MRH4_CANAL
ID MRH4_CANAL Reviewed; 555 AA.
AC Q59S59; A0A1D8PPW0;
DT 04-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2017, sequence version 2.
DT 03-AUG-2022, entry version 89.
DE RecName: Full=ATP-dependent RNA helicase MRH4, mitochondrial;
DE EC=3.6.4.13;
DE Flags: Precursor;
GN Name=MRH4; OrderedLocusNames=CAALFM_C602380WA;
GN ORFNames=CaO19.10985, CaO19.3481;
OS Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX NCBI_TaxID=237561;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=15123810; DOI=10.1073/pnas.0401648101;
RA Jones T., Federspiel N.A., Chibana H., Dungan J., Kalman S., Magee B.B.,
RA Newport G., Thorstenson Y.R., Agabian N., Magee P.T., Davis R.W.,
RA Scherer S.;
RT "The diploid genome sequence of Candida albicans.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:7329-7334(2004).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=17419877; DOI=10.1186/gb-2007-8-4-r52;
RA van het Hoog M., Rast T.J., Martchenko M., Grindle S., Dignard D.,
RA Hogues H., Cuomo C., Berriman M., Scherer S., Magee B.B., Whiteway M.,
RA Chibana H., Nantel A., Magee P.T.;
RT "Assembly of the Candida albicans genome into sixteen supercontigs aligned
RT on the eight chromosomes.";
RL Genome Biol. 8:RESEARCH52.1-RESEARCH52.12(2007).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME REANNOTATION.
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=24025428; DOI=10.1186/gb-2013-14-9-r97;
RA Muzzey D., Schwartz K., Weissman J.S., Sherlock G.;
RT "Assembly of a phased diploid Candida albicans genome facilitates allele-
RT specific measurements and provides a simple model for repeat and indel
RT structure.";
RL Genome Biol. 14:RESEARCH97.1-RESEARCH97.14(2013).
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; CP017628; AOW30173.1; -; Genomic_DNA.
DR RefSeq; XP_712520.2; XM_707427.2.
DR AlphaFoldDB; Q59S59; -.
DR SMR; Q59S59; -.
DR STRING; 237561.Q59S59; -.
DR GeneID; 3645883; -.
DR KEGG; cal:CAALFM_C602380WA; -.
DR CGD; CAL0000186407; orf19.10985.
DR VEuPathDB; FungiDB:C6_02380W_A; -.
DR eggNOG; KOG0335; Eukaryota.
DR HOGENOM; CLU_003041_18_0_1; -.
DR InParanoid; Q59S59; -.
DR OrthoDB; 1223767at2759; -.
DR PRO; PR:Q59S59; -.
DR Proteomes; UP000000559; Chromosome 6.
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.
PE 3: Inferred from homology;
KW ATP-binding; Helicase; Hydrolase; Mitochondrion; Nucleotide-binding;
KW Reference proteome; RNA-binding; Transit peptide.
FT TRANSIT 1..25
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 26..555
FT /note="ATP-dependent RNA helicase MRH4, mitochondrial"
FT /id="PRO_0000232350"
FT DOMAIN 144..361
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 395..555
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT MOTIF 101..108
FT /note="Q motif"
FT MOTIF 309..312
FT /note="DEAD box"
FT BINDING 157..164
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ SEQUENCE 555 AA; 62499 MW; 64F8417AB7C11882 CRC64;
MFKLLIPNKY NYVIRPLVRF KSIKSPKSPK PKPTAKLSPN VFSSGKFSQL HNDTSTTNIE
SKITSFDQLK IFPSVREAMI KEIKSQYNLK GPRHSNIDEI DIKPTPVQIA AIRKINQTRK
LKVPNKDLEG MDDAERIQFE LQNANEIQKT KVFTVAAETG SGKTWSYLAP LLSKLKSDDM
EFWKSDPEGY DNTRKKGQFV KSVILLPTNE LVDQVYETLQ RANSFELDHK GAPGNFTSFL
ELPENKTMNI TTMKLGQGEA PVRLFRQLET KGPIDVLITT PGKIVAFSKL VNINRPFRVF
ANVKYCVLDE ADTLFDDSFE KNTTDVITHF PKLLDLILVS ATIPKVFEKK LSKLFPDQRS
LIRVATPSLH KVPRNIKVMT IDADVAPYNG SKPRCLAQAL YAISKDGTEP GYVKRIIVFV
NEKSEVDGIV ESMITKYKVR PEDIVGVSGS VNIRDRKDML QPFLQPAELI ENDDFGSKVK
ILVTTDLLAR GLNFQGVKNV ILLGLPRNSV DLVHRLGRTG RMNQNGRVFV IVDKKSKKSW
VKGLGNAIIR GLRIG
