ID   MS116_CANGA             Reviewed;         666 AA.
AC   Q6FU81;
DT   31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 107.
DE   RecName: Full=ATP-dependent RNA helicase MSS116, mitochondrial;
DE            EC=3.6.4.13;
DE   Flags: Precursor;
GN   Name=MSS116; OrderedLocusNames=CAGL0F05577g;
OS   Candida glabrata (strain ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL
OS   Y-65) (Yeast) (Torulopsis glabrata).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Nakaseomyces;
OC   Nakaseomyces/Candida clade.
OX   NCBI_TaxID=284593;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL Y-65;
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-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; CR380952; CAG59137.1; -; Genomic_DNA.
DR   RefSeq; XP_446213.1; XM_446213.1.
DR   AlphaFoldDB; Q6FU81; -.
DR   SMR; Q6FU81; -.
DR   STRING; 5478.XP_446213.1; -.
DR   PRIDE; Q6FU81; -.
DR   EnsemblFungi; CAG59137; CAG59137; CAGL0F05577g.
DR   GeneID; 2887713; -.
DR   KEGG; cgr:CAGL0F05577g; -.
DR   CGD; CAL0129558; CAGL0F05577g.
DR   VEuPathDB; FungiDB:CAGL0F05577g; -.
DR   eggNOG; KOG0342; Eukaryota.
DR   HOGENOM; CLU_003041_26_6_1; -.
DR   InParanoid; Q6FU81; -.
DR   OMA; IGFKEDL; -.
DR   Proteomes; UP000002428; Chromosome F.
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: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: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   InterPro; IPR000629; RNA-helicase_DEAD-box_CS.
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; PS00039; DEAD_ATP_HELICASE; 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..22
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255"
FT   CHAIN           23..666
FT                   /note="ATP-dependent RNA helicase MSS116, mitochondrial"
FT                   /id="PRO_0000256010"
FT   DOMAIN          192..379
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT   DOMAIN          408..560
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT   REGION          38..131
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           159..187
FT                   /note="Q motif"
FT   MOTIF           320..323
FT                   /note="DEAD box"
FT   COMPBIAS        38..67
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        90..131
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         205..212
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ   SEQUENCE   666 AA;  76320 MW;  B79E1E88156C9130 CRC64;
     MLRHCSLGLV TTQISAIAPL RLVGSPLFCR SYQDFAGRDR RSSRSREDKP YNSRTRRFDD
     EGSSNYSSSR DDYRGQNTYG FRGKAPRKNF SSRDNYSSRD NFRSSNGFQE RGYKNKFSKN
     TKSYSKGGNT SGSFIPEGKM AKMTHIGKSD SDIVVTLESL LEKNVISRDL YDSISRMGFE
     QLTPVQQKTI EPIITNSDSD IIARAKTGTG KTFAFLLPIF QHLLNTKIDS QNKVKSVIVA
     PTRDLALQIE DEVRKIHSKN RKLKAFECVS LVGGTNFDRS IRYIEKVSPS IVIGTPGRLI
     DVMEKFGNKF FKDVDFKVLD EADRLLEIGF KEDLSYINKM LNTLNTNSTE HIRTLLFSAT
     LDHKVQSLSN DIMNKEECLY IDTIDENEPQ AHEKIDQTLV VGETFADNLY AAIEHIREFG
     TKTPNYKSIL FLPTVKFTKF MATILKRQVK LPIYEFHGQI DQKKRTRIVN EFKTMKKGLL
     VCTDVGARGM DFPNITEVLQ IGLPSEIPNY IHRIGRTARS GKEGSSVTFI SKEELPFFEI
     LEDKHNVTIK NIRKFEAQPH VMADLSLRLH VSEDELQEII LSVISFYRAC LKDYGINYKN
     MLPQIAHTYG TLLQNEDKRI PLAGNHILNR LGMDRDPIAT KMFQIDEMPN QYNRRGPRSN
     YNRRRF