Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

P20279

- RL3_HALMA

UniProt

P20279 - RL3_HALMA

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

50S ribosomal protein L3

Gene

rpl3

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

Functioni

One of the primary rRNA binding proteins, it binds directly near the 3'-end of the 23S rRNA, where it nucleates assembly of the 50S subunit.By similarity

GO - Molecular functioni

  1. rRNA binding Source: UniProtKB-HAMAP
  2. structural constituent of ribosome Source: InterPro

GO - Biological processi

  1. translation Source: UniProtKB-HAMAP
Complete GO annotation...

Keywords - Molecular functioni

Ribonucleoprotein, Ribosomal protein

Keywords - Ligandi

RNA-binding, rRNA-binding

Enzyme and pathway databases

BioCyciHMAR272569:GJDH-1467-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
50S ribosomal protein L3
Alternative name(s):
Hl1
Hmal3
Gene namesi
Name:rpl3
Ordered Locus Names:rrnAC1611
OrganismiHaloarcula marismortui (strain ATCC 43049 / DSM 3752 / JCM 8966 / VKM B-1809) (Halobacterium marismortui)
Taxonomic identifieri272569 [NCBI]
Taxonomic lineageiArchaeaEuryarchaeotaHalobacteriaHalobacterialesHalobacteriaceaeHaloarcula
ProteomesiUP000001169: Chromosome I

Subcellular locationi

GO - Cellular componenti

  1. ribosome Source: UniProtKB-KW
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed
Chaini2 – 33833750S ribosomal protein L3PRO_0000077207Add
BLAST

Interactioni

Subunit structurei

Part of the 50S ribosomal subunit. Forms a cluster with proteins L14 and L24e. Interacts weakly with protein L13.2 Publications

Protein-protein interaction databases

STRINGi272569.rrnAC1611.

Structurei

Secondary structure

1
338
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi12 – 143Combined sources
Beta strandi35 – 395Combined sources
Beta strandi42 – 5514Combined sources
Beta strandi59 – 613Combined sources
Turni62 – 654Combined sources
Beta strandi66 – 7611Combined sources
Beta strandi80 – 9112Combined sources
Beta strandi94 – 1029Combined sources
Helixi110 – 1123Combined sources
Helixi122 – 13514Combined sources
Beta strandi138 – 1469Combined sources
Helixi149 – 1513Combined sources
Beta strandi153 – 1553Combined sources
Beta strandi162 – 1687Combined sources
Helixi172 – 18514Combined sources
Beta strandi187 – 1893Combined sources
Turni192 – 1943Combined sources
Beta strandi200 – 2067Combined sources
Beta strandi209 – 2135Combined sources
Helixi215 – 2195Combined sources
Helixi226 – 2294Combined sources
Beta strandi230 – 2323Combined sources
Beta strandi234 – 2363Combined sources
Beta strandi243 – 2475Combined sources
Beta strandi250 – 2523Combined sources
Beta strandi256 – 2594Combined sources
Beta strandi262 – 27918Combined sources
Turni286 – 2883Combined sources
Beta strandi293 – 3008Combined sources
Beta strandi309 – 3146Combined sources
Beta strandi328 – 3314Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1FFKX-ray2.40B2-338[»]
1JJ2X-ray2.40B2-338[»]
1K73X-ray3.01D2-338[»]
1K8AX-ray3.00D2-338[»]
1K9MX-ray3.00D2-338[»]
1KC8X-ray3.01D2-338[»]
1KD1X-ray3.00D2-338[»]
1KQSX-ray3.10B2-338[»]
1M1KX-ray3.20D2-338[»]
1M90X-ray2.80D2-338[»]
1ML5electron microscopy14.00e2-311[»]
e312-338[»]
1N8RX-ray3.00D2-338[»]
1NJIX-ray3.00D2-338[»]
1Q7YX-ray3.20D2-338[»]
1Q81X-ray2.95D2-338[»]
1Q82X-ray2.98D2-338[»]
1Q86X-ray3.00D2-338[»]
1QVFX-ray3.10B2-338[»]
1QVGX-ray2.90B2-338[»]
1S72X-ray2.40B1-338[»]
1VQ4X-ray2.70B1-338[»]
1VQ5X-ray2.60B1-338[»]
1VQ6X-ray2.70B1-338[»]
1VQ7X-ray2.50B1-338[»]
1VQ8X-ray2.20B1-338[»]
1VQ9X-ray2.40B1-338[»]
1VQKX-ray2.30B1-338[»]
1VQLX-ray2.30B1-338[»]
1VQMX-ray2.30B1-338[»]
1VQNX-ray2.40B1-338[»]
1VQOX-ray2.20B1-338[»]
1VQPX-ray2.25B1-338[»]
1W2BX-ray3.50B2-338[»]
1YHQX-ray2.40B1-338[»]
1YI2X-ray2.65B1-338[»]
1YIJX-ray2.60B1-338[»]
1YITX-ray2.80B1-338[»]
1YJ9X-ray2.90B1-338[»]
1YJNX-ray3.00B1-338[»]
1YJWX-ray2.90B1-338[»]
2B9PX-ray6.46E2-338[»]
2OTJX-ray2.90B1-338[»]
2OTLX-ray2.70B2-338[»]
2QA4X-ray3.00B1-338[»]
2QEXX-ray2.90B1-338[»]
3CC2X-ray2.40B1-338[»]
3CC4X-ray2.70B1-338[»]
3CC7X-ray2.70B1-338[»]
3CCEX-ray2.75B1-338[»]
3CCJX-ray2.70B1-338[»]
3CCLX-ray2.90B1-338[»]
3CCMX-ray2.55B1-338[»]
3CCQX-ray2.90B1-338[»]
3CCRX-ray3.00B1-338[»]
3CCSX-ray2.95B1-338[»]
3CCUX-ray2.80B1-338[»]
3CCVX-ray2.90B1-338[»]
3CD6X-ray2.75B1-338[»]
3CMAX-ray2.80B1-338[»]
3CMEX-ray2.95B1-338[»]
3CPWX-ray2.70B1-338[»]
3CXCX-ray3.00B2-338[»]
3G4SX-ray3.20B2-338[»]
3G6EX-ray2.70B2-338[»]
3G71X-ray2.85B2-338[»]
3I55X-ray3.11B1-338[»]
3I56X-ray2.90B1-338[»]
3OW2X-ray2.70B2-338[»]
4ADXelectron microscopy6.60B1-338[»]
4HUBX-ray2.40B1-338[»]
ProteinModelPortaliP20279.
SMRiP20279. Positions 2-338.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP20279.

