3EN9
Structure of the Methanococcus jannaschii KAE1-BUD32 fusion protein
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000166 | molecular_function | nucleotide binding |
| A | 0000408 | cellular_component | EKC/KEOPS complex |
| A | 0002949 | biological_process | tRNA threonylcarbamoyladenosine modification |
| A | 0003824 | molecular_function | catalytic activity |
| A | 0004222 | molecular_function | metalloendopeptidase activity |
| A | 0004672 | molecular_function | protein kinase activity |
| A | 0004674 | molecular_function | protein serine/threonine kinase activity |
| A | 0004712 | molecular_function | protein serine/threonine/tyrosine kinase activity |
| A | 0005506 | molecular_function | iron ion binding |
| A | 0005524 | molecular_function | ATP binding |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0006400 | biological_process | tRNA modification |
| A | 0006468 | biological_process | protein phosphorylation |
| A | 0008033 | biological_process | tRNA processing |
| A | 0008270 | molecular_function | zinc ion binding |
| A | 0016301 | molecular_function | kinase activity |
| A | 0016740 | molecular_function | transferase activity |
| A | 0016746 | molecular_function | acyltransferase activity |
| A | 0016747 | molecular_function | acyltransferase activity, transferring groups other than amino-acyl groups |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0061711 | molecular_function | tRNA N(6)-L-threonylcarbamoyladenine synthase activity |
| A | 0070525 | biological_process | tRNA threonylcarbamoyladenosine metabolic process |
| A | 0106310 | molecular_function | protein serine kinase activity |
| B | 0000166 | molecular_function | nucleotide binding |
| B | 0000408 | cellular_component | EKC/KEOPS complex |
| B | 0002949 | biological_process | tRNA threonylcarbamoyladenosine modification |
| B | 0003824 | molecular_function | catalytic activity |
| B | 0004222 | molecular_function | metalloendopeptidase activity |
| B | 0004672 | molecular_function | protein kinase activity |
| B | 0004674 | molecular_function | protein serine/threonine kinase activity |
| B | 0004712 | molecular_function | protein serine/threonine/tyrosine kinase activity |
| B | 0005506 | molecular_function | iron ion binding |
| B | 0005524 | molecular_function | ATP binding |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0006400 | biological_process | tRNA modification |
| B | 0006468 | biological_process | protein phosphorylation |
| B | 0008033 | biological_process | tRNA processing |
| B | 0008270 | molecular_function | zinc ion binding |
| B | 0016301 | molecular_function | kinase activity |
| B | 0016740 | molecular_function | transferase activity |
| B | 0016746 | molecular_function | acyltransferase activity |
| B | 0016747 | molecular_function | acyltransferase activity, transferring groups other than amino-acyl groups |
| B | 0046872 | molecular_function | metal ion binding |
| B | 0061711 | molecular_function | tRNA N(6)-L-threonylcarbamoyladenine synthase activity |
| B | 0070525 | biological_process | tRNA threonylcarbamoyladenosine metabolic process |
| B | 0106310 | molecular_function | protein serine kinase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE MG A 600 |
| Chain | Residue |
| A | HIS106 |
| A | HIS110 |
| A | TYR127 |
| A | ASP284 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE MG B 600 |
| Chain | Residue |
| B | HIS106 |
| B | HIS110 |
| B | TYR127 |
| B | ASP284 |
| site_id | AC3 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE TBR B 601 |
| Chain | Residue |
| A | GLU501 |
| A | GLU504 |
| B | PRO0 |
| B | ASP21 |
| B | GLU23 |
| B | LEU25 |
| A | ASP500 |
| site_id | AC4 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE TBR A 601 |
| Chain | Residue |
| A | ILE519 |
| A | GLU522 |
Functional Information from PROSITE/UniProt
| site_id | PS00109 |
| Number of Residues | 13 |
| Details | PROTEIN_KINASE_TYR Tyrosine protein kinases specific active-site signature. VIHnDLTTSNFIF |
| Chain | Residue | Details |
| A | VAL447-PHE459 |
| site_id | PS01016 |
| Number of Residues | 21 |
| Details | GLYCOPROTEASE Glycoprotease family signature. RTlsltLKkPiIgvnHciAHI |
| Chain | Residue | Details |
| A | ARG91-ILE111 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 322 |
| Details | Region: {"description":"Kae1"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | Active site: {"description":"Proton acceptor; for kinase activity","evidences":[{"source":"HAMAP-Rule","id":"MF_01447","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 22 |
| Details | Binding site: {"evidences":[{"evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 4 |
| Details | Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_01447","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1ir3 |
| Chain | Residue | Details |
| A | SER455 | |
| A | ASP451 |
| site_id | CSA2 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1ir3 |
| Chain | Residue | Details |
| B | SER455 | |
| B | ASP451 |
| site_id | CSA3 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1ir3 |
| Chain | Residue | Details |
| A | THR453 | |
| A | ASP451 |
| site_id | CSA4 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1ir3 |
| Chain | Residue | Details |
| B | THR453 | |
| B | ASP451 |
| site_id | CSA5 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1ir3 |
| Chain | Residue | Details |
| A | ASN456 | |
| A | THR453 | |
| A | ASP451 |
| site_id | CSA6 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1ir3 |
| Chain | Residue | Details |
| B | ASN456 | |
| B | THR453 | |
| B | ASP451 |
