4C9B
Crystal structure of eIF4AIII-CWC22 complex
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0000184 | biological_process | nuclear-transcribed mRNA catabolic process, nonsense-mediated decay |
A | 0000398 | biological_process | mRNA splicing, via spliceosome |
A | 0003676 | molecular_function | nucleic acid binding |
A | 0003723 | molecular_function | RNA binding |
A | 0003724 | molecular_function | RNA helicase activity |
A | 0003729 | molecular_function | mRNA binding |
A | 0004386 | molecular_function | helicase activity |
A | 0005515 | molecular_function | protein binding |
A | 0005524 | molecular_function | ATP binding |
A | 0005634 | cellular_component | nucleus |
A | 0005654 | cellular_component | nucleoplasm |
A | 0005681 | cellular_component | spliceosomal complex |
A | 0005730 | cellular_component | nucleolus |
A | 0005737 | cellular_component | cytoplasm |
A | 0005829 | cellular_component | cytosol |
A | 0006364 | biological_process | rRNA processing |
A | 0006397 | biological_process | mRNA processing |
A | 0006406 | biological_process | mRNA export from nucleus |
A | 0006417 | biological_process | regulation of translation |
A | 0008143 | molecular_function | poly(A) binding |
A | 0008306 | biological_process | associative learning |
A | 0008380 | biological_process | RNA splicing |
A | 0010629 | biological_process | negative regulation of gene expression |
A | 0014070 | biological_process | response to organic cyclic compound |
A | 0016020 | cellular_component | membrane |
A | 0016607 | cellular_component | nuclear speck |
A | 0016787 | molecular_function | hydrolase activity |
A | 0016887 | molecular_function | ATP hydrolysis activity |
A | 0017148 | biological_process | negative regulation of translation |
A | 0030425 | cellular_component | dendrite |
A | 0035145 | cellular_component | exon-exon junction complex |
A | 0035368 | molecular_function | selenocysteine insertion sequence binding |
A | 0035613 | molecular_function | RNA stem-loop binding |
A | 0035640 | biological_process | exploration behavior |
A | 0043021 | molecular_function | ribonucleoprotein complex binding |
A | 0043025 | cellular_component | neuronal cell body |
A | 0045727 | biological_process | positive regulation of translation |
A | 0048701 | biological_process | embryonic cranial skeleton morphogenesis |
A | 0051028 | biological_process | mRNA transport |
A | 0071006 | cellular_component | U2-type catalytic step 1 spliceosome |
A | 0071013 | cellular_component | catalytic step 2 spliceosome |
A | 0072715 | biological_process | cellular response to selenite ion |
A | 0090394 | biological_process | negative regulation of excitatory postsynaptic potential |
A | 0098794 | cellular_component | postsynapse |
A | 0098978 | cellular_component | glutamatergic synapse |
A | 0099578 | biological_process | regulation of translation at postsynapse, modulating synaptic transmission |
A | 1904570 | biological_process | negative regulation of selenocysteine incorporation |
A | 1990416 | biological_process | cellular response to brain-derived neurotrophic factor stimulus |
A | 1990904 | cellular_component | ribonucleoprotein complex |
A | 2000622 | biological_process | regulation of nuclear-transcribed mRNA catabolic process, nonsense-mediated decay |
B | 0003723 | molecular_function | RNA binding |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE PO4 A 1412 |
Chain | Residue |
A | SER84 |
A | GLY85 |
A | THR86 |
A | GLY87 |
A | LYS88 |
A | THR89 |
A | GOL1419 |
B | PRO124 |
B | ARG128 |
site_id | AC2 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE GOL A 1413 |
Chain | Residue |
A | PHE58 |
A | GLU59 |
A | LYS60 |
A | HOH2168 |
A | HOH2169 |
site_id | AC3 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE GOL A 1414 |
Chain | Residue |
A | ASP310 |
A | HOH2134 |
A | HOH2147 |
A | HOH2149 |
B | LEU275 |
B | THR279 |
B | GLY311 |
site_id | AC4 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE GOL A 1415 |