Family & Domainsi

Sequence similaritiesi

Belongs to the ribosomal protein L3P family.Curated

Phylogenomic databases

eggNOGiCOG0087.
HOGENOMiHOG000107320.
KOiK02906.
OMAiTYISTES.

Family and domain databases

HAMAPiMF_01325_A. Ribosomal_L3_A.
InterProiIPR000597. Ribosomal_L3.
IPR019928. Ribosomal_L3_arc.
IPR019926. Ribosomal_L3_CS.
IPR009000. Transl_B-barrel.
[Graphical view]
PfamiPF00297. Ribosomal_L3. 1 hit.
[Graphical view]
SUPFAMiSSF50447. SSF50447. 1 hit.
TIGRFAMsiTIGR03626. L3_arch. 1 hit.
PROSITEiPS00474. RIBOSOMAL_L3. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P20279-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MPQPSRPRKG SLGFGPRKRS TSETPRFNSW PSDDGQPGVQ GFAGYKAGMT
60 70 80 90 100
HVVLVNDEPN SPREGMEETV PVTVIETPPM RAVALRAYED TPYGQRPLTE
110 120 130 140 150
VWTDEFHSEL DRTLDVPEDH DPDAAEEQIR DAHEAGDLGD LRLITHTVPD
160 170 180 190 200
AVPSVPKKKP DVMETRVGGG SVSDRLDHAL DIVEDGGEHA MNDIFRAGEY
210 220 230 240 250
ADVAGVTKGK GTQGPVKRWG VQKRKGKHAR QGWRRRIGNL GPWNPSRVRS
260 270 280 290 300
TVPQQGQTGY HQRTELNKRL IDIGEGDEPT VDGGFVNYGE VDGPYTLVKG
310 320 330
SVPGPDKRLV RFRPAVRPND QPRLDPEVRY VSNESNQG
Length:338
Mass (Da):37,341
Last modified:January 23, 2007 - v5
Checksum:i996D3BE503F4DBD4
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti311 – 3111R → P in AAA86859. (PubMed:2406244)Curated
Sequence conflicti312 – 3121F → FF AA sequence (PubMed:2406244)Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J05222 Genomic DNA. Translation: AAA86859.1.
AY596297 Genomic DNA. Translation: AAV46528.1.
PIRiC35063. R5HS3L.
RefSeqiYP_136234.1. NC_006396.1.

