CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-015049
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Translation initiation factor IF-2 
Protein Synonyms/Alias
  
Gene Name
 infB 
Gene Synonyms/Alias
 RPA0436 
Created Date
 July 27, 2013 
Organism
 Rhodopseudomonas palustris (strain ATCC BAA-98 / CGA009) 
NCBI Taxa ID
 258594 
Lysine Modification
Position
Peptide
Type
References
67PAAPEVAKKPAPAPAacetylation[1]
328DVIRLLMKQGAMHKIacetylation[1]
Reference
 [1] System-wide studies of N-lysine acetylation in Rhodopseudomonas palustris reveal substrate specificity of protein acetyltransferases.
 Crosby HA, Pelletier DA, Hurst GB, Escalante-Semerena JC.
 J Biol Chem. 2012 May 4;287(19):15590-601. [PMID: 22416131
Functional Description
 One of the essential components for the initiation of protein synthesis. Protects formylmethionyl-tRNA from spontaneous hydrolysis and promotes its binding to the 30S ribosomal subunits. Also involved in the hydrolysis of GTP during the formation of the 70S ribosomal complex (By similarity). 
Sequence Annotation
 NP_BIND 388 395 GTP (By similarity).
 NP_BIND 436 440 GTP (By similarity).
 NP_BIND 490 493 GTP (By similarity).
 REGION 382 532 G-domain.  
Keyword
 Complete proteome; Cytoplasm; GTP-binding; Initiation factor; Nucleotide-binding; Protein biosynthesis. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 883 AA 
Protein Sequence
MVDTKTPGDK TLTMPTKTLT LKPRVEQGVV RQSFSHGRSK QVVVEKRGKR RLGGDEPAAP 60
AAPEVAKKPA PAPAAPPRQQ QSRPAPQQSR SGMVLRTLTE DERTARATAL ADARVREIEE 120
RKQAEIEAQR RAEQEKIEKA EREAAEARRK AEEERHRQED EAKRKAETEA KKRFGDAEPA 180
KKPAETSTTT TTAAPARPAT TTTRTPTPAG RPPAVAAEAG DDDEAPRMIR RPGGPARPAP 240
PPKQPAAKPG ASKQRGRLTV VTALNADDVR ERSIASFRRR TQRLKGHASN EPKEKLVREV 300
VIPEVIAIQE LANRMSERAV DVIRLLMKQG AMHKITDVID ADTAQLIAEE LGHTVKRVAA 360
SDVEEGLFDV VDDSTDTEPR SPVVTVMGHV DHGKTSLLDA LRHANVVSGE AGGITQHIGA 420
YQVTSPESGK KITFIDTPGH AAFTAMRARG AKVTDIVVLV VAADDGVMPQ TIEAINHAKA 480
AGVPIIVAIN KIDKPDAKPD RVRTDLLQHN VQVESMGGDV VDVEVSAKNK INLDKLLEMI 540
ALQAEILELK TNTQRPAEGT VIEAKLDRGR GPVATVLVQR GTLRVGDIIV AGAEMGRVRA 600
LISDQGETVQ EAGPSVPVEV LGFNGPPEAG DRLAVVENEA RARQITDYRA HQKREKSAAS 660
VSGMRGSLEQ MMTQLKTSGR KEFPLIVKAD VQGSLEAILG SLEKLGTDEV AARILHAGVG 720
GISESDVTLA EGFNAVILGF SVRANKEAAA AAKRNGIEIR YYNIIYDLVD DIKKAMSGLL 780
APTLRETMLG NAQILEIFNI SKVGKVAGCR VTDGTVERGA NVRLIRDNVV VHEGKLSTLK 840
RFKDEVKEVV AGQECGMAFE NYTDMRAGDI IECYRVETIQ RSL 883 
Gene Ontology
 GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
 GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
 GO:0003924; F:GTPase activity; IEA:HAMAP.
 GO:0003743; F:translation initiation factor activity; IEA:HAMAP.
 GO:0006184; P:GTP catabolic process; IEA:GOC. 
Interpro
 IPR000795; EF_GTP-bd_dom.
 IPR013575; IF2_assoc_dom_bac.
 IPR006847; IF2_N.
 IPR027417; P-loop_NTPase.
 IPR005225; Small_GTP-bd_dom.
 IPR000178; TF_IF2_bacterial-like.
 IPR015760; TIF_IF2.
 IPR023115; TIF_IF2_dom3.
 IPR004161; Transl_elong_EFTu/EF1A_2.
 IPR009000; Transl_elong_init/rib_B-barrel. 
Pfam
 PF00009; GTP_EFTU
 PF03144; GTP_EFTU_D2
 PF11987; IF-2
 PF08364; IF2_assoc
 PF04760; IF2_N 
SMART
  
PROSITE
 PS01176; IF2 
PRINTS