YL419_YEAST
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 03-AUG-2022, entry version 166.
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}.
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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; 80.
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 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; YEADPFL; -.
DR BioCyc; YEAST:G3O-32480-MON; -.
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:1990904; C:ribonucleoprotein complex; 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: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:0034660; P:ncRNA metabolic process; IEA:UniProt.
DR GO; GO:0022613; P:ribonucleoprotein complex biogenesis; IEA:UniProt.
DR CDD; cd14271; UBA_YLR419W_like; 1.
DR Gene3D; 3.10.110.10; -; 1.
DR Gene3D; 3.40.50.300; -; 2.
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-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; 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
