5LM7

Crystal structure of the lambda N-Nus factor complex

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000166	molecular_function	nucleotide binding
A	0003676	molecular_function	nucleic acid binding
A	0003700	molecular_function	DNA-binding transcription factor activity
A	0003723	molecular_function	RNA binding
A	0006353	biological_process	DNA-templated transcription termination
A	0031554	biological_process	regulation of termination of DNA-templated transcription
A	0031564	biological_process	transcription antitermination
B	0003723	molecular_function	RNA binding
B	0005515	molecular_function	protein binding
B	0005829	cellular_component	cytosol
B	0006353	biological_process	DNA-templated transcription termination
B	0006355	biological_process	regulation of DNA-templated transcription
B	0008023	cellular_component	transcription elongation factor complex
B	0031564	biological_process	transcription antitermination
B	0032784	biological_process	regulation of DNA-templated transcription elongation
B	0042254	biological_process	ribosome biogenesis
C	0000166	molecular_function	nucleotide binding
C	0003676	molecular_function	nucleic acid binding
C	0003700	molecular_function	DNA-binding transcription factor activity
C	0003723	molecular_function	RNA binding
C	0006353	biological_process	DNA-templated transcription termination
C	0031554	biological_process	regulation of termination of DNA-templated transcription
C	0031564	biological_process	transcription antitermination
D	0003723	molecular_function	RNA binding
D	0005515	molecular_function	protein binding
D	0005829	cellular_component	cytosol
D	0006353	biological_process	DNA-templated transcription termination
D	0006355	biological_process	regulation of DNA-templated transcription
D	0008023	cellular_component	transcription elongation factor complex
D	0031564	biological_process	transcription antitermination
D	0032784	biological_process	regulation of DNA-templated transcription elongation
D	0042254	biological_process	ribosome biogenesis
E	0000049	molecular_function	tRNA binding
E	0001072	molecular_function	transcription antitermination factor activity, RNA binding
E	0002181	biological_process	cytoplasmic translation
E	0003723	molecular_function	RNA binding
E	0003735	molecular_function	structural constituent of ribosome
E	0005515	molecular_function	protein binding
E	0005737	cellular_component	cytoplasm
E	0005829	cellular_component	cytosol
E	0005840	cellular_component	ribosome
E	0006412	biological_process	translation
E	0008023	cellular_component	transcription elongation factor complex
E	0015935	cellular_component	small ribosomal subunit
E	0022627	cellular_component	cytosolic small ribosomal subunit
E	0031564	biological_process	transcription antitermination
E	0032784	biological_process	regulation of DNA-templated transcription elongation
E	0042254	biological_process	ribosome biogenesis
E	1990904	cellular_component	ribonucleoprotein complex
J	0000049	molecular_function	tRNA binding
J	0001072	molecular_function	transcription antitermination factor activity, RNA binding
J	0002181	biological_process	cytoplasmic translation
J	0003723	molecular_function	RNA binding
J	0003735	molecular_function	structural constituent of ribosome
J	0005515	molecular_function	protein binding
J	0005737	cellular_component	cytoplasm
J	0005829	cellular_component	cytosol
J	0005840	cellular_component	ribosome
J	0006412	biological_process	translation
J	0008023	cellular_component	transcription elongation factor complex
J	0015935	cellular_component	small ribosomal subunit
J	0022627	cellular_component	cytosolic small ribosomal subunit
J	0031564	biological_process	transcription antitermination
J	0032784	biological_process	regulation of DNA-templated transcription elongation
J	0042254	biological_process	ribosome biogenesis
J	1990904	cellular_component	ribonucleoprotein complex

Functional Information from PROSITE/UniProt

site_id	PS00361
Number of Residues	16
Details	RIBOSOMAL_S10 Ribosomal protein S10 signature. AkrtGAqvrGPIpLPT

Chain	Residue	Details
J	ALA29-THR44

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	130
Details	Domain: {"description":"S1 motif","evidences":[{"source":"HAMAP-Rule","id":"MF_00945","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI2
Number of Residues	126
Details	Domain: {"description":"KH 1","evidences":[{"source":"HAMAP-Rule","id":"MF_00945","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI3
Number of Residues	132
Details	Domain: {"description":"KH","evidences":[{"source":"HAMAP-Rule","id":"MF_00945","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI4
Number of Residues	100
Details	Repeat: {"description":"1"}

Chain

Residue

Details

---

site_id	SWS_FT_FI5
Number of Residues	272
Details	Region: {"description":"N-terminal domain (NTD) interacts with RNAP","evidences":[{"source":"PubMed","id":"21922055","evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI6
Number of Residues	81
Details	Region: {"description":"Acidic repeat 1 (AR1)","evidences":[{"source":"PubMed","id":"21922055","evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

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