Summary: OB-fold nucleic acid binding domain
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OB-fold nucleic acid binding domain Provide feedback
This family contains OB-fold domains that bind to nucleic acids [4]. The family includes the anti-codon binding domain of lysyl, aspartyl, and asparaginyl -tRNA synthetases (See PF00152). Aminoacyl-tRNA synthetases catalyse the addition of an amino acid to the appropriate tRNA molecule EC:6.1.1.-. This family also includes part of RecG helicase involved in DNA repair. Replication factor A is a heterotrimeric complex, that contains a subunit in this family [2,3]. This domain is also found at the C-terminus of bacterial DNA polymerase III alpha chain.
Literature references
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Ruff M, Krishnaswamy S, Boeglin M, Poterszman A, Mitschler A, Podjarny A, Rees B, Thierry JC, Moras D; , Science 1991;252:1682-1689.: Class II aminoacyl transfer RNA synthetases: crystal structure of yeast aspartyl-tRNA synthetase complexed with tRNA(Asp). PUBMED:2047877 EPMC:2047877
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Keshav KF, Chen C, Dutta A; , Mol Cell Biol 1995;15:3119-3128.: Rpa4, a homolog of the 34-kilodalton subunit of the replication protein A complex. PUBMED:7760808 EPMC:7760808
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Bochkarev A, Pfuetzner RA, Edwards AM, Frappier L; , Nature 1997;385:176-181.: Structure of the single-stranded-DNA-binding domain of replication protein A bound to DNA. PUBMED:8990123 EPMC:8990123
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Koonin EV, Wolf YI, Aravind L; , Adv Protein Chem 2000;54:245-275.: Protein fold recognition using sequence profiles and its application in structural genomics. PUBMED:10829230 EPMC:10829230
External database links
| HOMSTRAD: | asprs |
| PANDIT: | PF01336 |
| Pseudofam: | PF01336 |
| SCOP: | 1asy |
| SYSTERS: | tRNA_anti-codon |
This tab holds annotation information from the InterPro database.
InterPro entry IPR004365
The OB-fold (oligonucleotide/oligosaccharide-binding fold) is found in all three kingdoms and its common architecture presents a binding face that has adapted to bind different ligands. The OB-fold is a five/six-stranded closed beta-barrel formed by 70-80 amino acid residues. The strands are connected by loops of varying length which form the functional appendages of the protein. The majority of OB-fold proteins use the same face for ligand binding or as an active site. Different OB-fold proteins use this 'fold-related binding face' to, variously, bind oligosaccharides, oligonucleotides, proteins, metal ions and catalytic substrates.
This entry contains OB-fold domains that bind to nucleic acids [PUBMED:10829230]. It includes the anti-codon binding domain of lysyl, aspartyl, and asparaginyl-tRNA synthetases (See INTERPRO). Aminoacyl-tRNA synthetases catalyse the addition of an amino acid to the appropriate tRNA molecule EC. This domain is found in RecG helicase involved in DNA repair. Replication factor A is a heterotrimeric complex, that contains a subunit in this family [PUBMED:7760808, PUBMED:8990123]. This domain is also found at the C terminus of bacterial DNA polymerase III alpha chain.
Gene Ontology
The mapping between Pfam and Gene Ontology is provided by InterPro. If you use this data please cite InterPro.
| Molecular function | nucleic acid binding (GO:0003676) |
Domain organisation
Below is a listing of the unique domain organisations or architectures in which this domain is found. More...
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Pfam Clan
This family is a member of clan OB (CL0021), which contains the following 45 members:
BOF CSD DNA_ligase_OB DUF2110 DUF223 DUF3127 DUF35 EFP eIF-1a eIF-5a EutN_CcmL EXOSC1 mRNA_cap_C OB_NTP_bind OB_RNB OmdA Phage_DNA_bind POT1 RecO_N RecO_N_2 Rep-A_N Rep_fac-A_3 Rho_RNA_bind Ribosom_S12_S23 Ribosomal_L2 Ribosomal_S17 RNA_pol_Rbc25 RNA_pol_Rpb8 RuvA_N S1 S1-like S1_2 SSB Stn1 TEBP_beta Ten1 Ten1_2 TOBE TOBE_2 TOBE_3 TRAM tRNA_anti-codon tRNA_anti-like tRNA_anti_2 tRNA_bindAlignments
We store a range of different sequence alignments for families. As well as the seed alignment from which the family is built, we provide the full alignment, generated by searching the sequence database using the family HMM. We also generate alignments using four representative proteomes (RP) sets, the NCBI sequence database, and our metagenomics sequence database. More...
