1H0X
Structure of Alba: an archaeal chromatin protein modulated by acetylation
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003676 | molecular_function | nucleic acid binding |
| A | 0003677 | molecular_function | DNA binding |
| A | 0003690 | molecular_function | double-stranded DNA binding |
| A | 0003723 | molecular_function | RNA binding |
| A | 0004518 | molecular_function | nuclease activity |
| A | 0005515 | molecular_function | protein binding |
| A | 0005694 | cellular_component | chromosome |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0030261 | biological_process | chromosome condensation |
| A | 0042802 | molecular_function | identical protein binding |
| B | 0003676 | molecular_function | nucleic acid binding |
| B | 0003677 | molecular_function | DNA binding |
| B | 0003690 | molecular_function | double-stranded DNA binding |
| B | 0003723 | molecular_function | RNA binding |
| B | 0004518 | molecular_function | nuclease activity |
| B | 0005515 | molecular_function | protein binding |
| B | 0005694 | cellular_component | chromosome |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0030261 | biological_process | chromosome condensation |
| B | 0042802 | molecular_function | identical protein binding |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 10 |
| Details | BINDING: BINDING => ECO:0000250|UniProtKB:P60848 |
| Chain | Residue | Details |
| A | LEU13 | |
| B | ALA41 | |
| A | ILE14 | |
| A | VAL19 | |
| A | ILE39 | |
| A | ALA41 | |
| B | LEU13 | |
| B | ILE14 | |
| B | VAL19 | |
| B | ILE39 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | MOD_RES: N-acetylserine; by ard1 acetylase => ECO:0000269|PubMed:11935028, ECO:0000269|PubMed:17511810, ECO:0000269|PubMed:29679495 |
| Chain | Residue | Details |
| A | GLU-1 | |
| B | GLU-1 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | MOD_RES: N6-methyllysine; alternate => ECO:0000269|PubMed:29679495 |
| Chain | Residue | Details |
| A | LEU13 | |
| B | LEU13 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | SITE: Not acetylated by pat acetylase => ECO:0000269|PubMed:15824122 |
| Chain | Residue | Details |
| A | ILE14 | |
| B | ILE14 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 4 |
| Details | MOD_RES: Deamidated asparagine; partial => ECO:0000269|PubMed:29679495 |
| Chain | Residue | Details |
| A | THR28 | |
| A | ILE55 | |
| B | THR28 | |
| B | ILE55 |
| site_id | SWS_FT_FI6 |
| Number of Residues | 2 |
| Details | MOD_RES: Deamidated glutamine; partial => ECO:0000269|PubMed:29679495 |
| Chain | Residue | Details |
| A | LEU29 | |
| B | LEU29 |
| site_id | SWS_FT_FI7 |
| Number of Residues | 4 |
| Details | MOD_RES: N6-methyllysine; partial => ECO:0000269|PubMed:29679495 |
| Chain | Residue | Details |
| A | ILE37 | |
| A | ILE94 | |
| B | ILE37 | |
| B | ILE94 |
| site_id | SWS_FT_FI8 |
| Number of Residues | 4 |
| Details | MOD_RES: N6-acetyllysine; partial => ECO:0000269|PubMed:29679495 |
| Chain | Residue | Details |
| A | ALA45 | |
| A | ILE65 | |
| B | ALA45 | |
| B | ILE65 |
| site_id | SWS_FT_FI9 |
| Number of Residues | 4 |
| Details | MOD_RES: Aspartate methyl ester; partial => ECO:0000269|PubMed:29679495 |
| Chain | Residue | Details |
| A | LYS48 | |
| A | THR78 | |
| B | LYS48 | |
| B | THR78 |
| site_id | SWS_FT_FI10 |
| Number of Residues | 2 |
| Details | MOD_RES: N6-methyllysine; alternate; partial => ECO:0000269|PubMed:29679495 |
| Chain | Residue | Details |
| A | LEU61 | |
| B | LEU61 |
| site_id | SWS_FT_FI11 |
| Number of Residues | 2 |
| Details | MOD_RES: Glutamate methyl ester (Glu); partial => ECO:0000269|PubMed:29679495 |
| Chain | Residue | Details |
| A | GLU66 | |
| B | GLU66 |
| site_id | SWS_FT_FI12 |
| Number of Residues | 2 |
| Details | MOD_RES: N5-methylglutamine; partial => ECO:0000269|PubMed:29679495 |
| Chain | Residue | Details |
| A | VAL72 | |
| B | VAL72 |
