MRH4_PHANO
ID MRH4_PHANO Reviewed; 658 AA.
AC Q0U397;
DT 31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 29-APR-2008, sequence version 2.
DT 03-AUG-2022, entry version 74.
DE RecName: Full=ATP-dependent RNA helicase MRH4, mitochondrial;
DE EC=3.6.4.13;
DE Flags: Precursor;
GN Name=MRH4; ORFNames=SNOG_13767;
OS Phaeosphaeria nodorum (strain SN15 / ATCC MYA-4574 / FGSC 10173) (Glume
OS blotch fungus) (Parastagonospora nodorum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Pleosporineae; Phaeosphaeriaceae;
OC Parastagonospora.
OX NCBI_TaxID=321614;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SN15 / ATCC MYA-4574 / FGSC 10173;
RX PubMed=18024570; DOI=10.1105/tpc.107.052829;
RA Hane J.K., Lowe R.G.T., Solomon P.S., Tan K.-C., Schoch C.L.,
RA Spatafora J.W., Crous P.W., Kodira C.D., Birren B.W., Galagan J.E.,
RA Torriani S.F.F., McDonald B.A., Oliver R.P.;
RT "Dothideomycete-plant interactions illuminated by genome sequencing and EST
RT analysis of the wheat pathogen Stagonospora nodorum.";
RL Plant Cell 19:3347-3368(2007).
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=EAT78791.2; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; CH445352; EAT78791.2; ALT_SEQ; Genomic_DNA.
DR RefSeq; XP_001803973.1; XM_001803921.1.
DR AlphaFoldDB; Q0U397; -.
DR SMR; Q0U397; -.
DR STRING; 13684.SNOT_13767; -.
DR GeneID; 5980895; -.
DR KEGG; pno:SNOG_13767; -.
DR eggNOG; KOG0335; Eukaryota.
DR InParanoid; Q0U397; -.
DR OrthoDB; 1223767at2759; -.
DR Proteomes; UP000001055; Unassembled WGS sequence.
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 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; Helicase; Hydrolase; Mitochondrion; Nucleotide-binding;
KW Reference proteome; RNA-binding; Transit peptide.
FT TRANSIT 1..32
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 33..658
FT /note="ATP-dependent RNA helicase MRH4, mitochondrial"
FT /id="PRO_0000256055"
FT DOMAIN 233..449
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 490..658
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT REGION 25..150
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 268..292
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 552..573
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 182..214
FT /note="Q motif"
FT MOTIF 396..399
FT /note="DEAD box"
FT COMPBIAS 36..64
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 74..90
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 121..150
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 246..253
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ SEQUENCE 658 AA; 73123 MW; 15DB619EBA80ACCF CRC64;
MLRQVTRACP FCEVRSLLGQ APRSLQPQTR LYTQVQREAQ RERGSRDSNT PSRPRDRRTP
ETDAFPPSSD RGSRGRSPRG RDDRRPSRMI LSDAVSRPPQ SDQRPARRPQ EPFGHLNRTR
APPSLERERE RRESHFERPK RNDDGKRRTR AEPYHALKMQ RSLHEVPYGN RTTIKRKMEL
YDSFDKMPLL DTVQAAIKDA LPALEYRSPT PAQSVAVPAL LGLEAKKRTK ATSTKKGGPE
AFLLAAETGS GKTLAYLLPT LDAIKKAEQQ EKEDAEAQAQ KDADEAAAKA QDKRTDIFAA
EEPEVNKAVD PARPRAIILV PSAELVAQVG AVAKSLSHTV KFRAAPISAK MSATVIRNQL
FNEKGVDVVI STPPLLASIA ESNPNILARV THLICDEADS LFDRSFKPST TEILERATPS
LKQLILCSAT IPKYLDKYLA DRFPDMNRLV TPNLHAIPRR VQLGVVDVNK DPYHGNKNLA
CADTIWQIGR STGEYDPAEG KEAVPTKRIL VFVNEREDTE KVAQYLMSKG IDALAFHRDT
DPSRQAKTLA SFTGSDTSTA IKSSPDAPPK PELASKRTLA NTKVIVTTDL GSRGIDTVSV
RHVILYDVPH TTIDFIHRLG RTGRMGRRGR GIVLLGPGDR ADVVKEVREA MYRGEALI
