MS116_YEAST
ID MS116_YEAST Reviewed; 664 AA.
AC P15424; D6VSH6;
DT 01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-1990, sequence version 1.
DT 03-AUG-2022, entry version 204.
DE RecName: Full=ATP-dependent RNA helicase MSS116, mitochondrial;
DE EC=3.6.4.13;
DE Flags: Precursor;
GN Name=MSS116; OrderedLocusNames=YDR194C; ORFNames=YD9346.05C;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RX PubMed=2535893; DOI=10.1038/337084a0;
RA Seraphin B., Simon M., Boulet A., Faye G.;
RT "Mitochondrial splicing requires a protein from a novel helicase family.";
RL Nature 337:84-87(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169867;
RA Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G.,
RA Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C.,
RA Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F.,
RA Delaveau T., del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M.,
RA Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T.,
RA Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C.,
RA Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S.,
RA Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L.,
RA Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H.,
RA Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M.,
RA Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M.,
RA Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A.,
RA Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G.,
RA Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E.,
RA Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S.,
RA Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D.,
RA Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V.,
RA Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E.,
RA Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M.,
RA Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D.,
RA Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X.,
RA Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A.,
RA Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R.,
RA Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T.,
RA Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L.,
RA Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E.,
RA Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L.,
RA Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M.,
RA Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K.,
RA Mewes H.-W., Zollner A., Zaccaria P.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV.";
RL Nature 387:75-78(1997).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [4]
RP FUNCTION.
RX PubMed=7567443; DOI=10.1093/nar/23.15.2966;
RA Niemer I., Schmelzer C., Boerner G.V.;
RT "Overexpression of DEAD box protein pMSS116 promotes ATP-dependent splicing
RT of a yeast group II intron in vitro.";
RL Nucleic Acids Res. 23:2966-2972(1995).
RN [5]
RP FUNCTION.
RX PubMed=12402239; DOI=10.1002/yea.906;
RA Minczuk M., Dmochowska A., Palczewska M., Stepien P.P.;
RT "Overexpressed yeast mitochondrial putative RNA helicase Mss116 partially
RT restores proper mtRNA metabolism in strains lacking the Suv3 mtRNA
RT helicase.";
RL Yeast 19:1285-1293(2002).
RN [6]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=14562095; DOI=10.1038/nature02026;
RA Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA Weissman J.S., O'Shea E.K.;
RT "Global analysis of protein localization in budding yeast.";
RL Nature 425:686-691(2003).
RN [7]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [8]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RC STRAIN=ATCC 76625 / YPH499;
RX PubMed=14576278; DOI=10.1073/pnas.2135385100;
RA Sickmann A., Reinders J., Wagner Y., Joppich C., Zahedi R.P., Meyer H.E.,
RA Schoenfisch B., Perschil I., Chacinska A., Guiard B., Rehling P.,
RA Pfanner N., Meisinger C.;
RT "The proteome of Saccharomyces cerevisiae mitochondria.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:13207-13212(2003).
RN [9]
RP FUNCTION.
RX PubMed=15618406; DOI=10.1073/pnas.0407896101;
RA Huang H.-R., Rowe C.E., Mohr S., Jiang Y., Lambowitz A.M., Perlman P.S.;
RT "The splicing of yeast mitochondrial group I and group II introns requires
RT a DEAD-box protein with RNA chaperone function.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:163-168(2005).
CC -!- FUNCTION: ATP-dependent RNA helicase required for mitochondrial
CC splicing of group I and II introns. Specifically involved in the ATP-
CC dependent splicing of the bl1 intron of COB. Also required for
CC efficient mitochondrial translation. {ECO:0000269|PubMed:12402239,
CC ECO:0000269|PubMed:15618406, ECO:0000269|PubMed:2535893,
CC ECO:0000269|PubMed:7567443}.
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
CC {ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:14576278}.
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 -!- MISCELLANEOUS: Present with 10300 molecules/cell in log phase SD
CC medium. {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the DEAD box helicase family. DDX18/HAS1
CC subfamily. {ECO:0000305}.
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DR EMBL; Z48784; CAA88707.1; -; Genomic_DNA.
DR EMBL; BK006938; DAA12036.1; -; Genomic_DNA.
DR PIR; S02116; S02116.
DR RefSeq; NP_010480.1; NM_001180502.1.
DR PDB; 3I5X; X-ray; 1.90 A; A=37-597.
DR PDB; 3I5Y; X-ray; 2.49 A; A=37-597.
DR PDB; 3I61; X-ray; 2.10 A; A=37-597.
DR PDB; 3I62; X-ray; 1.95 A; A=37-597.
DR PDB; 3SQW; X-ray; 1.91 A; A=88-664.
DR PDB; 3SQX; X-ray; 2.11 A; A=88-597.
DR PDB; 4DB2; X-ray; 3.16 A; A/B/C/D=342-596.
DR PDB; 4DB4; X-ray; 3.60 A; A/B=342-596.
DR PDB; 4TYN; X-ray; 2.96 A; A=88-596.
DR PDB; 4TYW; X-ray; 2.20 A; A=88-595.
