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Database: UniProt
Entry: A5DTK7
LinkDB: A5DTK7
Original site: A5DTK7 
ID   MS116_LODEL             Reviewed;         692 AA.
AC   A5DTK7;
DT   10-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT   12-JUN-2007, sequence version 1.
DT   11-DEC-2019, entry version 63.
DE   RecName: Full=ATP-dependent RNA helicase MSS116, mitochondrial;
DE            EC=3.6.4.13;
DE   Flags: Precursor;
GN   Name=MSS116; ORFNames=LELG_00693;
OS   Lodderomyces elongisporus (strain ATCC 11503 / CBS 2605 / JCM 1781 / NBRC
OS   1676 / NRRL YB-4239) (Yeast) (Saccharomyces elongisporus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade;
OC   Lodderomyces.
OX   NCBI_TaxID=379508;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 11503 / CBS 2605 / JCM 1781 / NBRC 1676 / NRRL YB-4239;
RX   PubMed=19465905; DOI=10.1038/nature08064;
RA   Butler G., Rasmussen M.D., Lin M.F., Santos M.A.S., Sakthikumar S.,
RA   Munro C.A., Rheinbay E., Grabherr M., Forche A., Reedy J.L., Agrafioti I.,
RA   Arnaud M.B., Bates S., Brown A.J.P., Brunke S., Costanzo M.C.,
RA   Fitzpatrick D.A., de Groot P.W.J., Harris D., Hoyer L.L., Hube B.,
RA   Klis F.M., Kodira C., Lennard N., Logue M.E., Martin R., Neiman A.M.,
RA   Nikolaou E., Quail M.A., Quinn J., Santos M.C., Schmitzberger F.F.,
RA   Sherlock G., Shah P., Silverstein K.A.T., Skrzypek M.S., Soll D.,
RA   Staggs R., Stansfield I., Stumpf M.P.H., Sudbery P.E., Srikantha T.,
RA   Zeng Q., Berman J., Berriman M., Heitman J., Gow N.A.R., Lorenz M.C.,
RA   Birren B.W., Kellis M., Cuomo C.A.;
RT   "Evolution of pathogenicity and sexual reproduction in eight Candida
RT   genomes.";
RL   Nature 459:657-662(2009).
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}.
DR   EMBL; CH981524; EDK42515.1; -; Genomic_DNA.
DR   RefSeq; XP_001528173.1; XM_001528123.1.
DR   SMR; A5DTK7; -.
DR   STRING; 36914.XP_001528173.1; -.
DR   PRIDE; A5DTK7; -.
DR   EnsemblFungi; EDK42515; EDK42515; LELG_00693.
DR   GeneID; 5235040; -.
DR   KEGG; lel:LELG_00693; -.
DR   eggNOG; KOG0342; Eukaryota.
DR   eggNOG; COG0513; LUCA.
DR   InParanoid; A5DTK7; -.
DR   KO; K17679; -.
DR   OMA; VHENIHQ; -.
DR   OrthoDB; 537587at2759; -.
DR   Proteomes; UP000001996; 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: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   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; IPR014014; RNA_helicase_DEAD_Q_motif.
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..37
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255"
FT   CHAIN           38..692
FT                   /note="ATP-dependent RNA helicase MSS116, mitochondrial"
FT                   /id="PRO_0000294629"
FT   DOMAIN          162..349
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT   DOMAIN          384..534
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT   NP_BIND         175..182
FT                   /note="ATP"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT   MOTIF           130..158
FT                   /note="Q motif"
FT   MOTIF           290..293
FT                   /note="DEAD box"
FT   COMPBIAS        617..683
FT                   /note="Gly-rich"
SQ   SEQUENCE   692 AA;  77154 MW;  896E371C179D0F3B CRC64;
     MMIARFGKQV LRKNVLVSNR IHFPVISRGF HNSFINKSDD LKSPPIDITK GQTEAKVETK
     KDKFAGFGLD LDELIGETAK GSQVTEQTEL TKSEEEEKKK KNINTNTNKN DRKSVPAISL
     EDFNPSQFKD FKNTGLIDDV ILRALDRAHF KDLTPIQQKS IVPLLETERG MVCRAKTGTG
     KTLTFLIPTL QSAVSRKIAS GGRSSGVDTV IIVPTRDLAL QIYDEYQKVL RGISGSRKPH
     ISYVIGGMKN SFNPRNPSEI VIATPGRLEA DLRSPLFASA FTDIKYRVYD EADRLLDVGF
     EPTLDSIDRS IKMIRSDDAE PLKSLLFSAT VDARLDQFAK QHINKKYDYI NTVPEDDPEV
     HENIHQVMYK CKDAIDKFGS FFNYVNQLVK DSPDMKMMVF LPTQTAVEFL YSYMSEACHK
     HDVDIDIFHL HGKRSASQRQ RALSNFKRDD SGILITTDVA ARGIDVKGVT HVVQLFPSSE
     IADYVHKVGR TGRAGKEGKA VLFITQPEMA YVRRLNSERG VTFEQVHESS EIDNSIDFFE
     GMRPDEQVAN DFFYTLMSFL AQISSTYRLR ADDLVAENVS LYRAILQKPD AKLSLRAASA
     LIKRLNRDVV REFFEQGRGG NNGGYGGYGG YGGSSYGRSG GSNRYSGGGG NRSEKRFSFA
     GRGGNSGGHS GRGRGGRSGY SGGRSSQYSD WE
//
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