CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-006244
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 ATP-dependent RNA helicase DRS1 
Protein Synonyms/Alias
 Deficiency of ribosomal subunits protein 1 
Gene Name
 DRS1 
Gene Synonyms/Alias
 YLL008W; L1345 
Created Date
 July 27, 2013 
Organism
 Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) 
NCBI Taxa ID
 559292 
Lysine Modification
Position
Peptide
Type
References
112KKDVDLDKIIRRKGGacetylation[1]
432SLVSLSLKKPVRIMIacetylation[1]
657RAEMQLRKGENMLKHacetylation[2]
687ESDKKNSKVLGALSRacetylation[1]
Reference
 [1] Proteome-wide analysis of lysine acetylation suggests its broad regulatory scope in Saccharomyces cerevisiae.
 Henriksen P, Wagner SA, Weinert BT, Sharma S, Bacinskaja G, Rehman M, Juffer AH, Walther TC, Lisby M, Choudhary C.
 Mol Cell Proteomics. 2012 Nov;11(11):1510-22. [PMID: 22865919]
 [2] Preparative peptide isoelectric focusing as a tool for improving the identification of lysine-acetylated peptides from complex mixtures.
 Xie H, Bandhakavi S, Roe MR, Griffin TJ.
 J Proteome Res. 2007 May;6(5):2019-26. [PMID: 17397211
Functional Description
 ATP-binding RNA helicase involved in ribosome assembly. 
Sequence Annotation
 DOMAIN 262 437 Helicase ATP-binding.
 DOMAIN 448 639 Helicase C-terminal.
 NP_BIND 275 282 ATP (By similarity).
 MOTIF 231 259 Q motif.
 MOTIF 385 388 DEAD box.
 MOD_RES 208 208 Phosphoserine.  
Keyword
 ATP-binding; Coiled coil; Complete proteome; Helicase; Hydrolase; Nucleotide-binding; Nucleus; Phosphoprotein; Reference proteome; Ribosome biogenesis; RNA-binding. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 752 AA 
Protein Sequence
MVVGTKKYSN LDFVPTISDS EDDVPILDSS DDEKVEAKKT TKKRKGKNNK KKVSEGDNLD 60
EDVHEDLDAG FKFDLDADDT TSNFQGWNFL AEGESNKDDA EAFVKKDVDL DKIIRRKGGL 120
VKMAHIDSKQ EEETEKEKVE KENDSDDEEL AMDGFGMGAP MNNGDENQSE EEEEEEEKEE 180
EEEEEEEQEE MTLEKGGKDD EIDEEDDSEE AKADFYAPET EGDEAKKQMY ENFNSLSLSR 240
PVLKGLASLG YVKPSPIQSA TIPIALLGKD IIAGAVTGSG KTAAFMIPII ERLLYKPAKI 300
ASTRVIVLLP TRELAIQVAD VGKQIARFVS GITFGLAVGG LNLRQQEQML KSRPDIVIAT 360
PGRFIDHIRN SASFNVDSVE ILVMDEADRM LEEGFQDELN EIMGLLPSNR QNLLFSATMN 420
SKIKSLVSLS LKKPVRIMID PPKKAATKLT QEFVRIRKRD HLKPALLFNL IRKLDPTGQK 480
RIVVFVARKE TAHRLRIIMG LLGMSVGELH GSLTQEQRLD SVNKFKNLEV PVLICTDLAS 540
RGLDIPKIEV VINYDMPKSY EIYLHRVGRT ARAGREGRSV TFVGESSQDR SIVRAAIKSV 600
EENKSLTQGK ALGRNVDWVQ IEETNKLVES MNDTIEDILV EEKEEKEILR AEMQLRKGEN 660
MLKHKKEIQA RPRRTWFQSE SDKKNSKVLG ALSRNKKVTN SKKRKREEAK ADGNGARSYR 720
KTKTDRIADQ ERTFKKQKST NSNKKKGFKS RR 752 
Gene Ontology
 GO:0005730; C:nucleolus; IDA:SGD.
 GO:0030687; C:preribosome, large subunit precursor; IDA:SGD.
 GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
 GO:0004004; F:ATP-dependent RNA helicase activity; TAS:SGD.
 GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
 GO:0000027; P:ribosomal large subunit assembly; IMP:SGD.
 GO:0006364; P:rRNA processing; IMP:SGD. 
Interpro
 IPR011545; DNA/RNA_helicase_DEAD/DEAH_N.
 IPR014001; Helicase_ATP-bd.
 IPR001650; Helicase_C.
 IPR027417; P-loop_NTPase.
 IPR000629; RNA-helicase_DEAD-box_CS.
 IPR014014; RNA_helicase_DEAD_Q_motif. 
Pfam
 PF00270; DEAD
 PF00271; Helicase_C 
SMART
 SM00487; DEXDc
 SM00490; HELICc 
PROSITE
 PS00039; DEAD_ATP_HELICASE
 PS51192; HELICASE_ATP_BIND_1
 PS51194; HELICASE_CTER
 PS51195; Q_MOTIF 
PRINTS