Genome annotation databases

EnsemblBacteriaiAAV46528; AAV46528; rrnAC1611.
GeneIDi3128366.
KEGGihma:rrnAC1611.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J05222 Genomic DNA. Translation: AAA86859.1 .
AY596297 Genomic DNA. Translation: AAV46528.1 .
PIRi C35063. R5HS3L.
RefSeqi YP_136234.1. NC_006396.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1FFK X-ray 2.40 B 2-338 [» ]
1JJ2 X-ray 2.40 B 2-338 [» ]
1K73 X-ray 3.01 D 2-338 [» ]
1K8A X-ray 3.00 D 2-338 [» ]
1K9M X-ray 3.00 D 2-338 [» ]
1KC8 X-ray 3.01 D 2-338 [» ]
1KD1 X-ray 3.00 D 2-338 [» ]
1KQS X-ray 3.10 B 2-338 [» ]
1M1K X-ray 3.20 D 2-338 [» ]
1M90 X-ray 2.80 D 2-338 [» ]
1ML5 electron microscopy 14.00 e 2-311 [» ]
e 312-338 [» ]
1N8R X-ray 3.00 D 2-338 [» ]
1NJI X-ray 3.00 D 2-338 [» ]
1Q7Y X-ray 3.20 D 2-338 [» ]
1Q81 X-ray 2.95 D 2-338 [» ]
1Q82 X-ray 2.98 D 2-338 [» ]
1Q86 X-ray 3.00 D 2-338 [» ]
1QVF X-ray 3.10 B 2-338 [» ]
1QVG X-ray 2.90 B 2-338 [» ]
1S72 X-ray 2.40 B 1-338 [» ]
1VQ4 X-ray 2.70 B 1-338 [» ]
1VQ5 X-ray 2.60 B 1-338 [» ]
1VQ6 X-ray 2.70 B 1-338 [» ]
1VQ7 X-ray 2.50 B 1-338 [» ]
1VQ8 X-ray 2.20 B 1-338 [» ]
1VQ9 X-ray 2.40 B 1-338 [» ]
1VQK X-ray 2.30 B 1-338 [» ]
1VQL X-ray 2.30 B 1-338 [» ]
1VQM X-ray 2.30 B 1-338 [» ]
1VQN X-ray 2.40 B 1-338 [» ]
1VQO X-ray 2.20 B 1-338 [» ]
1VQP X-ray 2.25 B 1-338 [» ]
1W2B X-ray 3.50 B 2-338 [» ]
1YHQ X-ray 2.40 B 1-338 [» ]
1YI2 X-ray 2.65 B 1-338 [» ]
1YIJ X-ray 2.60 B 1-338 [» ]
1YIT X-ray 2.80 B 1-338 [» ]
1YJ9 X-ray 2.90 B 1-338 [» ]
1YJN X-ray 3.00 B 1-338 [» ]
1YJW X-ray 2.90 B 1-338 [» ]
2B9P X-ray 6.46 E 2-338 [» ]
2OTJ X-ray 2.90 B 1-338 [» ]
2OTL X-ray 2.70 B 2-338 [» ]
2QA4 X-ray 3.00 B 1-338 [» ]
2QEX X-ray 2.90 B 1-338 [» ]
3CC2 X-ray 2.40 B 1-338 [» ]
3CC4 X-ray 2.70 B 1-338 [» ]
3CC7 X-ray 2.70 B 1-338 [» ]
3CCE X-ray 2.75 B 1-338 [» ]
3CCJ X-ray 2.70 B 1-338 [» ]
3CCL X-ray 2.90 B 1-338 [» ]
3CCM X-ray 2.55 B 1-338 [» ]
3CCQ X-ray 2.90 B 1-338 [» ]
3CCR X-ray 3.00 B 1-338 [» ]
3CCS X-ray 2.95 B 1-338 [» ]
3CCU X-ray 2.80 B 1-338 [» ]
3CCV X-ray 2.90 B 1-338 [» ]
3CD6 X-ray 2.75 B 1-338 [» ]
3CMA X-ray 2.80 B 1-338 [» ]
3CME X-ray 2.95 B 1-338 [» ]
3CPW X-ray 2.70 B 1-338 [» ]
3CXC X-ray 3.00 B 2-338 [» ]
3G4S X-ray 3.20 B 2-338 [» ]
3G6E X-ray 2.70 B 2-338 [» ]
3G71 X-ray 2.85 B 2-338 [» ]
3I55 X-ray 3.11 B 1-338 [» ]
3I56 X-ray 2.90 B 1-338 [» ]
3OW2 X-ray 2.70 B 2-338 [» ]
4ADX electron microscopy 6.60 B 1-338 [» ]
4HUB X-ray 2.40 B 1-338 [» ]
ProteinModelPortali P20279.
SMRi P20279. Positions 2-338.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 272569.rrnAC1611.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAV46528 ; AAV46528 ; rrnAC1611 .
GeneIDi 3128366.
KEGGi hma:rrnAC1611.

