Loading
PDBj
MenuPDBj@FacebookPDBj@X(formerly Twitter)PDBj@BlueSkyPDBj@YouTubewwPDB FoundationwwPDBDonate
RCSB PDBPDBeBMRBAdv. SearchSearch help

9FMS

Cryo-EM structure of S. cerevisiae Rai1-Rat1-Rtt103(252-273) complex.

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0000448biological_processcleavage in ITS2 between 5.8S rRNA and LSU-rRNA of tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA)
A0000463biological_processmaturation of LSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA)
A0000466biological_processmaturation of 5.8S rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA)
A0000956biological_processnuclear-transcribed mRNA catabolic process
A0003723molecular_functionRNA binding
A0004518molecular_functionnuclease activity
A0005515molecular_functionprotein binding
A0005634cellular_componentnucleus
A0005829cellular_componentcytosol
A0006353biological_processDNA-templated transcription termination
A0006364biological_processrRNA processing
A0006397biological_processmRNA processing
A0016787molecular_functionhydrolase activity
A0030234molecular_functionenzyme regulator activity
A0030846biological_processtermination of RNA polymerase II transcription, poly(A)-coupled
A0031087biological_processdeadenylation-independent decapping of nuclear-transcribed mRNA
A0034353molecular_functionmRNA 5'-diphosphatase activity
A0046872molecular_functionmetal ion binding
A0071035biological_processnuclear polyadenylation-dependent rRNA catabolic process
A0090730cellular_componentLas1 complex
A0110103cellular_componentRNA polymerase II termination complex
A0110152molecular_functionRNA NAD+-cap (NAD+-forming) hydrolase activity
A0110155biological_processNAD-cap decapping
A1904595biological_processpositive regulation of termination of RNA polymerase II transcription
A1990174molecular_functionphosphodiesterase decapping endonuclease activity
B0000398biological_processmRNA splicing, via spliceosome
B0000448biological_processcleavage in ITS2 between 5.8S rRNA and LSU-rRNA of tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA)
B0000956biological_processnuclear-transcribed mRNA catabolic process
B0003676molecular_functionnucleic acid binding
B0003723molecular_functionRNA binding
B0003729molecular_functionmRNA binding
B0004518molecular_functionnuclease activity
B0004527molecular_functionexonuclease activity
B0004534molecular_function5'-3' RNA exonuclease activity
B0005515molecular_functionprotein binding
B0005634cellular_componentnucleus
B0005654cellular_componentnucleoplasm
B0005739cellular_componentmitochondrion
B0006139biological_processnucleobase-containing compound metabolic process
B0006353biological_processDNA-templated transcription termination
B0006364biological_processrRNA processing
B0006397biological_processmRNA processing
B0016787molecular_functionhydrolase activity
B0019843molecular_functionrRNA binding
B0030846biological_processtermination of RNA polymerase II transcription, poly(A)-coupled
B0030847biological_processtermination of RNA polymerase II transcription, exosome-dependent
B0034244biological_processnegative regulation of transcription elongation by RNA polymerase II
B0043144biological_processsno(s)RNA processing
B0071028biological_processnuclear mRNA surveillance
B0071035biological_processnuclear polyadenylation-dependent rRNA catabolic process
B0090730cellular_componentLas1 complex
B0110103cellular_componentRNA polymerase II termination complex
B0110155biological_processNAD-cap decapping
B1904595biological_processpositive regulation of termination of RNA polymerase II transcription
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues114
DetailsRegion: {"description":"Interaction with RAT1"}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues4
DetailsBinding site: {"evidences":[{"source":"UniProtKB","id":"O13836","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues3
DetailsBinding site: {"evidences":[{"source":"UniProtKB","id":"O70348","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"18407956","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

242500

PDB entries from 2025-10-01

PDB statisticsPDBj update infoContact PDBjnumon