0000255}.
FT   CHAIN        17    625       ATP-dependent RNA helicase mrh4,
FT                                mitochondrial.
FT                                /FTId=PRO_0000232355.
FT   DOMAIN      195    406       Helicase ATP-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00541}.
FT   DOMAIN      453    625       Helicase C-terminal.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00542}.
FT   NP_BIND     208    215       ATP. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00541}.
FT   MOTIF       144    177       Q motif.
FT   MOTIF       353    356       DEAD box.
SQ   SEQUENCE   625 AA;  69259 MW;  1B5C32C750A21C08 CRC64;
     MWKTARDSVC LICRSAATTT TSTSARASLE PWAGQRTFST RREQRPSRMV LSDRVARPPP
     VRGPGEGNKK PRNKPDGPWA GMNRRVANID PRKAPKPKPV EEDSRRDKRD KNTKGQKALK
     MQRALATISY GQRTSIKERM QEIQAFDQFD LLPVVKEAIA QEALKGMTEI KPTPVQRLAI
     PALLGQPMGR KPRRPKSDNG REEFLLAAET GSGKTLAYLV PAVNAIKKGD ADDELVASYN
     ERLAAEKERR GGAPVSEWIE KFEPHPNTAR PRVVVLVPTA ELVDQVTSVA KKLAHYTKFK
     VRPLSASISP LRNQRNLYSP IGVDMIVSTP HLLATIAKSD PNVLSRVSHL VIDEADSLLD
     RSFSGDTTSI VDRAMPSLKQ LILCSATIPR RLDTYMEEQF PYINRITTPN LHAIPRRVQL
     GVIDVSKDPY RNNKMLACAD AIWSIGKEAA KHEGPKSEID VKRIMVFVNE RETTQQVADY
     LVSKGIDAIA LHRDTEEHRK SEMLASFTSN EPMKISRPAD DDVAAAAAEG GKAGGAVSSS
     PTRRHLPNTK VIVATDLASR GIDTLAVRYV VLYDVPHTTI DFIHRLGRAG RMNRRGRGIV
     LVGKDDRRDV VAEVKESMFM GQALV
//
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