MS116_LODEL
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 03-AUG-2022, entry version 71.
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 / BCRC 21390 / CBS 2605 / JCM 1781 / NBRC 1676 / NRRL
RC 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}.
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DR EMBL; CH981524; EDK42515.1; -; Genomic_DNA.
DR RefSeq; XP_001528173.1; XM_001528123.1.
DR AlphaFoldDB; A5DTK7; -.
DR SMR; A5DTK7; -.
DR STRING; 379508.A5DTK7; -.
DR EnsemblFungi; EDK42515; EDK42515; LELG_00693.
DR GeneID; 5235040; -.
DR KEGG; lel:LELG_00693; -.
DR VEuPathDB; FungiDB:LELG_00693; -.
DR eggNOG; KOG0342; Eukaryota.
DR HOGENOM; CLU_003041_26_6_1; -.
DR InParanoid; A5DTK7; -.
DR OMA; IGFKEDL; -.
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: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..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 REGION 82..113
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 643..692
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 130..158
FT /note="Q motif"
FT MOTIF 290..293
FT /note="DEAD box"
FT COMPBIAS 89..107
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 175..182
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
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
