Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Entry version 94 (02 Jun 2021)
Sequence version 1 (01 Mar 2003)
Previous versions | rss
Add a publicationFeedback
Protein

RNA-splicing ligase RtcB homolog

Gene

PF11_0068

Organism
Plasmodium falciparum (isolate 3D7)
Status
Reviewed-Annotation score:

Annotation score:3 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Protein inferred from homologyi <p>This indicates the type of evidence that supports the existence of the protein. Note that the 'protein existence' evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

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.

UniRule annotation

Miscellaneous

Ligation probably proceeds through 3 nucleotidyl transfer steps, with 2',3'-cyclic phosphate termini being hydrolyzed to 3'-P termini in a step that precedes 3'-P activation with GMP. In the first nucleotidyl transfer step, RTCB reacts with GTP to form a covalent RTCB-histidine-GMP intermediate with release of PPi; in the second step, the GMP moiety is transferred to the RNA 3'-P; in the third step, the 5'-OH from the opposite RNA strand attacks the activated 3'-P to form a 3',5'-phosphodiester bond and release GMP.UniRule annotation

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

  • (Ribonucleotide)(n)-3'-phosphate + 5'-hydroxy-(ribonucleotide)(m) + GTP = (ribonucleotide)(n+m) + GMP + diphosphate.UniRule annotation EC:6.5.1.8
  • (Ribonucleotide)(n)-2',3'-cyclophosphate + 5'-hydroxy-(ribonucleotide)(m) + GTP + H(2)O = (ribonucleotide)(n+m) + GMP + diphosphate (overall reaction).UniRule annotation EC:6.5.1.8

<p>This subsection of the 'Function' section provides information relevant to cofactors. A cofactor is any non-protein substance required for a protein to be catalytically active. Some cofactors are inorganic, such as the metal atoms zinc, iron, and copper in various oxidation states. Others, such as most vitamins, are organic.<p><a href='/help/cofactor' target='_top'>More...</a></p>Cofactori

Mn2+UniRule annotationNote: Binds 2 manganese ions per subunit.UniRule annotation

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the 'Description' field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi120Manganese 1UniRule annotation1
Metal bindingi123Manganese 1UniRule annotation1
Metal bindingi123Manganese 2UniRule annotation1
Metal bindingi228Manganese 1; via tele nitrogenUniRule annotation1
Metal bindingi260Manganese 2; via tele nitrogenUniRule annotation1
Metal bindingi354Manganese 2; via tele nitrogenUniRule annotation1
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei410GMPUniRule annotation1
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section is used for enzymes and indicates the residues directly involved in catalysis.<p><a href='/help/act_site' target='_top'>More...</a></p>Active sitei429GMP-histidine intermediateUniRule annotation1
Binding sitei505GMPUniRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes a region in the protein which binds nucleotide phosphates. It always involves more than one amino acid and includes all residues involved in nucleotide-binding.<p><a href='/help/np_bind' target='_top'>More...</a></p>Nucleotide bindingi227 – 231GMPUniRule annotation5
Nucleotide bindingi354 – 355GMPUniRule annotation2
Nucleotide bindingi403 – 406GMPUniRule annotation4
Nucleotide bindingi429 – 432GMPUniRule annotation4

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionLigase
Biological processtRNA processing
LigandGTP-binding, Manganese, Metal-binding, Nucleotide-binding

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
RNA-splicing ligase RtcB homologUniRule annotation (EC:6.5.1.8UniRule annotation)
Alternative name(s):
3'-phosphate/5'-hydroxy nucleic acid ligaseUniRule annotation
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: 'Name', 'Synonyms', 'Ordered locus names' and 'ORF names'.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
ORF Names:PF11_0068
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiPlasmodium falciparum (isolate 3D7)
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the 'taxonomic identifier' or 'taxid'.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri36329 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryotaSarAlveolataApicomplexaAconoidasidaHaemosporidaPlasmodiidaePlasmodiumPlasmodium (Laverania)

Organism-specific databases

Eukaryotic Pathogen, Vector and Host Database Resources

More...
VEuPathDBi
PlasmoDB:PF3D7_1105700

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'PTM / Processing' section describes the extent of a polypeptide chain in the mature protein following processing or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00004072391 – 506RNA-splicing ligase RtcB homologAdd BLAST506

Proteomic databases

PRoteomics IDEntifications database

More...
PRIDEi
Q8IIU6

PTM databases

SwissPalm database of S-palmitoylation events

More...
SwissPalmi
Q8IIU6

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction%5Fsection">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function%5Fsection">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Catalytic component of the tRNA-splicing ligase complex.

UniRule annotation

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

3D structure databases

SWISS-MODEL Repository - a database of annotated 3D protein structure models

More...
SMRi
Q8IIU6

Database of comparative protein structure models

More...
ModBasei
Search...

