(data stored in ACNUC8465 zone)

SWISSPROT: 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   30-AUG-2017, entry version 82.
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 /
OS   NRRL Y-65) (Yeast) (Torulopsis glabrata).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
OC   Saccharomycetes; 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.,
RA   Lafontaine I., de Montigny J., Marck C., Neuveglise C., Talla E.,
RA   Goffard N., Frangeul L., Aigle M., Anthouard V., Babour A., Barbe V.,
RA   Barnay S., Blanchin S., Beckerich J.-M., Beyne E., Bleykasten C.,
RA   Boisrame A., Boyer J., Cattolico L., Confanioleri F., de Daruvar A.,
RA   Despons L., Fabre E., Fairhead C., Ferry-Dumazet H., Groppi A.,
RA   Hantraye F., Hennequin C., Jauniaux N., Joyet P., Kachouri R.,
RA   Kerrest A., Koszul R., Lemaire M., Lesur I., Ma L., Muller H.,
RA   Nicaud J.-M., Nikolski M., Oztas S., Ozier-Kalogeropoulos O.,
RA   Pellenz S., Potier S., Richard G.-F., Straub M.-L., Suleau A.,
RA   Swennen D., Tekaia F., Wesolowski-Louvel M., Westhof E., Wirth B.,
RA   Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M., Thierry A.,
RA   Bouchier C., Caudron B., Scarpelli C., Gaillardin C., Weissenbach J.,
RA   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: ATP + H(2)O = ADP + phosphate.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250}.
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. {ECO:0000305}.
DR   EMBL; CR380959; CAG62572.1; -; Genomic_DNA.
DR   RefSeq; XP_449596.1; XM_449596.1.
DR   ProteinModelPortal; Q6FJJ8; -.
DR   STRING; 284593.XP_449596.1; -.
DR   EnsemblFungi; CAG62572; CAG62572; CAGL0M05753g.
DR   KEGG; cgr:CAGL0M05753g; -.
DR   CGD; CAL0136825; CAGL0M05753g.
DR   EuPathDB; FungiDB:CAGL0M05753g; -.
DR   eggNOG; KOG0335; Eukaryota.
DR   eggNOG; ENOG410XNTI; LUCA.
DR   HOGENOM; HOG000065970; -.
DR   InParanoid; Q6FJJ8; -.
DR   KO; K17678; -.
DR   OMA; WSIGKAG; -.
DR   OrthoDB; EOG092C2Z1Z; -.
DR   Proteomes; UP000002428; Chromosome M.
DR   GO; GO:0005762; C:mitochondrial large ribosomal subunit; IEA:EnsemblFungi.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004004; F:ATP-dependent RNA helicase activity; IEA:EnsemblFungi.
DR   GO; GO:1990400; F:mitochondrial ribosomal large subunit rRNA binding; IEA:EnsemblFungi.
DR   GO; GO:1902775; P:mitochondrial large ribosomal subunit assembly; IEA:EnsemblFungi.
DR   GO; GO:0016070; P:RNA metabolic process; IEA:EnsemblFungi.
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; 2.
DR   PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR   PROSITE; PS51194; HELICASE_CTER; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q6FJJ8.
DR   SWISS-2DPAGE; Q6FJJ8.
KW   ATP-binding; Complete proteome; Helicase; Hydrolase; Mitochondrion;
KW   Nucleotide-binding; Reference proteome; RNA-binding; Transit peptide.
FT   TRANSIT       1     50       Mitochondrion. {ECO:0000255}.
FT   CHAIN        51    568       ATP-dependent RNA helicase MRH4,
FT                                mitochondrial.
FT                                /FTId=PRO_0000232351.
FT   DOMAIN      160    348       Helicase ATP-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00541}.
FT   DOMAIN      379    568       Helicase C-terminal.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00542}.
FT   NP_BIND     173    180       ATP. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00541}.
FT   MOTIF       143    150       Q motif.
FT   MOTIF       296    299       DEAD box.
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
//

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