View options
We make a range of alignments for each Pfam-A family. You can see a description of each above. You can view these alignments in various ways but please note that some types of alignment are never generated while others may not be available for all families, most commonly because the alignments are too large to handle.
| Seed (640) |
Full (22969) |
Representative proteomes | NCBI (20485) |
Meta (6498) |
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| RP15 (2125) |
RP35 (3961) |
RP55 (5336) |
RP75 (6345) |
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| PP/heatmap | 1 | |||||||
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1Cannot generate PP/Heatmap alignments for seeds; no PP data available
Key:
available,
not generated,
— not available.
Format an alignment
Download options
We make all of our alignments available in Stockholm format. You can download them here as raw, plain text files or as gzip-compressed files.
| Seed (640) |
Full (22969) |
Representative proteomes | NCBI (20485) |
Meta (6498) |
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|---|---|---|---|---|---|---|---|---|
| RP15 (2125) |
RP35 (3961) |
RP55 (5336) |
RP75 (6345) |
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| Raw Stockholm | ||||||||
| Gzipped | ||||||||
You can also download a FASTA format file containing the full-length sequences for all sequences in the full alignment.
External links
MyHits provides a collection of tools to handle multiple sequence alignments. For example, one can refine a seed alignment (sequence addition or removal, re-alignment or manual edition) and then search databases for remote homologs using HMMER3.
HMM logo
HMM logos is one way of visualising profile HMMs. Logos provide a quick overview of the properties of an HMM in a graphical form. You can see a more detailed description of HMM logos and find out how you can interpret them here. More...
Trees
This page displays the phylogenetic tree for this family's seed alignment. We use FastTree to calculate neighbour join trees with a local bootstrap based on 100 resamples (shown next to the tree nodes). FastTree calculates approximately-maximum-likelihood phylogenetic trees from our seed alignment.
Note: You can also download the data file for the tree.
Curation and family details
This section shows the detailed information about the Pfam family. You can see the definitions of many of the terms in this section in the glossary and a fuller explanation of the scoring system that we use in the scores section of the help pages.
Curation
| Seed source: | [4] |
| Previous IDs: | Aspartyl_tRNA_N; tRNA_anti; |
| Type: | Domain |
| Author: | Bateman A, Mian N, Finn RD |
| Number in seed: | 640 |
| Number in full: | 22969 |
| Average length of the domain: | 80.20 aa |
| Average identity of full alignment: | 20 % |
| Average coverage of the sequence by the domain: | 12.26 % |
HMM information
| HMM build commands: |
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 23193494 -E 1000 --cpu 4 HMM pfamseq
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| Model details: |
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| Model length: | 75 | ||||||||||||
| Family (HMM) version: | 20 | ||||||||||||
| Download: | download the raw HMM for this family |
Species distribution
Sunburst controls
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Interactions
There are 4 interactions for this family. More...
tRNA-synt_2 Rep_fac-A_3 Rep_fac-A_C DNA_pol3_alphaStructures
For those sequences which have a structure in the Protein DataBank, we use the mapping between UniProt, PDB and Pfam coordinate systems from the PDBe group, to allow us to map Pfam domains onto UniProt sequences and three-dimensional protein structures. The table below shows the structures on which the tRNA_anti-codon domain has been found. There are 111 instances of this domain found in the PDB. Note that there may be multiple copies of the domain in a single PDB structure, since many structures contain multiple copies of the same protein seqence.
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Archea
Eukaryota
Bacteria
Other sequences
Viruses
Unclassified
Viroids
Unclassified sequence