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9DSO

CRYO-EM STRUCTURE OF SACCHAROMYCES CEREVISIAE RAT1-RAI1-RTT103 COMPLEX

Functional Information from GO Data
ChainGOidnamespacecontents
A0000398biological_processmRNA splicing, via spliceosome
A0000448biological_processcleavage in ITS2 between 5.8S rRNA and LSU-rRNA of tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA)
A0000956biological_processnuclear-transcribed mRNA catabolic process
A0003676molecular_functionnucleic acid binding
A0003723molecular_functionRNA binding
A0003729molecular_functionmRNA binding
A0004518molecular_functionnuclease activity
A0004527molecular_functionexonuclease activity
A0004534molecular_function5'-3' RNA exonuclease activity
A0005515molecular_functionprotein binding
A0005634cellular_componentnucleus
A0005654cellular_componentnucleoplasm
A0005739cellular_componentmitochondrion
A0006139biological_processnucleobase-containing compound metabolic process
A0006351biological_processDNA-templated transcription
A0006353biological_processDNA-templated transcription termination
A0006364biological_processrRNA processing
A0006397biological_processmRNA processing
A0016787molecular_functionhydrolase activity
A0019843molecular_functionrRNA binding
A0030846biological_processtermination of RNA polymerase II transcription, poly(A)-coupled
A0030847biological_processtermination of RNA polymerase II transcription, exosome-dependent
A0034244biological_processnegative regulation of transcription elongation by RNA polymerase II
A0043144biological_processsno(s)RNA processing
A0071028biological_processnuclear mRNA surveillance
A0071035biological_processnuclear polyadenylation-dependent rRNA catabolic process
A0110155biological_processNAD-cap decapping
A1904595biological_processpositive regulation of termination of RNA polymerase II transcription
B0000166molecular_functionnucleotide binding
B0000448biological_processcleavage in ITS2 between 5.8S rRNA and LSU-rRNA of tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA)
B0000463biological_processmaturation of LSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA)
B0000466biological_processmaturation of 5.8S rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA)
B0000956biological_processnuclear-transcribed mRNA catabolic process
B0003723molecular_functionRNA binding
B0004518molecular_functionnuclease activity
B0005515molecular_functionprotein binding
B0005634cellular_componentnucleus
B0005829cellular_componentcytosol
B0006351biological_processDNA-templated transcription
B0006353biological_processDNA-templated transcription termination
B0006364biological_processrRNA processing
B0006397biological_processmRNA processing
B0016787molecular_functionhydrolase activity
B0030234molecular_functionenzyme regulator activity
B0030846biological_processtermination of RNA polymerase II transcription, poly(A)-coupled
B0031087biological_processdeadenylation-independent decapping of nuclear-transcribed mRNA
B0034353molecular_functionmRNA 5'-diphosphatase activity
B0046872molecular_functionmetal ion binding
B0071035biological_processnuclear polyadenylation-dependent rRNA catabolic process
B0110152molecular_functionRNA NAD+-cap (NAD+-forming) hydrolase activity
B0110155biological_processNAD-cap decapping
B1904595biological_processpositive regulation of termination of RNA polymerase II transcription
B1990174molecular_functionphosphodiesterase decapping endonuclease activity
C0000785cellular_componentchromatin
C0000993molecular_functionRNA polymerase II complex binding
C0003677molecular_functionDNA binding
C0005515molecular_functionprotein binding
C0005634cellular_componentnucleus
C0006351biological_processDNA-templated transcription
C0010526biological_processtransposable element silencing
C0031124biological_processmRNA 3'-end processing
C0035861cellular_componentsite of double-strand break
C0099122molecular_functionRNA polymerase II C-terminal domain binding
C1990269molecular_functionRNA polymerase II C-terminal domain phosphoserine binding
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsBinding site: {"evidences":[{"source":"UniProtKB","id":"O13836","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues3
DetailsBinding site: {"evidences":[{"source":"UniProtKB","id":"O70348","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"18407956","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

248335

PDB entries from 2026-01-28

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