MRH4_NEOFI
ID MRH4_NEOFI Reviewed; 631 AA.
AC A1DGF2;
DT 03-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 1.
DT 03-AUG-2022, entry version 81.
DE RecName: Full=ATP-dependent RNA helicase mrh4, mitochondrial;
DE EC=3.6.4.13;
DE Flags: Precursor;
GN Name=mrh4; ORFNames=NFIA_084110;
OS Neosartorya fischeri (strain ATCC 1020 / DSM 3700 / CBS 544.65 / FGSC A1164
OS / JCM 1740 / NRRL 181 / WB 181) (Aspergillus fischerianus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Fumigati.
OX NCBI_TaxID=331117;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 1020 / DSM 3700 / CBS 544.65 / FGSC A1164 / JCM 1740 / NRRL 181
RC / WB 181;
RX PubMed=18404212; DOI=10.1371/journal.pgen.1000046;
RA Fedorova N.D., Khaldi N., Joardar V.S., Maiti R., Amedeo P., Anderson M.J.,
RA Crabtree J., Silva J.C., Badger J.H., Albarraq A., Angiuoli S., Bussey H.,
RA Bowyer P., Cotty P.J., Dyer P.S., Egan A., Galens K., Fraser-Liggett C.M.,
RA Haas B.J., Inman J.M., Kent R., Lemieux S., Malavazi I., Orvis J.,
RA Roemer T., Ronning C.M., Sundaram J.P., Sutton G., Turner G., Venter J.C.,
RA White O.R., Whitty B.R., Youngman P., Wolfe K.H., Goldman G.H.,
RA Wortman J.R., Jiang B., Denning D.W., Nierman W.C.;
RT "Genomic islands in the pathogenic filamentous fungus Aspergillus
RT fumigatus.";
RL PLoS Genet. 4:E1000046-E1000046(2008).
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; DS027696; EAW18459.1; -; Genomic_DNA.
DR RefSeq; XP_001260356.1; XM_001260355.1.
DR AlphaFoldDB; A1DGF2; -.
DR SMR; A1DGF2; -.
DR STRING; 36630.CADNFIAP00007742; -.
DR EnsemblFungi; EAW18459; EAW18459; NFIA_084110.
DR GeneID; 4586914; -.
DR KEGG; nfi:NFIA_084110; -.
DR VEuPathDB; FungiDB:NFIA_084110; -.
DR eggNOG; KOG0335; Eukaryota.
DR HOGENOM; CLU_003041_18_0_1; -.
DR OMA; FHALKMQ; -.
DR OrthoDB; 1223767at2759; -.
DR Proteomes; UP000006702; 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; 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_0000282711"
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..111
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 82..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; 70397 MW; 3AC8458BB1E1BE37 CRC64;
MNRLGRLPLP LPPSVCLFCQ SRATTPLPPS LQATRSMATA RLRRRVARMT LSPDVAKPSV
VKKTRGDKER FGPFAGMNQT EARIRDKPRT RSRAAQKRSG EPEEDSQKES PLYKALKMQT
ALAPIPYGRR AAIKAKIADI TSFDQFQLLP VVRNSISSQA LPGLVDVTPT PIQRLAIPRL
LEEPKTEKKP TKADDDEPQY DQYLLAAETG SGKTLAYLLP VVDAVKREEA RDKELEKKEQ
EEKAREREEK LKNRAFDIEP EIPPLSNAGR PRAIILVPTS ELVAQVGVKV KALSHTVKYR
SGMISSNLTP RRIKNTLFHP DGIDILVATP HLLASIAKTE PYVLSRVSHL VLDEADSLLD
RSFAPTTTEI ISKAAPSLRK LILCSATIPR SLDNLLRKRY PDIKRLTTPN LHAIPRRVQL
GVVDIEKDPY RGNRSLACAD VIWSIGKAGD AESEGPYASY VAPKTKKILV FVNEREEADE
VAQFLRSKGI DAQSLSRDSD ARKQEEILAE FTEAPPPPTP DEILLAQKQR RHEDAIPFEM
PQKTNQDSSR RLANTKVLVT TDLASRGIDT LAVKTVILYH VPHTTIDFIH RLGRLGRMGK
RGRGVVLVGK KDRKDVVKEV REGMFRGQAL I
