| Tag | Content |
|---|
| CPLM ID | CPLM-003006 |
UniProt Accession | |
Genbank Protein ID | |
Genbank Nucleotide ID | |
Protein Name | Peptide chain release factor 3 |
Protein Synonyms/Alias | RF-3 |
Gene Name | prfC |
Gene Synonyms/Alias | miaD; tos; b4375; JW5873 |
Created Date | July 27, 2013 |
Organism | Escherichia coli (strain K12) |
NCBI Taxa ID | 83333 |
Lysine Modification | Position | Peptide | Type | References |
|---|
| 56 | RGSNQHAKSDWMEME | acetylation | [1] | | 64 | SDWMEMEKQRGISIT | acetylation | [1] | | 177 | TWPIGCGKLFKGVYH | acetylation | [1] | | 180 | IGCGKLFKGVYHLYK | acetylation | [1] | | 187 | KGVYHLYKDETYLYQ | acetylation | [1] | | 197 | TYLYQSGKGHTIQEV | acetylation | [1] | | 295 | TVEASEDKFTGFVFK | acetylation | [1] | | 310 | IQANMDPKHRDRVAF | acetylation | [1] | | 338 | LRQVRTAKDVVISDA | acetylation | [1] | | 408 | IRLKDPLKQKQLLKG | acetylation | [1] | | 410 | LKDPLKQKQLLKGLV | acetylation | [1] | | 480 | WVECADAKKFEEFKR | acetylation | [1] | | 488 | KFEEFKRKNESQLAL | acetylation | [1] |
|
Reference | [1] Acetyl-Phosphate Is a Critical Determinant of Lysine Acetylation in E. coli. Weinert BT, Iesmantavicius V, Wagner SA, Schölz C, Gummesson B, Beli P, Nyström T, Choudhary C. Mol Cell. 2013 Jul 25;51(2):265-72. [ PMID: 23830618] |
Functional Description | Increases the formation of ribosomal termination complexes and stimulates activities of RF-1 and RF-2. It binds guanine nucleotides and has strong preference for UGA stop codons. It may interact directly with the ribosome. The stimulation of RF- 1 and RF-2 is significantly reduced by GTP and GDP, but not by GMP. |
Sequence Annotation | NP_BIND 20 27 GTP (By similarity).
NP_BIND 88 92 GTP (By similarity).
NP_BIND 142 145 GTP (By similarity). |
Keyword | 3D-structure; Complete proteome; Cytoplasm; Direct protein sequencing; GTP-binding; Nucleotide-binding; Protein biosynthesis; Reference proteome. |
Sequence Source | UniProt (SWISSPROT/TrEMBL); GenBank; EMBL |
Protein Length | 529 AA |
Protein Sequence | MTLSPYLQEV AKRRTFAIIS HPDAGKTTIT EKVLLFGQAI QTAGTVKGRG SNQHAKSDWM 60
EMEKQRGISI TTSVMQFPYH DCLVNLLDTP GHEDFSEDTY RTLTAVDCCL MVIDAAKGVE 120
DRTRKLMEVT RLRDTPILTF MNKLDRDIRD PMELLDEVEN ELKIGCAPIT WPIGCGKLFK 180
GVYHLYKDET YLYQSGKGHT IQEVRIVKGL NNPDLDAAVG EDLAQQLRDE LELVKGASNE 240
FDKELFLAGE ITPVFFGTAL GNFGVDHMLD GLVEWAPAPM PRQTDTRTVE ASEDKFTGFV 300
FKIQANMDPK HRDRVAFMRV VSGKYEKGMK LRQVRTAKDV VISDALTFMA GDRSHVEEAY 360
PGDILGLHNH GTIQIGDTFT QGEMMKFTGI PNFAPELFRR IRLKDPLKQK QLLKGLVQLS 420
EEGAVQVFRP ISNNDLIVGA VGVLQFDVVV ARLKSEYNVE AVYESVNVAT ARWVECADAK 480
KFEEFKRKNE SQLALDGGDN LAYIATSMVN LRLAQERYPD VQFHQTREH 529 |
Gene Ontology | GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. GO:0019003; F:GDP binding; IDA:EcoCyc. GO:0005525; F:GTP binding; IEA:HAMAP. GO:0003924; F:GTPase activity; IDA:EcoCyc. GO:0016150; F:translation release factor activity, codon nonspecific; IDA:EcoCyc. GO:0016149; F:translation release factor activity, codon specific; IEA:HAMAP. GO:0006449; P:regulation of translational termination; IEA:HAMAP. |
Interpro | |
Pfam | |
SMART | |
PROSITE | |
PRINTS | |