ID   YL419_YEAST             Reviewed;        1435 AA.
AC   Q06698; D6VZ55;
DT   25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   27-MAR-2024, entry version 173.
DE   RecName: Full=Putative ATP-dependent RNA helicase YLR419W;
DE            EC=3.6.4.13;
GN   OrderedLocusNames=YLR419W;
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 [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=9169871;
RA   Johnston M., Hillier L.W., Riles L., Albermann K., Andre B., Ansorge W.,
RA   Benes V., Brueckner M., Delius H., Dubois E., Duesterhoeft A.,
RA   Entian K.-D., Floeth M., Goffeau A., Hebling U., Heumann K.,
RA   Heuss-Neitzel D., Hilbert H., Hilger F., Kleine K., Koetter P., Louis E.J.,
RA   Messenguy F., Mewes H.-W., Miosga T., Moestl D., Mueller-Auer S.,
RA   Nentwich U., Obermaier B., Piravandi E., Pohl T.M., Portetelle D.,
RA   Purnelle B., Rechmann S., Rieger M., Rinke M., Rose M., Scharfe M.,
RA   Scherens B., Scholler P., Schwager C., Schwarz S., Underwood A.P.,
RA   Urrestarazu L.A., Vandenbol M., Verhasselt P., Vierendeels F., Voet M.,
RA   Volckaert G., Voss H., Wambutt R., Wedler E., Wedler H., Zimmermann F.K.,
RA   Zollner A., Hani J., Hoheisel J.D.;
RT   "The nucleotide sequence of Saccharomyces cerevisiae chromosome XII.";
RL   Nature 387:87-90(1997).
RN   [2]
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   [3]
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   [4]
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   [5]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
RA   Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT   "A multidimensional chromatography technology for in-depth phosphoproteome
RT   analysis.";
RL   Mol. Cell. Proteomics 7:1389-1396(2008).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-9 AND SER-816, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=19779198; DOI=10.1126/science.1172867;
RA   Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
RT   "Global analysis of Cdk1 substrate phosphorylation sites provides insights
RT   into evolution.";
RL   Science 325:1682-1686(2009).
CC   -!- FUNCTION: Probable ATP-binding RNA helicase. {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: Cytoplasm {ECO:0000269|PubMed:14562095}.
CC   -!- MISCELLANEOUS: Present with 195 molecules/cell in log phase SD medium.
CC       {ECO:0000269|PubMed:14562106}.
CC   -!- SIMILARITY: Belongs to the DEAD box helicase family. DEAH subfamily.
CC       {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; U20162; AAB67492.1; -; Genomic_DNA.
DR   EMBL; BK006945; DAA09721.1; -; Genomic_DNA.
DR   PIR; S59384; S59384.
DR   RefSeq; NP_013523.3; NM_001182307.3.
DR   AlphaFoldDB; Q06698; -.
DR   SMR; Q06698; -.
DR   BioGRID; 31677; 107.
DR   IntAct; Q06698; 4.
DR   MINT; Q06698; -.
DR   STRING; 4932.YLR419W; -.
DR   iPTMnet; Q06698; -.
DR   MaxQB; Q06698; -.
DR   PaxDb; 4932-YLR419W; -.
DR   PeptideAtlas; Q06698; -.
DR   EnsemblFungi; YLR419W_mRNA; YLR419W; YLR419W.
DR   GeneID; 851137; -.
DR   KEGG; sce:YLR419W; -.
DR   AGR; SGD:S000004411; -.
DR   SGD; S000004411; YLR419W.
DR   VEuPathDB; FungiDB:YLR419W; -.
DR   eggNOG; KOG0920; Eukaryota.
DR   GeneTree; ENSGT00940000158279; -.
DR   HOGENOM; CLU_001832_4_0_1; -.
DR   InParanoid; Q06698; -.
DR   OMA; LFRVCNM; -.
DR   OrthoDB; 53793at2759; -.
DR   BioCyc; YEAST:G3O-32480-MONOMER; -.
DR   BioGRID-ORCS; 851137; 0 hits in 10 CRISPR screens.
DR   PRO; PR:Q06698; -.
DR   Proteomes; UP000002311; Chromosome XII.
DR   RNAct; Q06698; Protein.
DR   GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR   GO; GO:0005739; C:mitochondrion; HDA:SGD.
DR   GO; GO:0005634; C:nucleus; IEA:UniProt.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR   GO; GO:0004386; F:helicase activity; IBA:GO_Central.
DR   GO; GO:0003729; F:mRNA binding; HDA:SGD.
DR   GO; GO:0003723; F:RNA binding; IBA:GO_Central.
DR   GO; GO:0003724; F:RNA helicase activity; IEA:UniProtKB-EC.
DR   GO; GO:0034641; P:cellular nitrogen compound metabolic process; IEA:UniProt.
DR   GO; GO:0043170; P:macromolecule metabolic process; IEA:UniProt.
DR   GO; GO:0044238; P:primary metabolic process; IEA:UniProt.
DR   GO; GO:0022613; P:ribonucleoprotein complex biogenesis; IEA:UniProt.
DR   CDD; cd17917; DEXHc_RHA-like; 1.
DR   CDD; cd18791; SF2_C_RHA; 1.
DR   CDD; cd14271; UBA_YLR419W_like; 1.
DR   Gene3D; 1.20.120.1080; -; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR   Gene3D; 3.10.110.10; Ubiquitin Conjugating Enzyme; 1.
DR   InterPro; IPR011709; DEAD-box_helicase_OB_fold.
DR   InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR   InterPro; IPR007502; Helicase-assoc_dom.
DR   InterPro; IPR014001; Helicase_ATP-bd.
DR   InterPro; IPR001650; Helicase_C.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR006575; RWD_dom.