Phylogenomic databases

eggNOGi COG0087.
HOGENOMi HOG000107320.
KOi K02906.
OMAi TYISTES.

Enzyme and pathway databases

BioCyci HMAR272569:GJDH-1467-MONOMER.

Miscellaneous databases

EvolutionaryTracei P20279.

Family and domain databases

HAMAPi MF_01325_A. Ribosomal_L3_A.
InterProi IPR000597. Ribosomal_L3.
IPR019928. Ribosomal_L3_arc.
IPR019926. Ribosomal_L3_CS.
IPR009000. Transl_B-barrel.
[Graphical view ]
Pfami PF00297. Ribosomal_L3. 1 hit.
[Graphical view ]
SUPFAMi SSF50447. SSF50447. 1 hit.
TIGRFAMsi TIGR03626. L3_arch. 1 hit.
PROSITEi PS00474. RIBOSOMAL_L3. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Organization and nucleotide sequence of a gene cluster coding for eight ribosomal proteins in the archaebacterium Halobacterium marismortui."
    Arndt E., Kroemer W., Hatakeyama T.
    J. Biol. Chem. 265:3034-3039(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 43049 / DSM 3752 / JCM 8966 / VKM B-1809.
  3. "The complete atomic structure of the large ribosomal subunit at 2.4 A resolution."
    Ban N., Nissen P., Hansen J., Moore P.B., Steitz T.A.
    Science 289:905-920(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF THE 50S SUBUNIT.
    Strain: ATCC 43049 / DSM 3752 / JCM 8966 / VKM B-1809.
  4. "The structural basis of ribosome activity in peptide bond synthesis."
    Nissen P., Hansen J., Ban N., Moore P.B., Steitz T.A.
    Science 289:920-930(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF THE 50S SUBUNIT.
    Strain: ATCC 43049 / DSM 3752 / JCM 8966 / VKM B-1809.
  5. "A pre-translocational intermediate in protein synthesis observed in crystals of enzymatically active 50S subunits."
    Schmeing T.M., Seila A.C., Hansen J.L., Freeborn B., Soukup J.K., Scaringe S.A., Strobel S.A., Moore P.B., Steitz T.A.
    Nat. Struct. Biol. 9:225-230(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (3.1 ANGSTROMS) OF THE 50S SUBUNIT.
    Strain: ATCC 43049 / DSM 3752 / JCM 8966 / VKM B-1809.
  6. "The kink-turn: a new RNA secondary structure motif."
    Klein D.J., Schmeing T.M., Moore P.B., Steitz T.A.
    EMBO J. 20:4214-4221(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF THE 50S SUBUNIT.
    Strain: ATCC 43049 / DSM 3752 / JCM 8966 / VKM B-1809.
  7. "The structures of four macrolide antibiotics bound to the large ribosomal subunit."
    Hansen J.L., Ippolito J.A., Ban N., Nissen P., Moore P.B., Steitz T.A.
    Mol. Cell 10:117-128(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF THE 50S SUBUNIT IN COMPLEX WITH FOUR MACROLIDE ANTIBIOTICS.
    Strain: ATCC 43049 / DSM 3752 / JCM 8966 / VKM B-1809.
  8. Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF THE 50S SUBUNIT.
    Strain: ATCC 43049 / DSM 3752 / JCM 8966 / VKM B-1809.
  9. "Structures of five antibiotics bound at the peptidyl transferase center of the large ribosomal subunit."
    Hansen J.L., Moore P.B., Steitz T.A.
    J. Mol. Biol. 330:1061-1075(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF THE 50S SUBUNIT IN COMPLEX WITH FIVE ANTIBIOTICS AT THE PEPTIDYL TRANSFERASE CENTER.
    Strain: ATCC 43049 / DSM 3752 / JCM 8966 / VKM B-1809.
  10. "Structures of deacylated tRNA mimics bound to the E site of the large ribosomal subunit."
    Schmeing T.M., Moore P.B., Steitz T.A.
    RNA 9:1345-1352(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF THE 50S SUBUNIT WITH TWO DIFFERENT E SITE SUBSTRATES.
  11. "Revisiting the Haloarcula marismortui 50S ribosomal subunit model."
    Gabdulkhakov A., Nikonov S., Garber M.
    Acta Crystallogr. D 69:997-1004(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF THE 50S SUBUNIT.

Entry informationi

Entry nameiRL3_HALMA
AccessioniPrimary (citable) accession number: P20279
Secondary accession number(s): Q5V1S4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1991
Last sequence update: January 23, 2007
Last modified: November 26, 2014
This is version 110 of the entry and version 5 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

External Data

Dasty 3