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Protein

50S ribosomal protein L29P

Gene

rpl29p

Organism
Haloarcula marismortui (strain ATCC 43049 / DSM 3752 / JCM 8966 / VKM B-1809) (Halobacterium marismortui)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Stabilizes the tertiary rRNA structure within the 23S rRNA domain (domain I) to which it binds. Located at the polypeptide exit tunnel on the outside of the subunit.

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Ribonucleoprotein, Ribosomal protein

Keywords - Ligandi

RNA-binding, rRNA-binding

Names & Taxonomyi

Protein namesi
Recommended name:
50S ribosomal protein L29P
Alternative name(s):
Hl33
Hmal29
Gene namesi
Name:rpl29p
Ordered Locus Names:rrnAC1604
OrganismiHaloarcula marismortui (strain ATCC 43049 / DSM 3752 / JCM 8966 / VKM B-1809) (Halobacterium marismortui)
Taxonomic identifieri272569 [NCBI]
Taxonomic lineageiArchaeaEuryarchaeotaHalobacteriaHalobacterialesHalobacteriaceaeHaloarcula
Proteomesi
  • UP000001169 Componenti: Chromosome I

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemoved1 Publication
ChainiPRO_00001305082 – 7150S ribosomal protein L29PAdd BLAST70

Interactioni

Subunit structurei

Part of the 50S ribosomal subunit. Interacts with protein L23.2 Publications

Protein-protein interaction databases

STRINGi272569.rrnAC1604.

Structurei

Secondary structure

171
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi6 – 11Combined sources6
Helixi14 – 36Combined sources23
Helixi44 – 64Combined sources21

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1FFKX-ray2.40S2-71[»]
1JJ2X-ray2.40U2-71[»]
1K73X-ray3.01W2-71[»]
1K8AX-ray3.00W2-71[»]
1K9MX-ray3.00W2-71[»]
1KC8X-ray3.01W2-71[»]
1KD1X-ray3.00W2-71[»]
1KQSX-ray3.10U2-71[»]
1M1KX-ray3.20W2-71[»]
1M90X-ray2.80W2-71[»]
1N8RX-ray3.00W2-71[»]
1NJIX-ray3.00W2-71[»]
1Q7YX-ray3.20W2-71[»]
1Q81X-ray2.95W2-71[»]
1Q82X-ray2.98W2-71[»]
1Q86X-ray3.00W2-71[»]
1QVFX-ray3.10U2-71[»]
1QVGX-ray2.90U2-71[»]
1S72X-ray2.40V1-71[»]
1VQ4X-ray2.70V1-71[»]
1VQ5X-ray2.60V1-71[»]
1VQ6X-ray2.70V1-71[»]
1VQ7X-ray2.50V1-71[»]
1VQ8X-ray2.20V1-71[»]
1VQ9X-ray2.40V1-71[»]
1VQKX-ray2.30V1-71[»]
1VQLX-ray2.30V1-71[»]
1VQMX-ray2.30V1-71[»]
1VQNX-ray2.40V1-71[»]
1VQOX-ray2.20V1-71[»]
1VQPX-ray2.25V1-71[»]
1W2BX-ray3.50U2-71[»]
1YHQX-ray2.40V1-71[»]
1YI2X-ray2.65V1-71[»]
1YIJX-ray2.60V1-71[»]
1YITX-ray2.80V1-71[»]
1YJ9X-ray2.90V1-71[»]
1YJNX-ray3.00V1-71[»]
1YJWX-ray2.90V1-71[»]
2OTJX-ray2.90V1-71[»]
2OTLX-ray2.70V1-71[»]
2QA4X-ray3.00V1-71[»]
2QEXX-ray2.90V1-71[»]
3CC2X-ray2.40V1-71[»]
3CC4X-ray2.70V1-71[»]
3CC7X-ray2.70V1-71[»]
3CCEX-ray2.75V1-71[»]
3CCJX-ray2.70V1-71[»]
3CCLX-ray2.90V1-71[»]
3CCMX-ray2.55V1-71[»]
3CCQX-ray2.90V1-71[»]
3CCRX-ray3.00V1-71[»]
3CCSX-ray2.95V1-71[»]
3CCUX-ray2.80V1-71[»]
3CCVX-ray2.90V1-71[»]
3CD6X-ray2.75V1-71[»]
3CMAX-ray2.80V1-71[»]
3CMEX-ray2.95V1-71[»]
3CPWX-ray2.70U1-71[»]
3CXCX-ray3.00U2-71[»]
3G4SX-ray3.20V2-66[»]
3G6EX-ray2.70V2-66[»]
3G71X-ray2.85V2-66[»]
3I55X-ray3.11V1-71[»]
3I56X-ray2.90V1-71[»]
3OW2X-ray2.70U2-66[»]
4ADXelectron microscopy6.60V1-71[»]
4V4RX-ray5.9022-71[»]
4V4SX-ray6.7622-71[»]
4V4TX-ray6.4622-71[»]
4V9FX-ray2.40V1-71[»]
ProteinModelPortaliP10971.
SMRiP10971.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP10971.

