MRH4_CANGA
ID MRH4_CANGA Reviewed; 568 AA.
AC Q6FJJ8;
DT 04-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 102.
DE RecName: Full=ATP-dependent RNA helicase MRH4, mitochondrial;
DE EC=3.6.4.13;
DE Flags: Precursor;
GN Name=MRH4; OrderedLocusNames=CAGL0M05753g;
OS Candida glabrata (strain ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL
OS Y-65) (Yeast) (Torulopsis glabrata).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Nakaseomyces;
OC Nakaseomyces/Candida clade.
OX NCBI_TaxID=284593;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL Y-65;
RX PubMed=15229592; DOI=10.1038/nature02579;
RA Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA Weissenbach J., Wincker P., Souciet J.-L.;
RT "Genome evolution in yeasts.";
RL Nature 430:35-44(2004).
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; CR380959; CAG62572.1; -; Genomic_DNA.
DR RefSeq; XP_449596.1; XM_449596.1.
DR AlphaFoldDB; Q6FJJ8; -.
DR SMR; Q6FJJ8; -.
DR STRING; 5478.XP_449596.1; -.
DR EnsemblFungi; CAG62572; CAG62572; CAGL0M05753g.
DR GeneID; 2891644; -.
DR KEGG; cgr:CAGL0M05753g; -.
DR CGD; CAL0136825; CAGL0M05753g.
DR VEuPathDB; FungiDB:CAGL0M05753g; -.
DR eggNOG; KOG0335; Eukaryota.
DR HOGENOM; CLU_003041_18_0_1; -.
DR InParanoid; Q6FJJ8; -.
DR OMA; FHALKMQ; -.
DR Proteomes; UP000002428; Chromosome M.
DR GO; GO:0005759; C:mitochondrial matrix; IEA:EnsemblFungi.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR GO; GO:1990400; F:mitochondrial ribosomal large subunit rRNA binding; IEA:EnsemblFungi.
DR GO; GO:0003724; F:RNA helicase activity; IEA:UniProtKB-EC.
DR GO; GO:1902775; P:mitochondrial large ribosomal subunit assembly; IEA:EnsemblFungi.
DR GO; GO:0016070; P:RNA metabolic process; IEA:EnsemblFungi.
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.
PE 3: Inferred from homology;
KW ATP-binding; Helicase; Hydrolase; Mitochondrion; Nucleotide-binding;
KW Reference proteome; RNA-binding; Transit peptide.
FT TRANSIT 1..50
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 51..568
FT /note="ATP-dependent RNA helicase MRH4, mitochondrial"
FT /id="PRO_0000232351"
FT DOMAIN 160..348
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 379..568
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT REGION 36..64
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 143..150
FT /note="Q motif"
FT MOTIF 296..299
FT /note="DEAD box"
FT BINDING 173..180
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ SEQUENCE 568 AA; 63924 MW; CAC699B8C0C1F9C8 CRC64;
MVSILAIRTF NPLGHFVSTQ CVRAYAINSV RAGSKSSSVR AGSKNDTTRA SSKKNKAGKS
KLQLSARFKQ NANKSQKADK FKSQKQFKYG LYGGLKENEN KFLETNANLV EKITEFEELK
LLPEVRKHVI NLIKKDSLNT TEEIHPSPIQ TIAIKRLSKN LMEPKLQVHA IAAETGSGKT
MAYCAPLLDY LKRQEIETPE KWESIKDKAI IRSVILVPTL ELVDQIYTTL TCIPDTLGIH
VHKWTTGVDY QQLLENLKSR TDILITTPSK LLSLQRVRMI SRADLILKRI EFVVLDEADT
LLDKSWLEDT HKALKAMSDV NHLVLCSATI PNEFDRTMTK MFPNAIPLTT PRLHKLPKGI
NFRIINAAVS PYKGSKIKAL AQTLYAIAYD GTDPGFEKRC IVFINEKKNV DNVVQKLRNE
YGHDVVGLTG DMEGRTRLEL IRPFISPPEK LTEQEKQIDK DLNDQETVNI SGSNISIGNI
ENSNKASNFI PKLRVLVTTD LLARGLNFKG VRNVILYDVP ITAIDLVHRA GRTARMRQSG
RVFMIIDKKT QSWAKAVPTI LKKNKALT
