| Tag | Content |
|---|
| CPLM ID | CPLM-006795 |
UniProt Accession | |
Genbank Protein ID | |
Genbank Nucleotide ID | |
Protein Name | Ribosomal large subunit pseudouridine synthase B |
Protein Synonyms/Alias | 23S rRNA pseudouridine(2605) synthase; rRNA pseudouridylate synthase B; rRNA-uridine isomerase B |
Gene Name | rluB |
Gene Synonyms/Alias | yciL; b1269; JW1261 |
Created Date | July 27, 2013 |
Organism | Escherichia coli (strain K12) |
NCBI Taxa ID | 83333 |
Lysine Modification | Position | Peptide | Type | References |
|---|
| 49 | VEVTPGLKIRIDGHL | acetylation | [1] | | 74 | CRVLAYYKPEGELCT | acetylation | [1] | | 152 | FGQVDDAKLRDLSRG | acetylation | [1] | | 170 | EDGPAAFKTIKFSGG | acetylation | [1] | | 258 | SSKVAVEKDRRRMKA | 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 | Responsible for synthesis of pseudouridine from uracil- 2605 in 23S ribosomal RNA. |
Sequence Annotation | DOMAIN 3 75 S4 RNA-binding.
ACT_SITE 110 110 Nucleophile (Probable). |
Keyword | Complete proteome; Isomerase; Reference proteome; RNA-binding; rRNA processing. |
Sequence Source | UniProt (SWISSPROT/TrEMBL); GenBank; EMBL |
Protein Length | 291 AA |
Protein Sequence | MSEKLQKVLA RAGHGSRREI ESIIEAGRVS VDGKIAKLGD RVEVTPGLKI RIDGHLISVR 60
ESAEQICRVL AYYKPEGELC TRNDPEGRPT VFDRLPKLRG ARWIAVGRLD VNTCGLLLFT 120
TDGELANRLM HPSREVEREY AVRVFGQVDD AKLRDLSRGV QLEDGPAAFK TIKFSGGEGI 180
NQWYNVTLTE GRNREVRRLW EAVGVQVSRL IRVRYGDIPL PKGLPRGGWT ELDLAQTNYL 240
RELVELPPET SSKVAVEKDR RRMKANQIRR AVKRHSQVSG GRRSGGRNNN G 291 |
Gene Ontology | GO:0009982; F:pseudouridine synthase activity; IMP:EcoCyc. GO:0003723; F:RNA binding; IEA:UniProtKB-KW. GO:0000455; P:enzyme-directed rRNA pseudouridine synthesis; IMP:EcoCyc. |
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Pfam | |
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PRINTS | |