Reviewed, UniProtKB/Swiss-Prot O52704 (RL1_METTL)

Names and origin

Protein names

Recommended name:
    50S ribosomal protein L1P

Gene names

Name:

rpl1p

Organism

Methanococcus thermolithotrophicus

Taxonomic identifier

2186 [NCBI]

Taxonomic lineage

Archaea › Euryarchaeota › Methanococci › Methanococcales › Methanococcaceae › Methanothermococcus

Protein attributes

Sequence length	213 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Probably involved in E site tRNA release By similarity. Binds directly to 23S rRNA. Protein L1 is also a translational repressor protein, it controls the translation of its operon by binding to its mRNA By similarity.
Subunit structure	Part of the 50S ribosomal subunit. HAMAP MF_01318
Sequence similarities	Belongs to the ribosomal protein L1P family.

Ontologies

Keywords
Biological process	Translation regulation
Ligand	RNA-binding rRNA-binding tRNA-binding
Molecular function	Repressor Ribonucleoprotein Ribosomal protein
Technical term	3D-structure
Gene Ontology (GO)
Biological process	RNA processing Inferred from electronic annotation. Source: InterPro regulation of translation Inferred from electronic annotation. Source: UniProtKB-KW translation Inferred from electronic annotation. Source: HAMAP
Cellular component	ribosome Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	rRNA binding Inferred from electronic annotation. Source: HAMAP structural constituent of ribosome Inferred from electronic annotation. Source: InterPro tRNA binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 213

213

50S ribosomal protein L1P HAMAP MF_01318

PRO_0000125802

Secondary structure

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213

Helix Strand Turn

Details...

Helix

3 – 15

13

Beta strand

25 – 32

8

Helix

40 – 42

3

Beta strand

45 – 49

5

Beta strand

60 – 63

4

Helix

67 – 74

8

Beta strand

78 – 80

3

Helix

82 – 90

9

Helix

92 – 101

10

Beta strand

103 – 108

6

Helix

109 – 111

3

Helix

112 – 117

6

Helix

120 – 126

7

Beta strand

131 – 133

3

Helix

139 – 147

9

Beta strand

149 – 153

5

Beta strand

157 – 166

10

Helix

171 – 188

18

Beta strand

189 – 191

3

Helix

192 – 195

4

Beta strand

196 – 202

7

Sequences

	Sequence		Length	Mass (Da)
	O52704-1 [UniParc]. Last modified June 1, 1998. Version 1. Checksum: C435C5064300E5A8	FASTA	213	23,794
	10 20 30 40 50 60 MDRENILKAV KEARSLAKPR NFTQSLDLII NLKELDLSRP ENRLKEQVVL PNGRGKEPKI 70 80 90 100 110 120 AVIAKGDLAA QAEEMGLTVI RQDELEELGK NKKMAKKIAN EHDFFIAQAD MMPLVGKTLG 130 140 150 160 170 180 PVLGPRGKMP QPVPANANLT PLVERLKKTV LINTRDKPLF HVLVGNEKMS DEELAENIEA 190 200 210 ILNTVSRKYE KGLYHVKSAY TKLTMGPPAQ IEK

References

[1]	Linhart A., Piendl W. Submitted (JAN-1998) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"Interaction of ribosomal L1 proteins from mesophilic and thermophilic Archaea and Bacteria with specific L1-binding sites on 23S rRNA and mRNA." Koehrer C., Mayer C., Neumair O., Groebner P., Piendl W. Eur. J. Biochem. 256:97-105(1998) [PubMed: 9746351] [Abstract] Cited for: BINDING TO ENDOGENOUS 23S RRNA, TO METHANOCOCCUS VANNIELII L1 MRNA.
[3]	"Structure of ribosomal protein L1 from Methanococcus thermolithotrophicus. Functionally important structural invariants on the L1 surface." Nevskaya N., Tishchenko S., Paveliev M., Smolinskaya Y., Fedorov R., Piendl W., Nakamura Y., Toyoda T., Garber M.B., Nikonov S. Acta Crystallogr. D 58:1023-1029(2002) [PubMed: 12037305] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS).

Cross-references

Sequence databases

EMBLGenBankDDBJ

AF044919 Genomic DNA. Translation: AAC64510.1.

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1DWU	X-ray	2.80	A/B	1-213	[»]

ModBase

Search...

Family and domain databases

HAMAP

MF_01318.
[Tree]

InterPro

IPR002143. Ribosomal_L1.
IPR016094. Ribosomal_L1_2-a/b-sand.
[Graphical view]

Gene3D

G3DSA:3.30.190.20. Ribosomal_L1_2-a/b-sand. 1 hit.

Pfam

PF00687. Ribosomal_L1. 1 hit.
[Graphical view]

PIRSF

PIRSF002155. Ribosomal_L1. 1 hit.

ProDom

PD001314. Ribosomal_L1. 1 hit.
[Graphical view] [Entries sharing at least one domain]

PROSITE

PS01199. RIBOSOMAL_L1. 1 hit.
[Graphical view]

ProtoNet

Search...

Entry information

Entry name

RL1_METTL

Accession

Primary (citable) accession number: O52704

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 15, 1998
Last sequence update:	June 1, 1998
Last modified:	June 16, 2009
This is version 51 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)