Chain | Residue |
A | TRP292 |
A | LYS296 |
site_id | AC5 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE GOL B 1407 |
Chain | Residue |
A | ALA55 |
A | GLY57 |
A | HOH2031 |
B | ARG199 |
B | ASP380 |
B | ASN383 |
site_id | AC6 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE GOL A 1416 |
Chain | Residue |
A | LEU341 |
A | ILE349 |
A | ILE365 |
A | GLY366 |
A | ARG373 |
A | HOH2157 |
site_id | AC7 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE GOL A 1417 |
Chain | Residue |
A | LYS74 |
A | ARG76 |
B | LYS250 |
B | GLU291 |
site_id | AC8 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE GOL A 1418 |
Chain | Residue |
A | VAL304 |
A | ALA327 |
B | SER176 |
site_id | AC9 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE GOL A 1419 |
Chain | Residue |
A | SER84 |
A | LYS88 |
A | THR89 |
A | ASP187 |
A | GLU188 |
A | ILE217 |
A | PO41412 |
A | HOH2049 |
A | HOH2050 |
site_id | BC1 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE GOL A 1420 |
Chain | Residue |
A | CYS269 |
A | TYR272 |
A | ASP273 |
B | LYS172 |
Functional Information from PROSITE/UniProt
site_id | PS00039 |
Number of Residues | 9 |
Details | DEAD_ATP_HELICASE DEAD-box subfamily ATP-dependent helicases signature. VLDEADEmL |
Chain | Residue | Details |
A | VAL185-LEU193 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 5 |
Details | BINDING: BINDING => ECO:0000269|PubMed:16923391, ECO:0000269|PubMed:16931718, ECO:0000269|PubMed:19033377, ECO:0000269|PubMed:20479275, ECO:0007744|PDB:2HYI, ECO:0007744|PDB:2J0Q, ECO:0007744|PDB:2J0S, ECO:0007744|PDB:2XB2, ECO:0007744|PDB:3EX7 |
Chain | Residue | Details |
A | LYS60 | |
A | GLN65 | |
A | GLY85 | |
A | ASP342 | |
A | ARG367 |
site_id | SWS_FT_FI2 |
Number of Residues | 1 |
Details | MOD_RES: N-acetylmethionine => ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692 |
Chain | Residue | Details |
A | MET1 |
site_id | SWS_FT_FI3 |
Number of Residues | 1 |
Details | MOD_RES: N-acetylalanine; in Eukaryotic initiation factor 4A-III, N-terminally processed => ECO:0000269|Ref.8, ECO:0007744|PubMed:19369195, ECO:0007744|PubMed:19413330, ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:22223895, ECO:0007744|PubMed:22814378 |
Chain | Residue | Details |
A | ALA2 |
site_id | SWS_FT_FI4 |
Number of Residues | 1 |
Details | MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P60842 |
Chain | Residue | Details |
A | SER10 |
site_id | SWS_FT_FI5 |
Number of Residues | 1 |
Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163 |
Chain | Residue | Details |
A | SER12 |
site_id | SWS_FT_FI6 |
Number of Residues | 1 |
Details | MOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:P60842 |
Chain | Residue | Details |
A | LYS124 |
site_id | SWS_FT_FI7 |
Number of Residues | 1 |
Details | MOD_RES: Phosphothreonine => ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163 |
Chain | Residue | Details |
A | THR163 |
site_id | SWS_FT_FI8 |
Number of Residues | 1 |
Details | MOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:P60843 |
Chain | Residue | Details |
A | LYS198 |
site_id | SWS_FT_FI9 |
Number of Residues | 2 |
Details | MOD_RES: N6-acetyllysine => ECO:0007744|PubMed:19608861 |
Chain | Residue | Details |
A | LYS296 | |
A | LYS321 |
site_id | SWS_FT_FI10 |
Number of Residues | 1 |
Details | CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) => ECO:0007744|PubMed:25218447, ECO:0007744|PubMed:25755297, ECO:0007744|PubMed:25772364, ECO:0007744|PubMed:28112733 |
Chain | Residue | Details |
A | LYS19 |
site_id | SWS_FT_FI11 |
Number of Residues | 3 |
Details | CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) => ECO:0007744|PubMed:28112733 |
Chain | Residue | Details |
A | LYS314 | |
A | LYS382 |
site_id | SWS_FT_FI12 |
Number of Residues | 2 |
Details | CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) => ECO:0000250|UniProtKB:P60842 |
Chain | Residue | Details |
A | LYS152 | |
A | LYS374 |