ID   MS116_ASPOR             Reviewed;         633 AA.
AC   Q2UST1;
DT   31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   24-JAN-2006, sequence version 1.
DT   03-AUG-2022, entry version 89.
DE   RecName: Full=ATP-dependent RNA helicase mss116, mitochondrial;
DE            EC=3.6.4.13;
DE   Flags: Precursor;
GN   Name=mss116; ORFNames=AO090005000305;
OS   Aspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Circumdati.
OX   NCBI_TaxID=510516;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 42149 / RIB 40;
RX   PubMed=16372010; DOI=10.1038/nature04300;
RA   Machida M., Asai K., Sano M., Tanaka T., Kumagai T., Terai G., Kusumoto K.,
RA   Arima T., Akita O., Kashiwagi Y., Abe K., Gomi K., Horiuchi H.,
RA   Kitamoto K., Kobayashi T., Takeuchi M., Denning D.W., Galagan J.E.,
RA   Nierman W.C., Yu J., Archer D.B., Bennett J.W., Bhatnagar D.,
RA   Cleveland T.E., Fedorova N.D., Gotoh O., Horikawa H., Hosoyama A.,
RA   Ichinomiya M., Igarashi R., Iwashita K., Juvvadi P.R., Kato M., Kato Y.,
RA   Kin T., Kokubun A., Maeda H., Maeyama N., Maruyama J., Nagasaki H.,
RA   Nakajima T., Oda K., Okada K., Paulsen I., Sakamoto K., Sawano T.,
RA   Takahashi M., Takase K., Terabayashi Y., Wortman J.R., Yamada O.,
RA   Yamagata Y., Anazawa H., Hata Y., Koide Y., Komori T., Koyama Y.,
RA   Minetoki T., Suharnan S., Tanaka A., Isono K., Kuhara S., Ogasawara N.,
RA   Kikuchi H.;
RT   "Genome sequencing and analysis of Aspergillus oryzae.";
RL   Nature 438:1157-1161(2005).
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; AP007151; BAE55384.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q2UST1; -.
DR   SMR; Q2UST1; -.
DR   STRING; 510516.Q2UST1; -.
DR   EnsemblFungi; BAE55384; BAE55384; AO090005000305.
DR   VEuPathDB; FungiDB:AO090005000305; -.
DR   HOGENOM; CLU_003041_26_6_1; -.
DR   OMA; KAIVFAP; -.
DR   Proteomes; UP000006564; Chromosome 1.
DR   GO; GO:0005759; C:mitochondrial matrix; 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   GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR   GO; GO:0006417; P:regulation of translation; IEA:UniProtKB-KW.
DR   GO; GO:0008380; P:RNA splicing; IEA:UniProtKB-KW.
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; 2.
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..32
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255"
FT   CHAIN           33..633
FT                   /note="ATP-dependent RNA helicase mss116, mitochondrial"
FT                   /id="PRO_0000256009"
FT   DOMAIN          70..248
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT   DOMAIN          262..429
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT   REGION          567..633
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           38..66
FT                   /note="Q motif"
FT   MOTIF           195..198
FT                   /note="DEAD box"
FT   BINDING         83..90
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ   SEQUENCE   633 AA;  68795 MW;  FE68D13FD0EFB770 CRC64;
     MKTGRTRPLR VFDILVPPWP PTVPHRIKLP RGKTNWFEFY SAITRNWNKL KGLKNCWQIW
     KDVQEIIRRI RKYQGESTVM QGPGNNDGAH PYATMAGKLD SKLLQALKVM EFEYMTPVQH
     RVLTELPSWR SDCLVQAKTG TGKTLAFLLP TLHCLLQGHS APPRGQVAIL IITPTRELAQ
     QIAKSCDQLT SQLARPLECH IAVGGTARAS ALARFMKGAP SILVATPGRL KDYLSEPSTA
     EKLSNIQTLI LDEADTMLES GFLADVKRIL QLIPPKSTGW QGMCFSATVP PKVKDVVSVV
     LKPGYTSIST IEKNETPTHE RVPQYHVLIP SVADTFTTLA SLLNLEIKNS SKIIVFGVTA
     NMVALFAAAF SQGLTPLKVF EIHSRLSQSA RTKTTALFKE AATGIMFASD VIGRGMDFPN
     VDLVIQVGLP SNGEQYVHRV GRTARAGNDG RAIILLTEAE SFFMKVNRHL PIQPHPQTDA
     INAGASSCAD AVTKAMYSIG EETKQRAYSS YIGFFAGSGL LKQVRLDKPG LVQLANELAI
     QGMGCPEPPP MDKKVVGKMG LKGVPGFNYA TGNDLNGDRP ARPRGRPGNK TRDVLSPGAG
     QGDRRGSVSK NRGGRRGGGR GGRGGRGGKP RAA