MRH4_ASPFU
ID MRH4_ASPFU Reviewed; 631 AA.
AC Q4X1X0;
DT 04-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2005, sequence version 1.
DT 03-AUG-2022, entry version 102.
DE RecName: Full=ATP-dependent RNA helicase mrh4, mitochondrial;
DE EC=3.6.4.13;
DE Flags: Precursor;
GN Name=mrh4; ORFNames=AFUA_2G08480;
OS Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC
OS A1100) (Aspergillus fumigatus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Fumigati.
OX NCBI_TaxID=330879;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100;
RX PubMed=16372009; DOI=10.1038/nature04332;
RA Nierman W.C., Pain A., Anderson M.J., Wortman J.R., Kim H.S., Arroyo J.,
RA Berriman M., Abe K., Archer D.B., Bermejo C., Bennett J.W., Bowyer P.,
RA Chen D., Collins M., Coulsen R., Davies R., Dyer P.S., Farman M.L.,
RA Fedorova N., Fedorova N.D., Feldblyum T.V., Fischer R., Fosker N.,
RA Fraser A., Garcia J.L., Garcia M.J., Goble A., Goldman G.H., Gomi K.,
RA Griffith-Jones S., Gwilliam R., Haas B.J., Haas H., Harris D.E.,
RA Horiuchi H., Huang J., Humphray S., Jimenez J., Keller N., Khouri H.,
RA Kitamoto K., Kobayashi T., Konzack S., Kulkarni R., Kumagai T., Lafton A.,
RA Latge J.-P., Li W., Lord A., Lu C., Majoros W.H., May G.S., Miller B.L.,
RA Mohamoud Y., Molina M., Monod M., Mouyna I., Mulligan S., Murphy L.D.,
RA O'Neil S., Paulsen I., Penalva M.A., Pertea M., Price C., Pritchard B.L.,
RA Quail M.A., Rabbinowitsch E., Rawlins N., Rajandream M.A., Reichard U.,
RA Renauld H., Robson G.D., Rodriguez de Cordoba S., Rodriguez-Pena J.M.,
RA Ronning C.M., Rutter S., Salzberg S.L., Sanchez M., Sanchez-Ferrero J.C.,
RA Saunders D., Seeger K., Squares R., Squares S., Takeuchi M., Tekaia F.,
RA Turner G., Vazquez de Aldana C.R., Weidman J., White O., Woodward J.R.,
RA Yu J.-H., Fraser C.M., Galagan J.E., Asai K., Machida M., Hall N.,
RA Barrell B.G., Denning D.W.;
RT "Genomic sequence of the pathogenic and allergenic filamentous fungus
RT Aspergillus fumigatus.";
RL Nature 438:1151-1156(2005).
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; AAHF01000001; EAL93145.1; -; Genomic_DNA.
DR RefSeq; XP_755183.1; XM_750090.1.
DR AlphaFoldDB; Q4X1X0; -.
DR SMR; Q4X1X0; -.
DR STRING; 746128.CADAFUBP00002386; -.
DR PRIDE; Q4X1X0; -.
DR EnsemblFungi; EAL93145; EAL93145; AFUA_2G08480.
DR GeneID; 3513301; -.
DR KEGG; afm:AFUA_2G08480; -.
DR VEuPathDB; FungiDB:Afu2g08480; -.
DR eggNOG; KOG0335; Eukaryota.
DR HOGENOM; CLU_003041_18_0_1; -.
DR InParanoid; Q4X1X0; -.
DR OMA; FHALKMQ; -.
DR OrthoDB; 1223767at2759; -.
DR Proteomes; UP000002530; Chromosome 2.
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..45
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 46..631
FT /note="ATP-dependent RNA helicase mrh4, mitochondrial"
FT /id="PRO_0000232348"
FT DOMAIN 194..406
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 455..631
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT REGION 68..112
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 180..199
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 229..249
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 84..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 631 AA; 70437 MW; E9E5A0276F808200 CRC64;
MNRLGRLPLP LPPSVCLFCR FRATASLPSS LQATRSMATA RLRRRVARMT LSPDVAKPSV
VKKTRGDKER FGPFAGMNQT EARIRETPRA RSRAAQKRSG EPEEDSQKES PLYKALKMQT
ALTPIPYGRR AAIKAKIADI TSFDQFQLLP VVRNSISSQA LPGLVDVTPT PIQRLAIPRL
LEEPKTEKKP TKADDDEPRY DQYLLAAETG SGKTLAYLLP VVDAVKREEA RDKELEKKEQ
EEKAREREER LKNRAFDIEP EIPPLSNAGR PRAIILVPTS ELVAQVGVKV KALSHTVKYR
SGMISSNFTP RRIKNTLFHP DGIDILVATP HLLASIAKTE PYVLSRVSHL VLDEADSLLD
RSFAPTTTEI ISKAAPSLRK LILCSATIPR SLDNLLRKRY PDIKRLTTPN LHAIPRRVQL
GVVDIEKDPY RGNRSLACAD VIWSIGKAGD AESEGPYASY VAPKTKKILV FVNEREEADE
VAQFLRSKGI DAQSLSRDSD ARKQEEILAE FTEAPPPPSP DEILLAQKKR RYEDAIPFEM
PEKANQGSSR RLANTKVLVT TDLASRGIDT LAVKTVILYH VPHTTIDFIH RLGRLGRMGK
RGRGVVLVGK KDRKDVVKEV REGMFRGQAL I
