ID MRH4_CANAL Reviewed; 555 AA.
AC Q59S59;
DT 04-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT 26-APR-2005, sequence version 1.
DT 03-APR-2013, entry version 46.
DE RecName: Full=ATP-dependent RNA helicase MRH4, mitochondrial;
DE EC=3.6.4.13;
DE Flags: Precursor;
GN Name=MRH4; ORFNames=CaO19.10985, CaO19.3481;
OS Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
OC Saccharomycetes; Saccharomycetales; mitosporic Saccharomycetales;
OC 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.,
RA Magee B.B., Newport G., Thorstenson Y.R., Agabian N., Magee P.T.,
RA Davis R.W., Scherer S.;
RT "The diploid genome sequence of Candida albicans.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:7329-7334(2004).
CC -!- FUNCTION: ATP-binding RNA helicase involved in mitochondrial RNA
CC metabolism. Required for maintenance of mitochondrial DNA (By
CC similarity).
CC -!- CATALYTIC ACTIVITY: ATP + H(2)O = ADP + phosphate.
CC -!- SUBCELLULAR LOCATION: Mitochondrion (By similarity).
CC -!- DOMAIN: The Q motif is unique to and characteristic of the DEAD
CC box family of RNA helicases and controls ATP binding and
CC hydrolysis.
CC -!- SIMILARITY: Belongs to the DEAD box helicase family. MRH4
CC subfamily.
CC -!- SIMILARITY: Contains 1 helicase ATP-binding domain.
CC -!- SIMILARITY: Contains 1 helicase C-terminal domain.
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DR EMBL; AACQ01000154; EAK93370.1; -; Genomic_DNA.
DR EMBL; AACQ01000155; EAK93339.1; -; Genomic_DNA.
DR RefSeq; XP_712520.1; XM_707427.1.
DR RefSeq; XP_712550.1; XM_707457.1.
DR ProteinModelPortal; Q59S59; -.
DR STRING; 5476.CAL0005084; -.
DR GeneID; 3645858; -.
DR GeneID; 3645883; -.
DR KEGG; cal:CaO19.10985; -.
DR KEGG; cal:CaO19.3481; -.
DR CGD; CAL0005084; orf19.3481.
DR eggNOG; COG0513; -.
DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0008026; F:ATP-dependent helicase activity; IEA:InterPro.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR InterPro; IPR011545; DNA/RNA_helicase_DEAD/DEAH_N.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR Pfam; PF00270; DEAD; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR PROSITE; PS00039; DEAD_ATP_HELICASE; FALSE_NEG.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
PE 3: Inferred from homology;
KW ATP-binding; Complete proteome; Helicase; Hydrolase; Mitochondrion;
KW Nucleotide-binding; Reference proteome; RNA-binding; Transit peptide.
FT TRANSIT 1 25 Mitochondrion (Potential).
FT CHAIN 26 555 ATP-dependent RNA helicase MRH4,
FT mitochondrial.
FT /FTId=PRO_0000232350.
FT DOMAIN 144 361 Helicase ATP-binding.
FT DOMAIN 395 555 Helicase C-terminal.
FT NP_BIND 157 164 ATP (By similarity).
FT MOTIF 101 108 Q motif.
FT MOTIF 309 312 DEAD box.
SQ SEQUENCE 555 AA; 62513 MW; BBDD502F6D3E681C CRC64;
MFKLLIPNKY NYVIRPLVRF KSIKSPKSPK PKPTAKLSPN VFSSGKFSQL HNDTSTTNIE
SKITSFDQLK IFPSVREAMI KEIKSQYNLK GPRHSNIDEI DIKPTPVQIA AIRKINQTRK
LKVPNKDLEG MDDAERIQFE LQNANEIQKT KVFTVAAETG SGKTWSYLAP LLSKLKSDDM
EFWKSDPEGY DNTRKKGQFV KSVILLPTNE LVDQVYETLQ RANSFELEHK 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
//
