CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-031747
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Ribosome biogenesis protein BMS1, putative 
Protein Synonyms/Alias
 Ribosome biogenesis protein bms1, putative 
Gene Name
 TGME49_113830, TGVEG_098870 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Toxoplasma gondii 
NCBI Taxa ID
 5811 
Lysine Modification
Position
Peptide
Type
References
676SSRRERGKADVFSGSacetylation[1, 2]
Reference
 [1] Lysine acetylation is widespread on proteins of diverse function and localization in the protozoan parasite Toxoplasma gondii.
 Jeffers V, Sullivan WJ Jr.
 Eukaryot Cell. 2012 Jun;11(6):735-42. [PMID: 22544907]
 [2] Protein intrinsic disorder in the acetylome of intracellular and extracellular Toxoplasma gondii.
 Xue B, Jeffers V, Sullivan WJ, Uversky VN.
 Mol Biosyst. 2013 Apr 5;9(4):645-57. [PMID: 23403842] 
Functional Description
  
Sequence Annotation
  
Keyword
 ATP-binding; Complete proteome; GTP-binding; Nucleotide-binding; Reference proteome. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 1267 AA 
Protein Sequence
METPGGDQLH KRHQQRHGKS EKKKKNRMKG KDGKAAEKQH NPRAFTFSGG VVSVQRKVQR 60
SLDKFALKER EEKTDKTPDV PPPYVVVVQG PPGVGKTTLI RSLVKHYTRH SLQVVQGPVT 120
LVASKQRRLT FVECSGTDMQ QMLDLAKVAD LVLLLIDADF GFEMETFEFI NILQVHGFPR 180
VIGVLTHLDK VEDRHNQKAL RRCKKQLKSR FWTEIYEGAK LFYLTGLQYG RYKKREILNL 240
SRYIAVQKYA PLSWRSAHPY LLALRCEPSC DPTVSTEKEE KETREPSGSV RASHSSCVFY 300
GYVRGSVMRQ GQWIHIPGAG DFQISSLACS PDPCPPPQGA LPASEAASDD DAENEGQTPR 360
LENGDLKKRR RTRSLKDQQK AIYAPGCDVG NVRIDADAMY IHLPDTKVSF TRPELLIKER 420
AEKTRCRARS QQSTAEDSED EDESEADSDE DESASEDEEG VDLGAGKRPV VAKEKEDVGE 480
AIRMVRELQE AETYIDKQLQ TQELRLLPHS TQVLSVAERS RARQLAPVAE AEEEEDDDEG 540
EEVEEEEEQV EGGGRQRRRA PTTRRTASLD ASAGQAEFES DSEETDSDTE REEDEGDEED 600
EEDEGVTDEE DVEDGVAAVH EAARKRFARA PSLKEIIYFG RIGDAGEESE ETERSSSTSD 660
PAGGASGESS RRERGKADVF SGSEKARTIP LFDGEDEEEE EPDKEENRLR GGLLGNLPAV 720
LPAVLRRQGL NGGDKRVTMD EDSAFVPSSV LYAAVGGDPE GEEEEFWSAD RLEEVKAQFF 780
ITGGWSSAEE EEKKKEAEEK PPQTEEQIEE AKRRHQAEQK RLQDEARRLQ IRDQAVDGSM 840
FSSSSSEPQS GACASIGTFV RVCVERLPRN WLDSLSPNRP VLLGGLCAGE QAKTFIQVRI 900
KKHRWFPRVL KSDDVLLFSA GWRRFQSLPM YALEDRSNAR VRYLKYTPEH LHCLSYFWAP 960
GLPPATPILA IRDTRATANF RISATGLVLQ TSPSVELSKK LKLLGEPKKI FKNTAFIKNM 1020
FNSDLEVNMC MGAKIQTVSG IRGQVKKALG TDGTFRATFE DKILMSDLVV CKTWIKMQPR 1080
QFCNPVLDVE GWQRLRTQAE IRQALQLPTP TKPGSHPDGG LAALQAARRS KEFNPIRVPK 1140
QLMLKLPFHA RTKLQHSTSK LRKLKGKALE EELDLRKPLV SAYDRRVAAL LQRLQTIKNA 1200
RVERRKEQQK EKRLKVAKAA AKKEEERARK QTEMRKRRYV KQGKIELGMR KKMRLGSSGK 1260
GDRNEDD 1267 
Gene Ontology
 GO:0005634; C:nucleus; IEA:InterPro.
 GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
 GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
 GO:0003924; F:GTPase activity; IEA:InterPro.
 GO:0006184; P:GTP catabolic process; IEA:GOC.
 GO:0042254; P:ribosome biogenesis; IEA:InterPro. 
Interpro
 IPR003593; AAA+_ATPase.
 IPR012948; AARP2CN.
 IPR007034; BMS1_TSR1_C.
 IPR000795; EF_GTP-bd_dom.
 IPR027417; P-loop_NTPase. 
Pfam
 PF08142; AARP2CN
 PF04950; DUF663
 PF00009; GTP_EFTU 
SMART
 SM00382; AAA
 SM00785; AARP2CN 
PROSITE
  
PRINTS