DR   InterPro; IPR015940; UBA.
DR   InterPro; IPR009060; UBA-like_sf.
DR   InterPro; IPR016135; UBQ-conjugating_enzyme/RWD.
DR   InterPro; IPR035467; YLR419W-like_UBA.
DR   PANTHER; PTHR18934; ATP-DEPENDENT RNA HELICASE; 1.
DR   PANTHER; PTHR18934:SF145; ATP-DEPENDENT RNA HELICASE DHX29; 1.
DR   Pfam; PF00270; DEAD; 1.
DR   Pfam; PF00271; Helicase_C; 1.
DR   Pfam; PF07717; OB_NTP_bind; 1.
DR   Pfam; PF05773; RWD; 1.
DR   SMART; SM00487; DEXDc; 1.
DR   SMART; SM00847; HA2; 1.
DR   SMART; SM00490; HELICc; 1.
DR   SMART; SM00591; RWD; 1.
DR   SMART; SM00165; UBA; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   SUPFAM; SSF46934; UBA-like; 1.
DR   SUPFAM; SSF54495; UBC-like; 1.
DR   PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR   PROSITE; PS51194; HELICASE_CTER; 1.
DR   PROSITE; PS50908; RWD; 1.
DR   PROSITE; PS50030; UBA; 1.
PE   1: Evidence at protein level;
KW   ATP-binding; Cytoplasm; Helicase; Hydrolase; Nucleotide-binding;
KW   Phosphoprotein; Reference proteome.
FT   CHAIN           1..1435
FT                   /note="Putative ATP-dependent RNA helicase YLR419W"
FT                   /id="PRO_0000247257"
FT   DOMAIN          365..406
FT                   /note="UBA"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00212"
FT   DOMAIN          430..531
FT                   /note="RWD"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00179"
FT   DOMAIN          614..782
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT   DOMAIN          845..1020
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT   REGION          1..57
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          226..251
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          543..566
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           729..732
FT                   /note="DEAH box"
FT   COMPBIAS        1..19
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        23..47
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        547..566
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         627..634
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT   MOD_RES         9
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:19779198"
FT   MOD_RES         816
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:19779198"
SQ   SEQUENCE   1435 AA;  163045 MW;  0F91A40BB8C7772B CRC64;
     MAKKTKNNSK SSTPVNDVPT TAGKKKAKGK KGQEPEPEDD KRAKQQSNRA KVTSTASWTG
     KLPHTILHET CQKRKWNKVE YDMKKIGDKG FIAIAVLSFT DPKTKETLTA RMNDPTYDKA
     SGKGLVIPQE TPIEARHMAS TIALYRIAYN TNLHMMLPPN HRKTWYALDD FRKDNLKTDE
     KRINKLFDLD PFKTMVEDRK LKAQREKEQV AQNNQAQKEQ VARTILSSHG GISSSGKDRQ
     ERKVASHKNS HNPSLVRFPK KVWENSIFVD LDESSRQLIE TSLKEKIDWQ AKKISHKNET
     IAENREDLKA KLLTLQFRPK HVEEAMLYKD PLSFLLFNLP EDDLPPFFHK KKGDTKNKVE
     ITNLPLSTRM IVERLTEIGV SSDEALLALQ QNDMNENEAA GFLTREILPT LNSNTNEPVS
     ETESIECWNQ ELESLESIYE GCVMDAKEDS HYTLNLIEKL KIKLKVYRTK NYPASLPGIV
     VSTFDKNYKL PDYIKKQILT RLLHYLQEGN LIGDMLVYHI YEWLKENISK IIDNPGPLIP
     DSDSKGAINK RNISNGKRSI NNSSSRKFTK TTISEDTLSV LREEYTKRIK SSEYKSMQLV
     REQLPAWKKQ KVIIDIINKN EVVLITGETG SGKSTQVVQF ILDFLQKEKG DFGKTKIVCT
     QPRRISAIGL AERVSDERCV TCGEEVGYVI RGVNKTKAST RIKFMTTGVL VRLLQNARTM
     LENTIVVIDE VHERSIDTDL IVTLMKNLLH RVRGMKIVLM SATVNVDLFK KFFPGLATCH
     IEGRTFPITD YFLEDILSDL DFKIKREKAL SYDDDSVDER NNDDQYLKPR ADSKFFTSGQ
     INYDLLCQVV EYVHKRLKAA NDNGSIIVFL PGVGEINKCC NLLANKSNEA DFMVLPLHSA
     LTPEDQKRVF KKYHGKRKVV VSTNIAETSI TIDDCVATID TGRAKSMFYN PKDNTTKLIE
     SFISKAEVKQ RRGRAGRVRE GLSYKLFSKN LYENDMISMP IPEIKRIPLE SLYLSVKAMG
     IKDVKAFLST ALDAPPLPAL QKAERILTTI GLVDESDKSL TQLGQFISLM PVMDSKHGKL
     LIYGILFGCT DISVLLVSIL GIGVLPFIGG FENREKIKKL LCKYESRGDL FAVLEIVRDY
     FKIKDSSIKR KYLRDNLLSY NKINEIKSST AQYYSILKDV GFLPMDYKVG SISDLNRNER
     NFDILRAILT GAFYPHIARV QLPDVKYLST SSGAVEKDPE AKMIKYWIRS EEYQDKLEEY
     KTKISQETQK VDLEDLPLPA TRAFIHPSSV LFSTNSVNLE DAKLLSEVDG PISRQSKIPT
     VVKYPFVLFT TSQVTNKLYL RDLTPTTTLS LLLFGGAISY DIGGTIHSPG IVVDNWLPIR
     TWCKNGVLIK ELRTQLDEAI RKKLESPDYA KKSQIDNSGA DKTLKIVEKI IASEQ
//