DR PDB; 4TYY; X-ray; 2.74 A; A=88-596.
DR PDB; 4TZ0; X-ray; 2.35 A; A=88-596.
DR PDB; 4TZ6; X-ray; 3.21 A; A=88-596.
DR PDBsum; 3I5X; -.
DR PDBsum; 3I5Y; -.
DR PDBsum; 3I61; -.
DR PDBsum; 3I62; -.
DR PDBsum; 3SQW; -.
DR PDBsum; 3SQX; -.
DR PDBsum; 4DB2; -.
DR PDBsum; 4DB4; -.
DR PDBsum; 4TYN; -.
DR PDBsum; 4TYW; -.
DR PDBsum; 4TYY; -.
DR PDBsum; 4TZ0; -.
DR PDBsum; 4TZ6; -.
DR AlphaFoldDB; P15424; -.
DR SMR; P15424; -.
DR BioGRID; 32246; 132.
DR DIP; DIP-5368N; -.
DR IntAct; P15424; 35.
DR MINT; P15424; -.
DR STRING; 4932.YDR194C; -.
DR MaxQB; P15424; -.
DR PaxDb; P15424; -.
DR PRIDE; P15424; -.
DR EnsemblFungi; YDR194C_mRNA; YDR194C; YDR194C.
DR GeneID; 851775; -.
DR KEGG; sce:YDR194C; -.
DR SGD; S000002602; MSS116.
DR VEuPathDB; FungiDB:YDR194C; -.
DR eggNOG; KOG0342; Eukaryota.
DR HOGENOM; CLU_003041_26_6_1; -.
DR InParanoid; P15424; -.
DR OMA; IGFKEDL; -.
DR BioCyc; YEAST:G3O-29781-MON; -.
DR EvolutionaryTrace; P15424; -.
DR PRO; PR:P15424; -.
DR Proteomes; UP000002311; Chromosome IV.
DR RNAct; P15424; protein.
DR GO; GO:0005759; C:mitochondrial matrix; IMP:SGD.
DR GO; GO:0005739; C:mitochondrion; HDA:SGD.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR GO; GO:0003729; F:mRNA binding; HDA:SGD.
DR GO; GO:0003723; F:RNA binding; IDA:SGD.
DR GO; GO:0003724; F:RNA helicase activity; IDA:SGD.
DR GO; GO:0033592; F:RNA strand annealing activity; IDA:SGD.
DR GO; GO:0000372; P:Group I intron splicing; IMP:SGD.
DR GO; GO:0000373; P:Group II intron splicing; IDA:SGD.
DR GO; GO:0000963; P:mitochondrial RNA processing; IMP:SGD.
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; IMP:SGD.
DR GO; GO:0006364; P:rRNA processing; IBA:GO_Central.
DR GO; GO:0006392; P:transcription elongation from mitochondrial promoter; IDA:SGD.
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 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Helicase; Hydrolase; Mitochondrion;
KW mRNA processing; mRNA splicing; Nucleotide-binding; Reference proteome;
KW RNA-binding; Transit peptide; Translation regulation.
FT TRANSIT 1..26
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 27..664
FT /note="ATP-dependent RNA helicase MSS116, mitochondrial"
FT /id="PRO_0000030812"
FT DOMAIN 139..326
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 355..512
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT REGION 42..79
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 602..664
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 106..134
FT /note="Q motif"
FT MOTIF 267..270
FT /note="DEAD box"
FT COMPBIAS 48..64
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 602..617
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 627..646
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 647..664
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 152..159
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT STRAND 89..93
FT /evidence="ECO:0007829|PDB:3I5X"
FT HELIX 104..109
FT /evidence="ECO:0007829|PDB:3I5X"
FT HELIX 115..122
FT /evidence="ECO:0007829|PDB:3I5X"
FT TURN 123..125
FT /evidence="ECO:0007829|PDB:4TYW"
FT HELIX 131..141
FT /evidence="ECO:0007829|PDB:3I5X"
FT STRAND 142..151
FT /evidence="ECO:0007829|PDB:3I5X"
FT HELIX 158..172
FT /evidence="ECO:0007829|PDB:3I5X"
FT TURN 173..175
FT /evidence="ECO:0007829|PDB:3I5X"
