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P14121 (RL30_HALMA) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 110. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
50S ribosomal protein L30P
Alternative name(s):
Hl16
Hl20
Hmal30
Gene names
Name:rpl30p
Ordered Locus Names:rrnAC1591
OrganismHaloarcula marismortui (strain ATCC 43049 / DSM 3752 / JCM 8966 / VKM B-1809) (Halobacterium marismortui) [Complete proteome] [HAMAP]
Taxonomic identifier272569 [NCBI]
Taxonomic lineageArchaeaEuryarchaeotaHalobacteriaHalobacterialesHalobacteriaceaeHaloarcula

Protein attributes

Sequence length154 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

This is one of 5 proteins that mediate the attachment of the 5S rRNA onto the large ribosomal subunit, stabilizing the orientation of adjacent RNA domains. HAMAP-Rule MF_01371

Subunit structure

Part of the 50S ribosomal subunit. Binds 5S rRNA. Ref.5 Ref.6 Ref.7 Ref.8 Ref.9 Ref.10 Ref.11 Ref.12 Ref.13

Sequence similarities

Belongs to the ribosomal protein L30P family.

Ontologies

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 15415450S ribosomal protein L30P HAMAP-Rule MF_01371
PRO_0000104622

Experimental info

Sequence conflict831W → L AA sequence Ref.1
Sequence conflict1481Missing AA sequence Ref.1

Secondary structure

............................... 154
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P14121 [UniParc].

Last modified August 1, 1992. Version 2.
Checksum: ED673F036E974C14

FASTA15417,042
        10         20         30         40         50         60 
MHALVQLRGE VNMHTDIQDT LEMLNIHHVN HCTLVPETDA YRGMVAKVND FVAFGEPSQE 

        70         80         90        100        110        120 
TLETVLATRA EPLEGDADVD DEWVAEHTDY DDISGLAFAL LSEETTLREQ GLSPTLRLHP 

