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MRH4_DEBHA
ID   MRH4_DEBHA              Reviewed;         593 AA.
AC   Q6BV94;
DT   04-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT   16-AUG-2004, sequence version 1.
DT   03-AUG-2022, entry version 96.
DE   RecName: Full=ATP-dependent RNA helicase MRH4, mitochondrial;
DE            EC=3.6.4.13;
DE   Flags: Precursor;
GN   Name=MRH4; OrderedLocusNames=DEHA2C04378g;
OS   Debaryomyces hansenii (strain ATCC 36239 / CBS 767 / BCRC 21394 / JCM 1990
OS   / NBRC 0083 / IGC 2968) (Yeast) (Torulaspora hansenii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Debaryomyces.
OX   NCBI_TaxID=284592;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 36239 / CBS 767 / BCRC 21394 / JCM 1990 / NBRC 0083 / IGC 2968;
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; CR382135; CAG85921.1; -; Genomic_DNA.
DR   RefSeq; XP_457875.1; XM_457875.1.
DR   AlphaFoldDB; Q6BV94; -.
DR   SMR; Q6BV94; -.
DR   STRING; 4959.XP_457875.1; -.
DR   PRIDE; Q6BV94; -.
DR   EnsemblFungi; CAG85921; CAG85921; DEHA2C04378g.
DR   GeneID; 2900163; -.
DR   KEGG; dha:DEHA2C04378g; -.
DR   VEuPathDB; FungiDB:DEHA2C04378g; -.
DR   eggNOG; KOG0335; Eukaryota.
DR   HOGENOM; CLU_003041_18_0_1; -.
DR   InParanoid; Q6BV94; -.
DR   OMA; FHALKMQ; -.
DR   OrthoDB; 1223767at2759; -.
DR   Proteomes; UP000000599; Chromosome C.
DR   GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
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   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..36
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255"
FT   CHAIN           37..593
FT                   /note="ATP-dependent RNA helicase MRH4, mitochondrial"
FT                   /id="PRO_0000232352"
FT   DOMAIN          177..399
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT   DOMAIN          433..593
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT   MOTIF           132..139
FT                   /note="Q motif"
FT   MOTIF           347..350
FT                   /note="DEAD box"
FT   BINDING         190..197
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ   SEQUENCE   593 AA;  66876 MW;  0E04DD3B843B0C96 CRC64;
     MTLKIGGIVP IVRVMRDTII QRPVSTFVRY HSKRSRSFKK KANHKPGQVI RSKLGKTLEA
     PKTQPKLFSF GNFSGLDQPE NKLKEMSSNA IKNITSFESL RIFPTVRSAM LEEIKYGYNL
     KSTYIKSKEE LEIKPSPVQI AAIRKINQPR LRNVNAEKKL ADKKASGQEI LEDLQKSNEM
     NRLKIFTIAA ETGSGKTWAY LAPLLSKLKE EDMRVFNMSE QSYADAKKTS IIRSVILLPT
     HELVEQVYDS LKRASKASID LEASVNKKIL QDPQYARYLS LPENQTSLNL NVVKWGSGDS
     HQKLFDAGRK RIDVLVTTPA KIQGLAKLNN VSRPFRLFNF VEYCVVDEAD TLMDKSWIVD
     TTSVIRRLSK CKDLIFCSAT IPKEFKKTLG KMFPDEFSII NIVTPSLHKI PKQINLKVID
     AQLSPYNGSK TRCLAQALYA IHNDGTEQGY VKRILVFVNE KRDVQPLADT LIEKFGHREE
     DIIGITGADN ADDRLAKIEP FLKPAELLEE DLDGSKVKVL ITTDLLARGL NFNGIKNVIL
     MDLPNTSVDL VHRVGRTGRM RQSGRVFVII DKKTGKSWIK GLPKVIKKGI PLG
 
 
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