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Database: UniProt
Entry: Q06698
LinkDB: Q06698
Original site: Q06698 
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   16-OCT-2019, entry version 153.
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;
OC   Saccharomycetes; 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.,
RA   Ansorge W., Benes V., Brueckner M., Delius H., Dubois E.,
RA   Duesterhoeft A., Entian K.-D., Floeth M., Goffeau A., Hebling U.,
RA   Heumann K., Heuss-Neitzel D., Hilbert H., Hilger F., Kleine K.,
RA   Koetter P., Louis E.J., Messenguy F., Mewes H.-W., Miosga T.,
RA   Moestl D., Mueller-Auer S., Nentwich U., Obermaier B., Piravandi E.,
RA   Pohl T.M., Portetelle D., Purnelle B., Rechmann S., Rieger M.,
RA   Rinke M., Rose M., Scharfe M., Scherens B., Scholler P., Schwager C.,
RA   Schwarz S., Underwood A.P., Urrestarazu L.A., Vandenbol M.,
RA   Verhasselt P., Vierendeels F., Voet M., Volckaert G., Voss H.,
RA   Wambutt R., Wedler E., Wedler H., Zimmermann F.K., Zollner A.,
RA   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.,
RA   Cherry J.M.;
RT   "The reference genome sequence of Saccharomyces cerevisiae: Then and
RT   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.,
RA   Dephoure N., 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
RT   phosphoproteome 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
RT   insights 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
CC       medium. {ECO:0000269|PubMed:14562106}.
CC   -!- SIMILARITY: Belongs to the DEAD box helicase family. DEAH
CC       subfamily. {ECO:0000305}.
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   BioGrid; 31677; 54.
DR   IntAct; Q06698; 4.
DR   MINT; Q06698; -.
DR   STRING; 4932.YLR419W; -.
DR   iPTMnet; Q06698; -.
DR   MaxQB; Q06698; -.
DR   PaxDb; Q06698; -.
DR   PRIDE; Q06698; -.
DR   EnsemblFungi; YLR419W_mRNA; YLR419W; YLR419W.
DR   GeneID; 851137; -.
DR   KEGG; sce:YLR419W; -.
DR   EuPathDB; FungiDB:YLR419W; -.
DR   SGD; S000004411; YLR419W.
DR   HOGENOM; HOG000167651; -.
DR   InParanoid; Q06698; -.
DR   OMA; YFNQENG; -.
DR   BioCyc; YEAST:G3O-32480-MONOMER; -.
DR   Reactome; R-SCE-3134963; DEx/H-box helicases activate type I IFN and inflammatory cytokines production.
DR   PRO; PR:Q06698; -.
DR   Proteomes; UP000002311; Chromosome XII.
DR   GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR   GO; GO:0005739; C:mitochondrion; HDA:SGD.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
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   CDD; cd14271; UBA_YLR419W_like; 1.
DR   Gene3D; 3.10.110.10; -; 1.
DR   InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR   InterPro; IPR011709; DUF1605.
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-domain.
DR   InterPro; IPR015940; UBA.
DR   InterPro; IPR009060; UBA-like_sf.
DR   InterPro; IPR016135; UBQ-conjugating_enzyme/RWD.
DR   InterPro; IPR035467; YLR419W-like_UBA.
DR   Pfam; PF00270; DEAD; 1.
DR   Pfam; PF04408; HA2; 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; SSF46934; SSF46934; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   SUPFAM; SSF54495; SSF54495; 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; Complete proteome; Cytoplasm; Helicase; Hydrolase;
KW   Nucleotide-binding; Phosphoprotein; Reference proteome.
FT   CHAIN         1   1435       Putative ATP-dependent RNA helicase
FT                                YLR419W.
FT                                /FTId=PRO_0000247257.
FT   DOMAIN      365    406       UBA. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00212}.
FT   DOMAIN      430    531       RWD. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00179}.
FT   DOMAIN      614    782       Helicase ATP-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00541}.
FT   DOMAIN      845   1020       Helicase C-terminal.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00542}.
FT   NP_BIND     627    634       ATP. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00541}.
FT   MOTIF       729    732       DEAH box.
FT   MOD_RES       9      9       Phosphoserine.
FT                                {ECO:0000244|PubMed:19779198}.
FT   MOD_RES     816    816       Phosphoserine.
FT                                {ECO:0000244|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
//
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