       130        140        150 
PRGGHDGVKH PVKEGGQLGK HDTEGIDDLL EAMR 

« Hide

References

« Hide 'large scale' references
[1]"Primary structures of five ribosomal proteins from the archaebacterium Halobacterium marismortui and their structural relationships to eubacterial and eukaryotic ribosomal proteins."
Hatakeyama T., Kaufmann F., Schroeter B., Hatakeyama T.
Eur. J. Biochem. 185:685-693(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE.
[2]"Organization and nucleotide sequence of ten ribosomal protein genes from the region equivalent to the spectinomycin operon in the archaebacterium Halobacterium marismortui."
Scholzen T., Arndt E.
Mol. Gen. Genet. 228:70-80(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]"Genome sequence of Haloarcula marismortui: a halophilic archaeon from the Dead Sea."
Baliga N.S., Bonneau R., Facciotti M.T., Pan M., Glusman G., Deutsch E.W., Shannon P., Chiu Y., Weng R.S., Gan R.R., Hung P., Date S.V., Marcotte E., Hood L., Ng W.V.
Genome Res. 14:2221-2234(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 43049 / DSM 3752 / JCM 8966 / VKM B-1809.
[4]"Extended N-terminal sequencing of proteins of archaebacterial ribosomes blotted from two-dimensional gels onto glass fiber and poly(vinylidene difluoride) membrane."
Walsh M.J., McDougall J., Wittmann-Liebold B.
Biochemistry 27:6867-6876(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 1-30.
[5]"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.
[6]"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.
[7]"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.
[8]"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.
[9]"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.
[10]"Structural insights into peptide bond formation."
Hansen J.L., Schmeing T.M., Moore P.B., Steitz T.A.
Proc. Natl. Acad. Sci. U.S.A. 99:11670-11675(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF THE 50S SUBUNIT.
Strain: ATCC 43049 / DSM 3752 / JCM 8966 / VKM B-1809.
[11]"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.
[12]"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.
[13]"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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X58395 Genomic DNA. Translation: CAA41292.1.
AY596297 Genomic DNA. Translation: AAV46509.1.
PIRR5HS30. S16543.
RefSeqYP_136215.1. NC_006396.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1FFKX-ray2.40T1-154[»]
1JJ2X-ray2.40V1-154[»]
1K73X-ray3.01X1-154[»]
1K8AX-ray3.00X1-154[»]
1K9MX-ray3.00X1-154[»]
1KC8X-ray3.01X1-154[»]
1KD1X-ray3.00X1-154[»]
1KQSX-ray3.10V1-154[»]
1M1KX-ray3.20X1-154[»]
1M90X-ray2.80X1-154[»]
1N8RX-ray3.00X1-154[»]
1NJIX-ray3.00X1-154[»]
1Q7YX-ray3.20X1-154[»]
1Q81X-ray2.95X1-154[»]
1Q82X-ray2.98X1-154[»]
1Q86X-ray3.00X1-154[»]
1QVFX-ray3.10V1-154[»]
1QVGX-ray2.90V1-154[»]
1S72X-ray2.40W1-154[»]
1VQ4X-ray2.70W1-154[»]
1VQ5X-ray2.60W1-154[»]
1VQ6X-ray2.70W1-154[»]
1VQ7X-ray2.50W1-154[»]
1VQ8X-ray2.20W1-154[»]
1VQ9X-ray2.40W1-154[»]
1VQKX-ray2.30W1-154[»]
1VQLX-ray2.30W1-154[»]
1VQMX-ray2.30W1-154[»]
1VQNX-ray2.40W1-154[»]
1VQOX-ray2.20W1-154[»]
1VQPX-ray2.25W1-154[»]
1W2BX-ray3.50V1-154[»]
1YHQX-ray2.40W1-154[»]
1YI2X-ray2.65W1-154[»]
1YIJX-ray2.60W1-154[»]
1YITX-ray2.80W1-154[»]
1YJ9X-ray2.90W1-154[»]
1YJNX-ray3.00W1-154[»]
1YJWX-ray2.90W1-154[»]
2OTJX-ray2.90W1-154[»]
2OTLX-ray2.70W1-154[»]
2QA4X-ray3.00W1-154[»]
2QEXX-ray2.90W1-154[»]
3CC2X-ray2.40W1-154[»]
3CC4X-ray2.70W1-154[»]
3CC7X-ray2.70W1-154[»]
3CCEX-ray2.75W1-154[»]
3CCJX-ray2.70W1-154[»]
3CCLX-ray2.90W1-154[»]
3CCMX-ray2.55W1-154[»]
3CCQX-ray2.90W1-154[»]
3CCRX-ray3.00W1-154[»]
3CCSX-ray2.95W1-154[»]
3CCUX-ray2.80W1-154[»]
3CCVX-ray2.90W1-154[»]
3CD6X-ray2.75W1-154[»]
3CMAX-ray2.80W1-154[»]
3CMEX-ray2.95W1-154[»]
3CPWX-ray2.70V1-154[»]
3CXCX-ray3.00V1-154[»]
3G4SX-ray3.20W1-154[»]
3G6EX-ray2.70W1-154[»]
3G71X-ray2.85W1-154[»]
3I55X-ray3.11W1-154[»]
3I56X-ray2.90W1-154[»]
3OW2X-ray2.70V1-154[»]
4HUBX-ray2.40W1-154[»]
ProteinModelPortalP14121.
SMRP14121. Positions 1-154.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING272569.rrnAC1591.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAV46509; AAV46509; rrnAC1591.
GeneID3127531.
KEGGhma:rrnAC1591.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG1841.
HOGENOMHOG000170918.
KOK02907.
OMAKEGGQLG.
ProtClustDBPRK06049.

Enzyme and pathway databases

BioCycHMAR272569:GJDH-1447-MONOMER.

Family and domain databases

Gene3D1.10.15.30. 1 hit.
3.30.1390.20. 2 hits.
HAMAPMF_01371_A. Ribosomal_L30_A.
InterProIPR005997. Ribosomal_L30_arc.
IPR023106. Ribosomal_L30_central_dom_arc.
IPR018038. Ribosomal_L30_CS.
IPR016082. Ribosomal_L30_ferredoxin-like.
[Graphical view]
PfamPF00327. Ribosomal_L30. 1 hit.
[Graphical view]
SUPFAMSSF55129. SSF55129. 1 hit.
TIGRFAMsTIGR01309. L30P_arch. 1 hit.
PROSITEPS00634. RIBOSOMAL_L30. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP14121.

Entry information

Entry nameRL30_HALMA
AccessionPrimary (citable) accession number: P14121
Secondary accession number(s): Q5V1U3
Entry history
Integrated into UniProtKB/Swiss-Prot: January 1, 1990
Last sequence update: August 1, 1992
Last modified: February 19, 2014
This is version 110 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Ribosomal proteins

Ribosomal proteins families and list of entries

PDB cross-references

Index of Protein Data Bank (PDB) cross-references