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MS116_ASHGO
ID   MS116_ASHGO             Reviewed;         658 AA.
AC   Q750Q4;
DT   21-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 104.
DE   RecName: Full=ATP-dependent RNA helicase MSS116, mitochondrial;
DE            EC=3.6.4.13;
DE   Flags: Precursor;
GN   Name=MSS116; OrderedLocusNames=AGL112C;
OS   Ashbya gossypii (strain ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056)
OS   (Yeast) (Eremothecium gossypii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Eremothecium.
OX   NCBI_TaxID=284811;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX   PubMed=15001715; DOI=10.1126/science.1095781;
RA   Dietrich F.S., Voegeli S., Brachat S., Lerch A., Gates K., Steiner S.,
RA   Mohr C., Poehlmann R., Luedi P., Choi S., Wing R.A., Flavier A.,
RA   Gaffney T.D., Philippsen P.;
RT   "The Ashbya gossypii genome as a tool for mapping the ancient Saccharomyces
RT   cerevisiae genome.";
RL   Science 304:304-307(2004).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX   PubMed=23749448; DOI=10.1534/g3.112.002881;
RA   Dietrich F.S., Voegeli S., Kuo S., Philippsen P.;
RT   "Genomes of Ashbya fungi isolated from insects reveal four mating-type
RT   loci, numerous translocations, lack of transposons, and distinct gene
RT   duplications.";
RL   G3 (Bethesda) 3:1225-1239(2013).
CC   -!- FUNCTION: ATP-dependent RNA helicase required for mitochondrial
CC       splicing of group I and II introns. Also required for efficient
CC       mitochondrial translation (By 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 matrix {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. DDX18/HAS1
CC       subfamily. {ECO:0000305}.
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DR   EMBL; AE016820; AAS54379.1; -; Genomic_DNA.
DR   RefSeq; NP_986555.1; NM_211617.1.
DR   AlphaFoldDB; Q750Q4; -.
DR   SMR; Q750Q4; -.
DR   STRING; 33169.AAS54379; -.
DR   EnsemblFungi; AAS54379; AAS54379; AGOS_AGL112C.
DR   GeneID; 4622854; -.
DR   KEGG; ago:AGOS_AGL112C; -.
DR   eggNOG; KOG0342; Eukaryota.
DR   HOGENOM; CLU_003041_26_6_1; -.
DR   InParanoid; Q750Q4; -.
DR   Proteomes; UP000000591; Chromosome VII.
DR   GO; GO:0005759; C:mitochondrial matrix; 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:0003724; F:RNA helicase activity; IEA:UniProtKB-EC.
DR   GO; GO:0033592; F:RNA strand annealing activity; IEA:EnsemblFungi.
DR   GO; GO:0000372; P:Group I intron splicing; IEA:EnsemblFungi.
DR   GO; GO:0000373; P:Group II intron splicing; IEA:EnsemblFungi.
DR   GO; GO:0000963; P:mitochondrial RNA processing; IEA:EnsemblFungi.
DR   GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR   GO; GO:0006417; P:regulation of translation; IEA:UniProtKB-KW.
DR   GO; GO:0034337; P:RNA folding; IEA:EnsemblFungi.
DR   GO; GO:0006364; P:rRNA processing; IBA:GO_Central.
DR   GO; GO:0006392; P:transcription elongation from mitochondrial promoter; IEA:EnsemblFungi.
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.
DR   PROSITE; PS51195; Q_MOTIF; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Helicase; Hydrolase; Mitochondrion; mRNA processing;
KW   mRNA splicing; Nucleotide-binding; Reference proteome; RNA-binding;
KW   Transit peptide; Translation regulation.
FT   TRANSIT         1..35
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255"
FT   CHAIN           36..658
FT                   /note="ATP-dependent RNA helicase MSS116, mitochondrial"
FT                   /id="PRO_0000227943"
FT   DOMAIN          158..343
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT   DOMAIN          372..528
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT   REGION          40..104
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           126..154
FT                   /note="Q motif"
FT   MOTIF           284..287
FT                   /note="DEAD box"
FT   COMPBIAS        44..97
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         171..178
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ   SEQUENCE   658 AA;  73643 MW;  297B93E00A339D04 CRC64;
     MFRVTGIATA RAVALQPFRA PLGVIRRFGI SATASYEFQH GHDMQSRNGS RWDSRRQGDR
     RSSRWEGRGS DREDGERGSR GGMWRKPQGR RGRTDGAARE GFSLGPNTEV VRVADEAAGV
     ESTPRTLVEE GVLSNELYEM LQSRGFDKLT PVQQKTLKPI LQTEHDVVAR AKTGTGKTLA
     FLMPLFQRLL EGPPSENVKA VVIAPTRDLA AQIFNEINEM RNANRKLRRF NAVVMMGGSS
     RTETFRSLER RRPNIVVATP GRLIDMLEAC GPKYFTEVDF KVLDEADTLL EIGFKQALEQ
     INDILNQLNQ KGTTHIRTLL VSATLDDKVQ SLANSIMNHA KCLFIDTVDP NEQATNENIA
     QKVVISKDFA DNITASLYKI REEASANPKL KAIVFMPTIV AVEYWGELLQ SQCRGTPVLL
     FHGGLSQGRR NSTMKRFRAM DSGILVCTDV AARGMDVSDV QHVYQVGVPT SPDNYIHRIG
     RTGRAGRKGS STIFLAEHEL CILDILRRKN NVVISDQETF DAAAQELSDV REAFSLDRDR
     LHDFLLKNLS FYRGSQGEYD FPLEAYISIA RAYGTLLGDS NQRLTLSGRM LTTFVPNHPA
     VCSLFNIIGP VNSKSSYGFR DTNKRHRRGR LDDSGRLEYS KKRHSYARSY SPSISDGF
 
 
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