| Tag |
Content |
LipidDB ID |
LipidDB-36329-01348 |
Entry Name |
|
UniProt Accession |
|
Theoretical PI |
8.5 |
Molecular Weight |
56320.86 |
Genbank Protein ID |
|
Genbank Nucleotide ID |
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Protein Name |
tRNA-splicing ligase RtcB homolog |
Protein Synonyms/Alias |
6.5.1.3; |
Gene Name |
|
Gene Synonyms/Alias |
PF11_0068; |
Created Date |
05-APR-2011 |
| Lipid Modification Sites |
|---|
| Position |
Sequence Form |
Peptide |
References |
Modification Type |
194 | Canonical | WIEDKLNCEDNGRSL | [1] | S-Palmitoylation |
|
Organism |
Plasmodium falciparum (isolate 3D7) |
NCBI Taxa ID |
36329 |
Reference |
[1] Predicted from GPS-Lipid
|
Functional Description |
Catalytic subunit of the tRNA-splicing ligase complex that acts by directly joining spliced tRNA halves to mature-sized tRNAs by incorporating the precursor-derived splice junction phosphate into the mature tRNA as a canonical 3',5'- phosphodiester. May act as an RNA ligase with broad substrate specificity, and may function toward other RNAs (By similarity). |
Sequence Annotation |
Nucleotide-binding: 354 355 GMP.
Nucleotide-binding: 401 404 GMP.
Nucleotide-binding: 429 432 GMP.
Active site: 429 429 GMP-histidine intermediate.
Metal binding site: 120 120 Manganese 1.
Metal binding site: 123 123 Manganese 1.
Metal binding site: 123 123 Manganese 2.
Metal binding site: 228 228 Manganese 1.
Metal binding site: 260 260 Manganese 2.
Metal binding site: 354 354 Manganese 2.
Binding site: 231 231 GMP.
Binding site: 410 410 GMP.
Binding site: 505 505 GMP.
|
Protein Length |
506 AA. |
Protein Sequence
(Canonical) |
MKGIPKRPIS NYIEKTNETN LYKIRKGLVN EMNVEGHIYV NEKLKTLLDE EIATYELNKN 60
STFLPAVMQI ANVSTLPGIV KASIALPDVH AGYGFSIGNV AAFDMDNEKA IVSPGGVGFD 120
INCGVRLIRT NLFYEDIKPK QEELTQLLFN HIPVGVGSQG FILCNQENLD DALCLGMDWC 180
VKEGYSWIED KLNCEDNGRS LYADSNFVSI RAKKRGITQM GTLGAGNHYA EIQIVDQIYD 240
KKSAKLMGIE KKNQVCIMIH SGSRGLGHQI ATDALIDMEK SMNKYKINVI DKQLACTPIH 300
SKEGQNYLKA MGSACNFAWI NRSSMTFLAR QAFSKIFNQS PDDLDMHVIY DVSHNIAKIE 360
EHYIDGKIKK LLVHRKGSTR AFPPFHPLVP LDYQYCGQPI LIGGTMGTYS YVLTGNEKAM 420
QATFGSTCHG AGRALSRNKS RNTLSYLDVL NKLKEQNISI RVASPKLIME EAPESYKNVC 480
DVVQTCHDAG ISNKCFRLKP VAVIKG 506
|
FASTA
(Canonical) |
>LipidDB-36329-01348|Q8IIU6
MKGIPKRPISNYIEKTNETNLYKIRKGLVNEMNVEGHIYVNEKLKTLLDEEIATYELNKN
STFLPAVMQIANVSTLPGIVKASIALPDVHAGYGFSIGNVAAFDMDNEKAIVSPGGVGFD
INCGVRLIRTNLFYEDIKPKQEELTQLLFNHIPVGVGSQGFILCNQENLDDALCLGMDWC
VKEGYSWIEDKLNCEDNGRSLYADSNFVSIRAKKRGITQMGTLGAGNHYAEIQIVDQIYD
KKSAKLMGIEKKNQVCIMIHSGSRGLGHQIATDALIDMEKSMNKYKINVIDKQLACTPIH
SKEGQNYLKAMGSACNFAWINRSSMTFLARQAFSKIFNQSPDDLDMHVIYDVSHNIAKIE
EHYIDGKIKKLLVHRKGSTRAFPPFHPLVPLDYQYCGQPILIGGTMGTYSYVLTGNEKAM
QATFGSTCHGAGRALSRNKSRNTLSYLDVLNKLKEQNISIRVASPKLIMEEAPESYKNVC
DVVQTCHDAGISNKCFRLKPVAVIKG
|
Gene Ontology |
GO:0072669; C:tRNA-splicing ligase complex; IEA:UniProtKB-HAMAP GO:0005524; F:ATP binding; IEA:UniProtKB-KW GO:0046872; F:metal ion binding; IEA:UniProtKB-KW GO:0003972; F:RNA ligase (ATP) activity; IEA:UniProtKB-HAMAP GO:0006388; P:tRNA splicing, via endonucleolytic cleavage and ligation; IEA:UniProtKB-HAMAP |
Interpro |
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Pfam |
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SMART |
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PROSITE |
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PRINTS |
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