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

<p>This subsection of the 'Family and domains' section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Belongs to the RtcB family.UniRule annotation

Phylogenomic databases

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
CLU_022279_0_0_1

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
Q8IIU6

Identification of Orthologs from Complete Genome Data

More...
OMAi
QTRGVEC

Database for complete collections of gene phylogenies

More...
PhylomeDBi
Q8IIU6

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
3.90.1860.10, 1 hit

HAMAP database of protein families

More...
HAMAPi
MF_03144, RtcB_euk, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR001233, RtcB
IPR036025, RtcB-like_sf
IPR027513, RtcB_euk

The PANTHER Classification System

More...
PANTHERi
PTHR11118, PTHR11118, 1 hit

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF01139, RtcB, 1 hit

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF103365, SSF103365, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence%5Flength">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

Q8IIU6-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MKGIPKRPIS NYIEKTNETN LYKIRKGLVN EMNVEGHIYV NEKLKTLLDE
60 70 80 90 100
EIATYELNKN STFLPAVMQI ANVSTLPGIV KASIALPDVH AGYGFSIGNV
110 120 130 140 150
AAFDMDNEKA IVSPGGVGFD INCGVRLIRT NLFYEDIKPK QEELTQLLFN
160 170 180 190 200
HIPVGVGSQG FILCNQENLD DALCLGMDWC VKEGYSWIED KLNCEDNGRS
210 220 230 240 250
LYADSNFVSI RAKKRGITQM GTLGAGNHYA EIQIVDQIYD KKSAKLMGIE
260 270 280 290 300
KKNQVCIMIH SGSRGLGHQI ATDALIDMEK SMNKYKINVI DKQLACTPIH
310 320 330 340 350
SKEGQNYLKA MGSACNFAWI NRSSMTFLAR QAFSKIFNQS PDDLDMHVIY
360 370 380 390 400
DVSHNIAKIE EHYIDGKIKK LLVHRKGSTR AFPPFHPLVP LDYQYCGQPI
410 420 430 440 450
LIGGTMGTYS YVLTGNEKAM QATFGSTCHG AGRALSRNKS RNTLSYLDVL
460 470 480 490 500
NKLKEQNISI RVASPKLIME EAPESYKNVC DVVQTCHDAG ISNKCFRLKP

VAVIKG
Length:506
Mass (Da):56,321
Last modified:March 1, 2003 - v1
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:i03BED714DB8B27DB
GO

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

More...
GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
AE014186 Genomic DNA Translation: AAN35657.1

NCBI Reference Sequences

More...
RefSeqi
XP_001347744.1, XM_001347708.1

Genome annotation databases

Ensembl protists genome annotation project

More...
EnsemblProtistsi
CZT98723; CZT98723; PF3D7_1105700

GeneDB pathogen genome database from Sanger Institute

More...
GeneDBi
PF3D7_1105700.1:pep

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
810620

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
pfa:PF3D7_1105700

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE014186 Genomic DNA Translation: AAN35657.1
RefSeqiXP_001347744.1, XM_001347708.1

3D structure databases

SMRiQ8IIU6
ModBaseiSearch...

PTM databases

SwissPalmiQ8IIU6

Proteomic databases

PRIDEiQ8IIU6

Genome annotation databases

EnsemblProtistsiCZT98723; CZT98723; PF3D7_1105700
GeneDBiPF3D7_1105700.1:pep
GeneIDi810620
KEGGipfa:PF3D7_1105700

Organism-specific databases

VEuPathDBiPlasmoDB:PF3D7_1105700

Phylogenomic databases

HOGENOMiCLU_022279_0_0_1
InParanoidiQ8IIU6
OMAiQTRGVEC
PhylomeDBiQ8IIU6

Family and domain databases

Gene3Di3.90.1860.10, 1 hit
HAMAPiMF_03144, RtcB_euk, 1 hit
InterProiView protein in InterPro
IPR001233, RtcB
IPR036025, RtcB-like_sf
IPR027513, RtcB_euk
PANTHERiPTHR11118, PTHR11118, 1 hit
PfamiView protein in Pfam
PF01139, RtcB, 1 hit
SUPFAMiSSF103365, SSF103365, 1 hit

MobiDB: a database of protein disorder and mobility annotations

More...
MobiDBi
Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the 'Entry information' section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiRTCB_PLAF7
<p>This subsection of the 'Entry information' section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called 'Primary (citable) accession number'.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: Q8IIU6
<p>This subsection of the 'Entry information' section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification ('Last modified'). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: April 5, 2011
Last sequence update: March 1, 2003
Last modified: June 2, 2021
This is version 94 of the entry and version 1 of the sequence. See complete history.
<p>This subsection of the 'Entry information' section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)

<p>This section contains any relevant information that doesn't fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Documents

  1. SIMILARITY comments
    Index of protein domains and families
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health

We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.

Do not show this banner again