MS116_KLULA
ID MS116_KLULA Reviewed; 685 AA.
AC Q6CQA1;
DT 31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 1.
DT 03-AUG-2022, entry version 102.
DE RecName: Full=ATP-dependent RNA helicase MSS116, mitochondrial;
DE EC=3.6.4.13;
DE Flags: Precursor;
GN Name=MSS116; OrderedLocusNames=KLLA0D18667g;
OS Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 /
OS NRRL Y-1140 / WM37) (Yeast) (Candida sphaerica).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Kluyveromyces.
OX NCBI_TaxID=284590;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37;
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; CR382124; CAH00984.1; -; Genomic_DNA.
DR RefSeq; XP_453888.1; XM_453888.1.
DR AlphaFoldDB; Q6CQA1; -.
DR SMR; Q6CQA1; -.
DR STRING; 28985.XP_453888.1; -.
DR EnsemblFungi; CAH00984; CAH00984; KLLA0_D18667g.
DR GeneID; 2893113; -.
DR KEGG; kla:KLLA0_D18667g; -.
DR eggNOG; KOG0342; Eukaryota.
DR HOGENOM; CLU_003041_26_6_1; -.
DR InParanoid; Q6CQA1; -.
DR OMA; IGFKEDL; -.
DR Proteomes; UP000000598; Chromosome D.
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 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..34
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 35..685
FT /note="ATP-dependent RNA helicase MSS116, mitochondrial"
FT /id="PRO_0000256011"
FT DOMAIN 170..357
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 386..542
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT REGION 42..107
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 633..685
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 138..166
FT /note="Q motif"
FT MOTIF 298..301
FT /note="DEAD box"
FT COMPBIAS 53..76
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 83..100
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 657..685
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 183..190
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ SEQUENCE 685 AA; 78559 MW; B918E392317AA3BB CRC64;
MLVLQRIPKR ALQFNGVTGT VCSTRLFHHA FNLNLQQSFV PSEERRYRNS NRGFTRGSDS
NSNNKYRNSS YDDNRSRSNY GGDKRNNRNN NNYGNNRNNG SRRRYQDENS DIEVFKSKSF
NVTTLNPESF HEQVTIDSLL EESLLDANVH KAISAMKFES LTPVQQRTIK PILTTENDVV
AKAKTGTGKT LAFLAPLFQH LISTKLQNPL AVKAVIVTPT RDLAIQIASE VKKLQQCNPS
LKSYRSLTLI GGTNLDKSLK DLHTLNPNII VGTPGRINDI LDRVGAKYFK DVDFKVLDEA
DTLLQIGFQT ELSLISRKLN EFNTQGEEHI RTLLFSATMD HNVQELAATI MNKKDCLFID
TVDKNDSEAH DSIDQKLVIT KSFAESMVAL IQSIESELLQ KKNFKAILFL PTVKFVDFFS
ETLSESLTKR IDIIKFHGKI DQKKRTKLVD RFKKTNHGIF VCTDVGARGM HFPSVEHVYQ
LCVPTSLPNY IHRIGRTARA GESGAATIFL FREELKFVDE LRRDTNVVIK NQEDYLNQDK
ENFDMISSII TNNPDFPEAL KSIIGFYKGV QNEYRLNYKV AQNVLRSFSE LHSDSSMLLR
FRPSEINNFF SNRDMRFVSD LIDVKNPHSF GKDREFDDED RYTSRSQNNY KSKQSSKSNR
FEGRNDYSNS RRSHANQKRN FTFDD
