8CGL

Cryo-EM structure of RNase J from Helicobacter pylori

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0001558	biological_process	regulation of cell growth
A	0003723	molecular_function	RNA binding
A	0004518	molecular_function	nuclease activity
A	0004519	molecular_function	endonuclease activity
A	0004521	molecular_function	RNA endonuclease activity
A	0004527	molecular_function	exonuclease activity
A	0004534	molecular_function	5'-3' RNA exonuclease activity
A	0005515	molecular_function	protein binding
A	0005737	cellular_component	cytoplasm
A	0006364	biological_process	rRNA processing
A	0006396	biological_process	RNA processing
A	0006397	biological_process	mRNA processing
A	0008270	molecular_function	zinc ion binding
A	0016787	molecular_function	hydrolase activity
A	0042802	molecular_function	identical protein binding
A	0042803	molecular_function	protein homodimerization activity
A	0046872	molecular_function	metal ion binding
A	0051289	biological_process	protein homotetramerization
B	0001558	biological_process	regulation of cell growth
B	0003723	molecular_function	RNA binding
B	0004518	molecular_function	nuclease activity
B	0004519	molecular_function	endonuclease activity
B	0004521	molecular_function	RNA endonuclease activity
B	0004527	molecular_function	exonuclease activity
B	0004534	molecular_function	5'-3' RNA exonuclease activity
B	0005515	molecular_function	protein binding
B	0005737	cellular_component	cytoplasm
B	0006364	biological_process	rRNA processing
B	0006396	biological_process	RNA processing
B	0006397	biological_process	mRNA processing
B	0008270	molecular_function	zinc ion binding
B	0016787	molecular_function	hydrolase activity
B	0042802	molecular_function	identical protein binding
B	0042803	molecular_function	protein homodimerization activity
B	0046872	molecular_function	metal ion binding
B	0051289	biological_process	protein homotetramerization
C	0001558	biological_process	regulation of cell growth
C	0003723	molecular_function	RNA binding
C	0004518	molecular_function	nuclease activity
C	0004519	molecular_function	endonuclease activity
C	0004521	molecular_function	RNA endonuclease activity
C	0004527	molecular_function	exonuclease activity
C	0004534	molecular_function	5'-3' RNA exonuclease activity
C	0005515	molecular_function	protein binding
C	0005737	cellular_component	cytoplasm
C	0006364	biological_process	rRNA processing
C	0006396	biological_process	RNA processing
C	0006397	biological_process	mRNA processing
C	0008270	molecular_function	zinc ion binding
C	0016787	molecular_function	hydrolase activity
C	0042802	molecular_function	identical protein binding
C	0042803	molecular_function	protein homodimerization activity
C	0046872	molecular_function	metal ion binding
C	0051289	biological_process	protein homotetramerization
D	0001558	biological_process	regulation of cell growth
D	0003723	molecular_function	RNA binding
D	0004518	molecular_function	nuclease activity
D	0004519	molecular_function	endonuclease activity
D	0004521	molecular_function	RNA endonuclease activity
D	0004527	molecular_function	exonuclease activity
D	0004534	molecular_function	5'-3' RNA exonuclease activity
D	0005515	molecular_function	protein binding
D	0005737	cellular_component	cytoplasm
D	0006364	biological_process	rRNA processing
D	0006396	biological_process	RNA processing
D	0006397	biological_process	mRNA processing
D	0008270	molecular_function	zinc ion binding
D	0016787	molecular_function	hydrolase activity
D	0042802	molecular_function	identical protein binding
D	0042803	molecular_function	protein homodimerization activity
D	0046872	molecular_function	metal ion binding
D	0051289	biological_process	protein homotetramerization

Functional Information from PROSITE/UniProt

site_id	PS01292
Number of Residues	29
Details	UPF0036 Uncharacterized protein family UPF0036 signature. HvSGHAaqeEqklMlrlikPkffLPvHGE

Chain	Residue	Details
A	HIS500-GLU528

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	44
Details	Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_01491","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI2
Number of Residues	32
Details	Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"38057323","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

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