F4IHI1 · F4IHI1_ARATH
- ProteinSUMO-activating enzyme subunit
- GeneSAE2
- StatusUniProtKB unreviewed (TrEMBL)
- Amino acids628 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score3/5
Function
Pathway
Protein modification; protein sumoylation.
Features
Showing features for binding site, active site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 19-24 | ATP (UniProtKB | ChEBI) | ||||
Sequence: GAGGIG | ||||||
Binding site | 43 | ATP (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 51-54 | ATP (UniProtKB | ChEBI) | ||||
Sequence: NLNR | ||||||
Binding site | 67 | ATP (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 112-117 | ATP (UniProtKB | ChEBI) | ||||
Sequence: DNLDAR | ||||||
Binding site | 153 | Zn2+ (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 156 | Zn2+ (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Active site | 168 | Glycyl thioester intermediate | ||||
Sequence: C | ||||||
Binding site | 435 | Zn2+ (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 438 | Zn2+ (UniProtKB | ChEBI) | ||||
Sequence: C |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | SUMO activating enzyme complex | |
Molecular Function | ATP binding | |
Molecular Function | metal ion binding | |
Molecular Function | SUMO activating enzyme activity | |
Biological Process | protein sumoylation |
Keywords
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameSUMO-activating enzyme subunit
Gene names
Organism names
- Strain
- Taxonomic lineageEukaryota > Viridiplantae > Streptophyta > Embryophyta > Tracheophyta > Spermatophyta > Magnoliopsida > eudicotyledons > Gunneridae > Pentapetalae > rosids > malvids > Brassicales > Brassicaceae > Camelineae > Arabidopsis
Accessions
- Primary accessionF4IHI1
Proteomes
Organism-specific databases
Genome annotation databases
Subcellular Location
UniProt Annotation
GO Annotation
PTM/Processing
Proteomic databases
Expression
Gene expression databases
Interaction
Subunit
Heterodimer.
Structure
Family & Domains
Features
Showing features for domain, compositional bias, region.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 4-408 | THIF-type NAD/FAD binding fold | ||||
Sequence: QQQQSAIKGAKVLMVGAGGIGCELLKTLALSGFEDIHIIDMDTIEVSNLNRQFLFRRSHVGQSKAKVARDAVLRFRPNINIRSYHANVKNPEFDVDFFKQFDVVLNGLDNLDARRHVNRLCLAADVPLVESGTTGFLGQVTVHIKGKTECYECQTKPAPKTYPVCTITSTPTKFVHCIVWAKDLLFAKLFGDKNQDNDLNVRSNNSASSSKETEDVFERSEDEDIEQYGRKIYDHVFGSNIEAALSNEETWKNRRRPRPIYSKDVLPESLTQQNGSTQNCSVTDGDLMVSAMPSLGLKNPQELWGLTQNSLVFIEALKLFFAKRKKVCVEIGHLTFDKDDQLAVEFVTAAANIRAESFGIPLHSLFEAKGIAGNIVHAVATTNAIIAGLIVIEAIKVLKKDVDKF | ||||||
Compositional bias | 200-214 | Polar residues | ||||
Sequence: NDLNVRSNNSASSSK | ||||||
Region | 200-224 | Disordered | ||||
Sequence: NDLNVRSNNSASSSKETEDVFERSE | ||||||
Domain | 325-372 | Ubiquitin-activating enzyme SCCH | ||||
Sequence: AKRKKVCVEIGHLTFDKDDQLAVEFVTAAANIRAESFGIPLHSLFEAK | ||||||
Domain | 445-537 | Ubiquitin/SUMO-activating enzyme ubiquitin-like | ||||
Sequence: LEINTRKSKLRDLVDKIVKTKLGMNLPLIMHGNSLLYEVGDDLDDIMVANYNANLEKYLSELPSPILNGSILTVEDLQQELSCKINVKHREEF | ||||||
Region | 535-628 | Disordered | ||||
Sequence: EEFDEEKEPEGMVLSGWTPSPATNGESASTSNNENPVDVTESSSGSEPASKKRRLSETEASNHKKETENVESEDDDIMEVENPMMVSKKKIRVE | ||||||
Compositional bias | 551-580 | Polar residues | ||||
Sequence: WTPSPATNGESASTSNNENPVDVTESSSGS | ||||||
Compositional bias | 581-605 | Basic and acidic residues | ||||
Sequence: EPASKKRRLSETEASNHKKETENVE |
Sequence similarities
Belongs to the ubiquitin-activating E1 family.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length628
- Mass (Da)70,055
- Last updated2011-06-28 v1
- Checksum0F49EDC21C5BCD8E
Computationally mapped potential isoform sequences
There is 1 potential isoform mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
Q9SJT1 | SAE2_ARATH | SAE2 | 700 |
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 200-214 | Polar residues | ||||
Sequence: NDLNVRSNNSASSSK | ||||||
Compositional bias | 551-580 | Polar residues | ||||
Sequence: WTPSPATNGESASTSNNENPVDVTESSSGS | ||||||
Compositional bias | 581-605 | Basic and acidic residues | ||||
Sequence: EPASKKRRLSETEASNHKKETENVE |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
CP002685 EMBL· GenBank· DDBJ | AEC07183.1 EMBL· GenBank· DDBJ | Genomic DNA |