Family & Domainsi

Sequence similaritiesi

Belongs to the ribosomal protein L29P family.Curated

Phylogenomic databases

eggNOGiarCOG00785. Archaea.
COG0255. LUCA.
HOGENOMiHOG000248755.
KOiK02904.
OMAiIQREEGD.

Family and domain databases

CDDicd00427. Ribosomal_L29_HIP. 1 hit.
Gene3Di1.10.287.310. 1 hit.
HAMAPiMF_00374. Ribosomal_L29. 1 hit.
InterProiIPR001854. Ribosomal_L29.
IPR018254. Ribosomal_L29_CS.
[Graphical view]
PfamiPF00831. Ribosomal_L29. 1 hit.
[Graphical view]
SUPFAMiSSF46561. SSF46561. 1 hit.
TIGRFAMsiTIGR00012. L29. 1 hit.
PROSITEiPS00579. RIBOSOMAL_L29. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P10971-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTVLHVQEIR DMTPAEREAE LDDLKTELLN ARAVQAAGGA PENPGRIKEL
60 70
RKAIARIKTI QGEEGDLQEN E
Length:71
Mass (Da):7,879
Last modified:January 23, 2007 - v3
Checksum:i31779CA339CC699A
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J05222 Genomic DNA. Translation: AAA86866.1.
AY596297 Genomic DNA. Translation: AAV46521.1.
X55311 Genomic DNA. Translation: CAA39015.1.
PIRiA35064. R5HS29.
T46794.
RefSeqiWP_004516964.1. NC_006396.1.

