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Database: UniProt
Entry: Q59S59
LinkDB: Q59S59
Original site: Q59S59 
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-SEP-2014, entry version 53.
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   KO; K17678; -.
DR   OrthoDB; EOG79W9DT; -.
DR   GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004386; F:helicase activity; IEA:UniProtKB-KW.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.300; -; 3.
DR   InterPro; IPR011545; DNA/RNA_helicase_DEAD/DEAH_N.
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; 3.
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
//
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