MRH4_COCIM
ID MRH4_COCIM Reviewed; 656 AA.
AC Q1E9B7; I9NPJ8;
DT 31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 11-JUL-2006, sequence version 1.
DT 03-AUG-2022, entry version 73.
DE RecName: Full=ATP-dependent RNA helicase MRH4, mitochondrial;
DE EC=3.6.4.13;
DE Flags: Precursor;
GN Name=MRH4; ORFNames=CIMG_00846;
OS Coccidioides immitis (strain RS) (Valley fever fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Onygenaceae; Coccidioides.
OX NCBI_TaxID=246410;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RS;
RX PubMed=19717792; DOI=10.1101/gr.087551.108;
RA Sharpton T.J., Stajich J.E., Rounsley S.D., Gardner M.J., Wortman J.R.,
RA Jordar V.S., Maiti R., Kodira C.D., Neafsey D.E., Zeng Q., Hung C.-Y.,
RA McMahan C., Muszewska A., Grynberg M., Mandel M.A., Kellner E.M.,
RA Barker B.M., Galgiani J.N., Orbach M.J., Kirkland T.N., Cole G.T.,
RA Henn M.R., Birren B.W., Taylor J.W.;
RT "Comparative genomic analyses of the human fungal pathogens Coccidioides
RT and their relatives.";
RL Genome Res. 19:1722-1731(2009).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=RS;
RX PubMed=20516208; DOI=10.1101/gr.103911.109;
RA Neafsey D.E., Barker B.M., Sharpton T.J., Stajich J.E., Park D.J.,
RA Whiston E., Hung C.-Y., McMahan C., White J., Sykes S., Heiman D.,
RA Young S., Zeng Q., Abouelleil A., Aftuck L., Bessette D., Brown A.,
RA FitzGerald M., Lui A., Macdonald J.P., Priest M., Orbach M.J.,
RA Galgiani J.N., Kirkland T.N., Cole G.T., Birren B.W., Henn M.R.,
RA Taylor J.W., Rounsley S.D.;
RT "Population genomic sequencing of Coccidioides fungi reveals recent
RT hybridization and transposon control.";
RL Genome Res. 20:938-946(2010).
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; GG704911; EAS35492.3; -; Genomic_DNA.
DR RefSeq; XP_001247075.1; XM_001247074.2.
DR AlphaFoldDB; Q1E9B7; -.
DR SMR; Q1E9B7; -.
DR STRING; 246410.Q1E9B7; -.
DR PRIDE; Q1E9B7; -.
DR EnsemblFungi; EAS35492; EAS35492; CIMG_12830.
DR GeneID; 24164457; -.
DR KEGG; cim:CIMG_12830; -.
DR VEuPathDB; FungiDB:CIMG_12830; -.
DR InParanoid; Q1E9B7; -.
DR OMA; FHALKMQ; -.
DR OrthoDB; 1223767at2759; -.
DR Proteomes; UP000001261; 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 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..46
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 47..656
FT /note="ATP-dependent RNA helicase MRH4, mitochondrial"
FT /id="PRO_0000256053"
FT DOMAIN 210..431
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 480..656
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT REGION 42..125
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 246..270
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 157..190
FT /note="Q motif"
FT MOTIF 378..381
FT /note="DEAD box"
FT COMPBIAS 54..72
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 95..125
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 223..230
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ SEQUENCE 656 AA; 73735 MW; 7396AD0B39F16DFB CRC64;
MTSFSHLSRL RMSAFLPHVC LQCRLKTVSS LPAQSSASSL LQAVRHASSA RPRRRTPSRM
TLSPNVAQST VKYGEKRKSV RHQNGPFGGM NQRRANLRDR QRPRSQAELK RTSFKKDKDG
SEKKQPELFK ALKMQTALSS VSYGRRTSIK SKISNITSFD QFDLLPSVRQ SVYDSALPGL
EYVTPTPIQR LAIPAILRQG SATPKPEEGQ EDMPRFDQYL LAAETGSGKT LAYLLPVVDA
IKRTEAKDKE EEERMAKEEL EKEQEQAKEK NQNLFELESP GEEEEPINAP KSVVKPKAII
LVPTSELVEQ IGRIVKQLAH TVKYRSALLA SNYTPRKIRK TLFNPNGLDI LVTTPYLVAS
IAEANPYIFS RVTHLVVDEA DSLFDKSFSP KTNTIIDRTA PTLKQLILCS ATIPRSLDNR
LRERFPQIRR LVTPNLHAIP RRVQLGVVDI DKEPYRGRRH LACADAIWSI GRSGNPYDAD
VGYQVTGQKE PKSIIVFVNE RETAAEVAEF LVTKGINAVS LTRDTSEKRQ AQILAEFTTE
KNPPQPEDYK MLKGNRSDDD SVPFVNVRPG NERSNRLSNT KVLVVTDLGS RGIDTVAVKT
VILYDVPHST IDFIHRLGRL GRMGRRGRGI VLVGKKDRKD VVREVREAMY RGQALI