FT STRAND 183..186
FT /evidence="ECO:0007829|PDB:3I5X"
FT HELIX 190..206
FT /evidence="ECO:0007829|PDB:3I5X"
FT HELIX 208..210
FT /evidence="ECO:0007829|PDB:3I5X"
FT STRAND 215..218
FT /evidence="ECO:0007829|PDB:3I5X"
FT HELIX 224..234
FT /evidence="ECO:0007829|PDB:3I5X"
FT STRAND 237..241
FT /evidence="ECO:0007829|PDB:3I5X"
FT HELIX 243..257
FT /evidence="ECO:0007829|PDB:3I5X"
FT STRAND 258..260
FT /evidence="ECO:0007829|PDB:4TYY"
FT STRAND 263..267
FT /evidence="ECO:0007829|PDB:3I5X"
FT HELIX 269..272
FT /evidence="ECO:0007829|PDB:3I5X"
FT TURN 275..277
FT /evidence="ECO:0007829|PDB:3I5X"
FT HELIX 278..291
FT /evidence="ECO:0007829|PDB:3I5X"
FT STRAND 300..307
FT /evidence="ECO:0007829|PDB:3I5X"
FT HELIX 311..315
FT /evidence="ECO:0007829|PDB:3I5X"
FT TURN 316..319
FT /evidence="ECO:0007829|PDB:3I5X"
FT STRAND 322..331
FT /evidence="ECO:0007829|PDB:3I5X"
FT STRAND 333..335
FT /evidence="ECO:0007829|PDB:3I5X"
FT STRAND 342..351
FT /evidence="ECO:0007829|PDB:3I5X"
FT HELIX 354..369
FT /evidence="ECO:0007829|PDB:3I5X"
FT TURN 370..372
FT /evidence="ECO:0007829|PDB:3I5X"
FT STRAND 375..379
FT /evidence="ECO:0007829|PDB:3I5X"
FT HELIX 383..397
FT /evidence="ECO:0007829|PDB:3I5X"
FT TURN 398..400
FT /evidence="ECO:0007829|PDB:3I5X"
FT STRAND 403..407
FT /evidence="ECO:0007829|PDB:3I5X"
FT HELIX 412..424
FT /evidence="ECO:0007829|PDB:3I5X"
FT STRAND 426..432
FT /evidence="ECO:0007829|PDB:3I5X"
FT HELIX 434..436
FT /evidence="ECO:0007829|PDB:3I5X"
FT STRAND 437..439
FT /evidence="ECO:0007829|PDB:4TZ0"
FT STRAND 447..452
FT /evidence="ECO:0007829|PDB:3I5X"
FT STRAND 455..457
FT /evidence="ECO:0007829|PDB:4TYY"
FT HELIX 459..464
FT /evidence="ECO:0007829|PDB:3I5X"
FT HELIX 469..471
FT /evidence="ECO:0007829|PDB:4TYN"
FT STRAND 474..481
FT /evidence="ECO:0007829|PDB:3I5X"
FT HELIX 482..484
FT /evidence="ECO:0007829|PDB:3I5X"
FT HELIX 485..495
FT /evidence="ECO:0007829|PDB:3I5X"
FT STRAND 501..505
FT /evidence="ECO:0007829|PDB:3I5X"
FT HELIX 509..518
FT /evidence="ECO:0007829|PDB:3I5X"
FT HELIX 523..539
FT /evidence="ECO:0007829|PDB:3I5X"
FT HELIX 541..544
FT /evidence="ECO:0007829|PDB:3I5X"
FT HELIX 548..556
FT /evidence="ECO:0007829|PDB:3I5X"
FT HELIX 558..562
FT /evidence="ECO:0007829|PDB:3I5X"
FT STRAND 570..572
FT /evidence="ECO:0007829|PDB:3I5X"
FT HELIX 574..580
FT /evidence="ECO:0007829|PDB:3I5X"
FT STRAND 583..585
FT /evidence="ECO:0007829|PDB:4TYW"
FT HELIX 586..591
FT /evidence="ECO:0007829|PDB:3I5X"
FT STRAND 592..594
FT /evidence="ECO:0007829|PDB:3I5X"
SQ SEQUENCE 664 AA; 76269 MW; DAEECCA4ED0CB2BE CRC64;
MLTSILIKGR TPVLASRNLL AALSNCNHIT WAVSRRLYND GNRDQRNFGR NQRNNNSNRY
RNSRFNSRPR TRSREDDDEV HFDKTTFSKL IHVPKEDNSK EVTLDSLLEE GVLDKEIHKA
ITRMEFPGLT PVQQKTIKPI LSSEDHDVIA RAKTGTGKTF AFLIPIFQHL INTKFDSQYM
VKAVIVAPTR DLALQIEAEV KKIHDMNYGL KKYACVSLVG GTDFRAAMNK MNKLRPNIVI
ATPGRLIDVL EKYSNKFFRF VDYKVLDEAD RLLEIGFRDD LETISGILNE KNSKSADNIK
TLLFSATLDD KVQKLANNIM NKKECLFLDT VDKNEPEAHE RIDQSVVISE KFANSIFAAV
EHIKKQIKER DSNYKAIIFA PTVKFTSFLC SILKNEFKKD LPILEFHGKI TQNKRTSLVK
RFKKDESGIL VCTDVGARGM DFPNVHEVLQ IGVPSELANY IHRIGRTARS GKEGSSVLFI
CKDELPFVRE LEDAKNIVIA KQEKYEPSEE IKSEVLEAVT EEPEDISDIV ISLISSYRSC
IKEYRFSERR ILPEIASTYG VLLNDPQLKI PVSRRFLDKL GLSRSPIGKA MFEIRDYSSR
DGNNKSYDYD DDSEISFRGN KNYNNRSQNR DYDDEPFRRS NNNRRSFSRS NDKNNYSSRN
SNIY
