MRH4_SCLS1
ID MRH4_SCLS1 Reviewed; 615 AA.
AC A7EWH6;
DT 13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT 11-SEP-2007, sequence version 1.
DT 03-AUG-2022, entry version 68.
DE RecName: Full=ATP-dependent RNA helicase mrh4, mitochondrial;
DE EC=3.6.4.13;
DE Flags: Precursor;
GN Name=mrh4; ORFNames=SS1G_09685;
OS Sclerotinia sclerotiorum (strain ATCC 18683 / 1980 / Ss-1) (White mold)
OS (Whetzelinia sclerotiorum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Helotiales; Sclerotiniaceae; Sclerotinia.
OX NCBI_TaxID=665079;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 18683 / 1980 / Ss-1;
RX PubMed=21876677; DOI=10.1371/journal.pgen.1002230;
RA Amselem J., Cuomo C.A., van Kan J.A.L., Viaud M., Benito E.P., Couloux A.,
RA Coutinho P.M., de Vries R.P., Dyer P.S., Fillinger S., Fournier E.,
RA Gout L., Hahn M., Kohn L., Lapalu N., Plummer K.M., Pradier J.-M.,
RA Quevillon E., Sharon A., Simon A., ten Have A., Tudzynski B., Tudzynski P.,
RA Wincker P., Andrew M., Anthouard V., Beever R.E., Beffa R., Benoit I.,
RA Bouzid O., Brault B., Chen Z., Choquer M., Collemare J., Cotton P.,
RA Danchin E.G., Da Silva C., Gautier A., Giraud C., Giraud T., Gonzalez C.,
RA Grossetete S., Gueldener U., Henrissat B., Howlett B.J., Kodira C.,
RA Kretschmer M., Lappartient A., Leroch M., Levis C., Mauceli E.,
RA Neuveglise C., Oeser B., Pearson M., Poulain J., Poussereau N.,
RA Quesneville H., Rascle C., Schumacher J., Segurens B., Sexton A., Silva E.,
RA Sirven C., Soanes D.M., Talbot N.J., Templeton M., Yandava C., Yarden O.,
RA Zeng Q., Rollins J.A., Lebrun M.-H., Dickman M.;
RT "Genomic analysis of the necrotrophic fungal pathogens Sclerotinia
RT sclerotiorum and Botrytis cinerea.";
RL PLoS Genet. 7:E1002230-E1002230(2011).
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; CH476634; EDN93818.1; -; Genomic_DNA.
DR RefSeq; XP_001589052.1; XM_001589002.1.
DR AlphaFoldDB; A7EWH6; -.
DR SMR; A7EWH6; -.
DR STRING; 665079.A7EWH6; -.
DR GeneID; 5485369; -.
DR KEGG; ssl:SS1G_09685; -.
DR VEuPathDB; FungiDB:sscle_01g000610; -.
DR InParanoid; A7EWH6; -.
DR OMA; FHALKMQ; -.
DR Proteomes; UP000001312; 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 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..37
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 38..615
FT /note="ATP-dependent RNA helicase mrh4, mitochondrial"
FT /id="PRO_0000310260"
FT DOMAIN 184..395
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 444..615
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT REGION 21..108
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 138..171
FT /note="Q motif"
FT MOTIF 342..345
FT /note="DEAD box"
FT COMPBIAS 78..108
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 197..204
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ SEQUENCE 615 AA; 68126 MW; D61C97B9DEC86FB0 CRC64;
MLRPKAGKCL LCSFRAAQKP VSQKWPSRAL SMRTRLPSRP NRMSLAGAGK VSSSPTKEGP
ARRKQDGPFG GMNLREAKIR GVPERPSAAQ ERRTSRLDHR DRDDKKDRGF HALKMQSPLA
PVSYVRRTDI KGRMNEVQSF EQFALLDSVK QAIFQQALPE LKEHVPTPVQ RIAVPALLGD
QQSRRPKSEM EQYLIAAETG SGKTLSYLIP TINAIKVAEA KDAEVKAYEK ELQEEKLRQN
NLTLVSPPLS NMPHPTTGRP RAIILVPTSE LVTQVGTLLK LFSHTVKFKA AVISSNFSGK
VIRNRLFSPS GIDILVSTPH LLSSIADSDP NILSRVTHLI IDEADSLLDR GFSPLTSAII
DRATPSLEKL VLCSATIPRS LDSFLRKRFP DINRLVTPNL HAIPRRVQLG VVDVERDPYR
NNKNLACADT IWSIGKAAAE HDGPVKGLMD VKRILVFVNE REKTQEVADY LVSKGVDAIA
LSRDTPEQRQ SEMLASFTSP AKLSVEKPVS HPGSLSDNQP NYVPFGEVAP PVKRRLPNTK
VLVTTDLGSR GIDTVAVRHV ILYDVPHSTI DFIHRLGRTG RMGRRGRGIV LVGKGDRRDV
VKEVREGMFE GKALI
