ID   MS116_PHANO             Reviewed;         550 AA.
AC   Q0UG00;
DT   31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   05-SEP-2006, sequence version 1.
DT   03-AUG-2022, entry version 81.
DE   RecName: Full=ATP-dependent RNA helicase MSS116, mitochondrial;
DE            EC=3.6.4.13;
DE   Flags: Precursor;
GN   Name=MSS116; ORFNames=SNOG_09314;
OS   Phaeosphaeria nodorum (strain SN15 / ATCC MYA-4574 / FGSC 10173) (Glume
OS   blotch fungus) (Parastagonospora nodorum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Pleosporomycetidae; Pleosporales; Pleosporineae; Phaeosphaeriaceae;
OC   Parastagonospora.
OX   NCBI_TaxID=321614;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SN15 / ATCC MYA-4574 / FGSC 10173;
RX   PubMed=18024570; DOI=10.1105/tpc.107.052829;
RA   Hane J.K., Lowe R.G.T., Solomon P.S., Tan K.-C., Schoch C.L.,
RA   Spatafora J.W., Crous P.W., Kodira C.D., Birren B.W., Galagan J.E.,
RA   Torriani S.F.F., McDonald B.A., Oliver R.P.;
RT   "Dothideomycete-plant interactions illuminated by genome sequencing and EST
RT   analysis of the wheat pathogen Stagonospora nodorum.";
RL   Plant Cell 19:3347-3368(2007).
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; CH445338; EAT83506.1; -; Genomic_DNA.
DR   RefSeq; XP_001799609.1; XM_001799557.1.
DR   AlphaFoldDB; Q0UG00; -.
DR   SMR; Q0UG00; -.
DR   STRING; 13684.SNOT_09314; -.
DR   EnsemblFungi; SNOT_09314; SNOT_09314; SNOG_09314.
DR   GeneID; 5976510; -.
DR   KEGG; pno:SNOG_09314; -.
DR   eggNOG; KOG0342; Eukaryota.
DR   HOGENOM; CLU_003041_26_6_1; -.
DR   InParanoid; Q0UG00; -.
DR   OMA; KAIVFAP; -.
DR   OrthoDB; 537587at2759; -.
DR   Proteomes; UP000001055; Unassembled WGS sequence.
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; 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..41
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255"
FT   CHAIN           42..550
FT                   /note="ATP-dependent RNA helicase MSS116, mitochondrial"
FT                   /id="PRO_0000256012"
FT   DOMAIN          103..285
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT   DOMAIN          316..472
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT   REGION          1..51
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           71..99
FT                   /note="Q motif"
FT   MOTIF           230..233
FT                   /note="DEAD box"
FT   COMPBIAS        21..36
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         116..123
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ   SEQUENCE   550 AA;  59705 MW;  7103B1C05E7477BC CRC64;
     MPPPPKRKWP NRPRGGGGAN GSASGTPTTP RSTVAQQPKR PKVEDAAPAA EGVDVKQMYS
     TSAGNASAKP FSELSSVLDK SLLDGLDKMG FEFMSPVQQK VLTELPSLSS DCVVQAKTGT
     GKTVAFLLPA IQNLLAGNMP PRGKVAILVV CPTRELALQI AKECNGVTAC LPRKMECHTA
     FGGTSRASNL KAFLNGNPTI LVATPGRLDD ILGEEHVRER FTHLKTVVLD EADQMLDAGF
     APAVKKILRR IPPKSDGWQG MCFSATLPKE VLDIAKIVLF PGFTHLTTVD PNEVPTHERV
     PQYFLSVPNV GQTFAALSAL IQEEHKQDPT DFKAIVFGTT ANGVGLLYDL YKHALPQFRV
     FELHSRMSQP MRTRTTAQFK EATSGILFAS DVVGRGMDFP NVGLVVQLGL PSSTEQYVHR
     VGRTARAGKD GRAVLVLFEK EAFFPRINRT LPIKPYPVDI AAKVPEQEAA ITRAFANVEE
     EAKAKAYQAF LGYNKTFLKK LQLSTTELVR VANEYSRAMG CPEPPLIEKS TIGKMGLKGV
     PGLNIGSRRH