MRH4_NEUCR
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 03-AUG-2022, entry version 105.
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 1257 /
OS FGSC 987).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Sordariales; Sordariaceae; 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., Werner-Washburne M.,
RA Selitrennikoff C.P., Kinsey J.A., Braun E.L., Zelter A., Schulte U.,
RA Kothe G.O., Jedd G., Mewes H.-W., Staben C., Marcotte E., Greenberg D.,
RA Roy A., Foley K., Naylor J., Stange-Thomann N., Barrett R., Gnerre S.,
RA Kamal M., Kamvysselis M., Mauceli E.W., Bielke C., Rudd S., Frishman D.,
RA Krystofova S., Rasmussen C., Metzenberg R.L., Perkins D.D., Kroken S.,
RA Cogoni C., 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., Paulsen I.,
RA 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 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; CM002238; EAA33861.3; -; Genomic_DNA.
DR RefSeq; XP_963097.3; XM_958004.3.
DR AlphaFoldDB; Q7SBR1; -.
DR SMR; Q7SBR1; -.
DR STRING; 367110.Q7SBR1; -.
DR PRIDE; Q7SBR1; -.
DR EnsemblFungi; EAA33861; EAA33861; NCU06246.
DR GeneID; 3879220; -.
DR KEGG; ncr:NCU06246; -.
DR VEuPathDB; FungiDB:NCU06246; -.
DR InParanoid; Q7SBR1; -.
DR Proteomes; UP000001805; Chromosome 3, Linkage Group III.
DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
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 GO; GO:0006364; P:rRNA processing; IBA:GO_Central.
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..16
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 17..625
FT /note="ATP-dependent RNA helicase mrh4, mitochondrial"
FT /id="PRO_0000232355"
FT DOMAIN 195..406
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 453..625
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT REGION 19..119
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 144..177
FT /note="Q motif"
FT MOTIF 353..356
FT /note="DEAD box"
FT COMPBIAS 19..40
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 89..117
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 208..215
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
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
