MRH4_ASPOR
ID MRH4_ASPOR Reviewed; 628 AA.
AC Q2TZH2;
DT 04-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT 24-JAN-2006, sequence version 1.
DT 03-AUG-2022, entry version 82.
DE RecName: Full=ATP-dependent RNA helicase mrh4, mitochondrial;
DE EC=3.6.4.13;
DE Flags: Precursor;
GN Name=mrh4; ORFNames=AO090011000853;
OS Aspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=510516;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 42149 / RIB 40;
RX PubMed=16372010; DOI=10.1038/nature04300;
RA Machida M., Asai K., Sano M., Tanaka T., Kumagai T., Terai G., Kusumoto K.,
RA Arima T., Akita O., Kashiwagi Y., Abe K., Gomi K., Horiuchi H.,
RA Kitamoto K., Kobayashi T., Takeuchi M., Denning D.W., Galagan J.E.,
RA Nierman W.C., Yu J., Archer D.B., Bennett J.W., Bhatnagar D.,
RA Cleveland T.E., Fedorova N.D., Gotoh O., Horikawa H., Hosoyama A.,
RA Ichinomiya M., Igarashi R., Iwashita K., Juvvadi P.R., Kato M., Kato Y.,
RA Kin T., Kokubun A., Maeda H., Maeyama N., Maruyama J., Nagasaki H.,
RA Nakajima T., Oda K., Okada K., Paulsen I., Sakamoto K., Sawano T.,
RA Takahashi M., Takase K., Terabayashi Y., Wortman J.R., Yamada O.,
RA Yamagata Y., Anazawa H., Hata Y., Koide Y., Komori T., Koyama Y.,
RA Minetoki T., Suharnan S., Tanaka A., Isono K., Kuhara S., Ogasawara N.,
RA Kikuchi H.;
RT "Genome sequencing and analysis of Aspergillus oryzae.";
RL Nature 438:1157-1161(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; AP007171; BAE65293.1; -; Genomic_DNA.
DR AlphaFoldDB; Q2TZH2; -.
DR SMR; Q2TZH2; -.
DR STRING; 510516.Q2TZH2; -.
DR PRIDE; Q2TZH2; -.
DR EnsemblFungi; BAE65293; BAE65293; AO090011000853.
DR HOGENOM; CLU_003041_18_0_1; -.
DR OMA; FHALKMQ; -.
DR Proteomes; UP000006564; Chromosome 7.
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..40
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 41..628
FT /note="ATP-dependent RNA helicase mrh4, mitochondrial"
FT /id="PRO_0000232349"
FT DOMAIN 190..402
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 456..628
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT REGION 51..109
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 228..260
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 137..170
FT /note="Q motif"
FT MOTIF 349..352
FT /note="DEAD box"
FT COMPBIAS 78..103
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 228..255
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 203..210
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ SEQUENCE 628 AA; 69853 MW; DCB6177FB57CDB3B CRC64;
MSLAVRPPVC LLCRSGAPTL LPSSVSQVAR SMATARLRRK VARMALSPDV AKSSINQKRS
GKAKFGPWSG MNQTEAHIRG EPRSRSQAAL RRSGEKAADT PRKSDSPLYK ALKMQTTLAP
VPYGRRTAVK SKIADITSFD HFPLLPVVRH SIFSQALPGL VDVTPTPIQR LAIPKLMEDS
PDGKRGTKLE DGDPQYDQYL LAAETGSGKT LAYLLPLVDA VKRLEVEDKE NERKEEERKA
KEKEERLKNR AFDLEPEEPP LSNAGRPRVI ILVPTSELVA QVGVKVKALA HTVKYRSGMI
SSNLTPRRIK STLFNPDGID ILVSTPHLLA SIAKTEPYVL SRVSHLVLDE ADSLMDRSFL
PTTTEIISKV APSLRKLILC SATIPRSLDN LLRKRYPDIK RLTTPNLHAI PRRVQLGVVD
IQKEPYRGNR NLACADVIWS IGKAGDSEPS EPFASYVGPN IKKILVFVNE REEADEVAQF
LRSKGIDAQS LSRDSSARKQ EEILAEFTES APPPSPEEIM LAQKKRRQED AIPFELPENH
NKPENVRRLA NTKVLVTTDL ASRGIDTLPV KTVILYHVPH TTIDFIHRLG RLGRMNKRGR
GIVLVGKKDR KDVVKEVREG MFRGQALI
