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
