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The following sections contain reference sequences that belong to a
specific genome build. Explain
This section includes genomic Reference
Sequences (RefSeqs) from all assemblies on which this gene is annotated, such as
RefSeqs for chromosomes and scaffolds (contigs) from both reference and alternate
assemblies. Model RNAs and proteins are also reported here.
Reference assembly
Genomic
-
NC_003076.8 Reference assembly
- Range
-
1840755..1843872 complement
- Download
- GenBank, FASTA, Sequence Viewer (Graphics)
mRNA and Protein(s)
-
NM_120693.4 → NP_196229.1 DnaJ and myb-like DNA-binding domain-containing protein [Arabidopsis thaliana]
See identical proteins and their annotated locations for NP_196229.1
Status: REVIEWED
- UniProtKB/TrEMBL
- A0A178UFW7, A0A5S9Y411, Q9LHS5
- Conserved Domains (2) summary
-
- COG5269
Location:98 → 422
- ZUO1; Ribosome-associated chaperone zuotin [Translation, ribosomal structure and biogenesis / Posttranslational modification, protein turnover, chaperones]
- cd00167
Location:607 → 653
- SANT; 'SWI3, ADA2, N-CoR and TFIIIB' DNA-binding domains. Tandem copies of the domain bind telomeric DNA tandem repeatsas part of the capping complex. Binding is sequence dependent for repeats which contain the G/C rich motif [C2-3 A (CA)1-6]. The domain is ...
-
NM_001203305.1 → NP_001190234.1 DnaJ and myb-like DNA-binding domain-containing protein [Arabidopsis thaliana]
See identical proteins and their annotated locations for NP_001190234.1
Status: REVIEWED
- UniProtKB/TrEMBL
- A0A178UFW7, A0A5S9Y411, Q9LHS5
- Conserved Domains (2) summary
-
- COG5269
Location:98 → 422
- ZUO1; Ribosome-associated chaperone zuotin [Translation, ribosomal structure and biogenesis / Posttranslational modification, protein turnover, chaperones]
- cd00167
Location:607 → 653
- SANT; 'SWI3, ADA2, N-CoR and TFIIIB' DNA-binding domains. Tandem copies of the domain bind telomeric DNA tandem repeatsas part of the capping complex. Binding is sequence dependent for repeats which contain the G/C rich motif [C2-3 A (CA)1-6]. The domain is ...