Genome annotation databases

EnsemblBacteriaiAAV46521; AAV46521; rrnAC1604.
GeneIDi3128342.
KEGGihma:rrnAC1604.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J05222 Genomic DNA. Translation: AAA86866.1.
AY596297 Genomic DNA. Translation: AAV46521.1.
X55311 Genomic DNA. Translation: CAA39015.1.
PIRiA35064. R5HS29.
T46794.
RefSeqiWP_004516964.1. NC_006396.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1FFKX-ray2.40S2-71[»]
1JJ2X-ray2.40U2-71[»]
1K73X-ray3.01W2-71[»]
1K8AX-ray3.00W2-71[»]
1K9MX-ray3.00W2-71[»]
1KC8X-ray3.01W2-71[»]
1KD1X-ray3.00W2-71[»]
1KQSX-ray3.10U2-71[»]
1M1KX-ray3.20W2-71[»]
1M90X-ray2.80W2-71[»]
1N8RX-ray3.00W2-71[»]
1NJIX-ray3.00W2-71[»]
1Q7YX-ray3.20W2-71[»]
1Q81X-ray2.95W2-71[»]
1Q82X-ray2.98W2-71[»]
1Q86X-ray3.00W2-71[»]
1QVFX-ray3.10U2-71[»]
1QVGX-ray2.90U2-71[»]
1S72X-ray2.40V1-71[»]
1VQ4X-ray2.70V1-71[»]
1VQ5X-ray2.60V1-71[»]
1VQ6X-ray2.70V1-71[»]
1VQ7X-ray2.50V1-71[»]
1VQ8X-ray2.20V1-71[»]
1VQ9X-ray2.40V1-71[»]
1VQKX-ray2.30V1-71[»]
1VQLX-ray2.30V1-71[»]
1VQMX-ray2.30V1-71[»]
1VQNX-ray2.40V1-71[»]
1VQOX-ray2.20V1-71[»]
1VQPX-ray2.25V1-71[»]
1W2BX-ray3.50U2-71[»]
1YHQX-ray2.40V1-71[»]
1YI2X-ray2.65V1-71[»]
1YIJX-ray2.60V1-71[»]
1YITX-ray2.80V1-71[»]
1YJ9X-ray2.90V1-71[»]
1YJNX-ray3.00V1-71[»]
1YJWX-ray2.90V1-71[»]
2OTJX-ray2.90V1-71[»]
2OTLX-ray2.70V1-71[»]
2QA4X-ray3.00V1-71[»]
2QEXX-ray2.90V1-71[»]
3CC2X-ray2.40V1-71[»]
3CC4X-ray2.70V1-71[»]
3CC7X-ray2.70V1-71[»]
3CCEX-ray2.75V1-71[»]
3CCJX-ray2.70V1-71[»]
3CCLX-ray2.90V1-71[»]
3CCMX-ray2.55V1-71[»]
3CCQX-ray2.90V1-71[»]
3CCRX-ray3.00V1-71[»]
3CCSX-ray2.95V1-71[»]
3CCUX-ray2.80V1-71[»]
3CCVX-ray2.90V1-71[»]
3CD6X-ray2.75V1-71[»]
3CMAX-ray2.80V1-71[»]
3CMEX-ray2.95V1-71[»]
3CPWX-ray2.70U1-71[»]
3CXCX-ray3.00U2-71[»]
3G4SX-ray3.20V2-66[»]
3G6EX-ray2.70V2-66[»]
3G71X-ray2.85V2-66[»]
3I55X-ray3.11V1-71[»]
3I56X-ray2.90V1-71[»]
3OW2X-ray2.70U2-66[»]
4ADXelectron microscopy6.60V1-71[»]
4V4RX-ray5.9022-71[»]
4V4SX-ray6.7622-71[»]
4V4TX-ray6.4622-71[»]
4V9FX-ray2.40V1-71[»]
ProteinModelPortaliP10971.
SMRiP10971.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi272569.rrnAC1604.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAV46521; AAV46521; rrnAC1604.
GeneIDi3128342.
KEGGihma:rrnAC1604.

Phylogenomic databases

eggNOGiarCOG00785. Archaea.
COG0255. LUCA.
HOGENOMiHOG000248755.
KOiK02904.
OMAiIQREEGD.

Miscellaneous databases

EvolutionaryTraceiP10971.

Family and domain databases

CDDicd00427. Ribosomal_L29_HIP. 1 hit.
Gene3Di1.10.287.310. 1 hit.
HAMAPiMF_00374. Ribosomal_L29. 1 hit.
InterProiIPR001854. Ribosomal_L29.
IPR018254. Ribosomal_L29_CS.
[Graphical view]
PfamiPF00831. Ribosomal_L29. 1 hit.
[Graphical view]
SUPFAMiSSF46561. SSF46561. 1 hit.
TIGRFAMsiTIGR00012. L29. 1 hit.
PROSITEiPS00579. RIBOSOMAL_L29. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiRL29_HALMA
AccessioniPrimary (citable) accession number: P10971
Secondary accession number(s): P22526, Q5V1T1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: January 23, 2007
Last modified: November 2, 2016
This is version 124 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. Ribosomal proteins
    Ribosomal proteins families and list of entries
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.