Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

P12736 (RL32_HALMA) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 113. 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 L32e
Alternative name(s):
Hl5
Gene names
Name:rpl32e
Ordered Locus Names:rrnAC1595
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 length241 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Binds to the 23S rRNA. HAMAP-Rule MF_00810

Subunit structure

Part of the 50S ribosomal subunit. Interacts weakly with protein L15. Ref.5 Ref.6 Ref.7 Ref.8 Ref.9 Ref.10 Ref.11 Ref.12

Sequence similarities

Belongs to the ribosomal protein L32e family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.3
Chain2 – 24124050S ribosomal protein L32e HAMAP-Rule MF_00810
PRO_0000131148

Experimental info

Sequence conflict261S → R AA sequence Ref.3
Sequence conflict311Missing AA sequence Ref.3
Sequence conflict110 – 1112LS → SL AA sequence Ref.3

Secondary structure

............................. 241
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P12736 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: F4FFF58DE34B3711

FASTA24126,416
        10         20         30         40         50         60 
MADNEEDVEA EEEYTELTDI SGVGPSKAES LREAGFESVE DVRGADQSAL ADVSGIGNAL 

        70         80         90        100        110        120 
AARIKADVGG LEVESETEAE VEEEGGEEAP DEDVETELQA RGLTEKTPDL SDEDARLLTQ 

       130        140        150        160        170        180 
RHRVGKPQFN RQDHHKKKRV STSWRKPRGQ LSKQRRGIKG KGDTVEAGFR SPTAVRGKHP 

       190        200        210        220        230        240 
SGFEEVRVHN VDDLEGVDGD TEAVRIASKV GARKRERIEE EAEDAGIRVL NPTYVEVEVS 


E 

« Hide

References

« Hide 'large scale' references
[1]"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].
[2]"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.
[3]"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 2-32 AND 98-113.
[4]"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 99-241.
Strain: ATCC 43049 / DSM 3752 / JCM 8966 / VKM B-1809.
[5]"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.
[6]"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.
[7]"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.
[8]"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.
[9]"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.
[10]"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.
[11]"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.
[12]"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: CAA41288.1.
AY596297 Genomic DNA. Translation: AAV46513.1.
PIRR7HSH5. S16539.
RefSeqYP_136219.1. NC_006396.1.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1FFKX-ray2.40V99-241[»]
1JJ2X-ray2.40X2-241[»]
1K73X-ray3.01Z2-241[»]
1K8AX-ray3.00Z2-241[»]
1K9MX-ray3.00Z2-241[»]
1KC8X-ray3.01Z2-241[»]
1KD1X-ray3.00Z2-241[»]
1KQSX-ray3.10X2-241[»]
1M1KX-ray3.20Z2-241[»]
1M90X-ray2.80Z2-241[»]
1N8RX-ray3.00Z2-241[»]
1NJIX-ray3.00Z2-241[»]
1Q7YX-ray3.20Z2-241[»]
1Q81X-ray2.95Z2-241[»]
1Q82X-ray2.98Z2-241[»]
1Q86X-ray3.00Z2-241[»]
1QVFX-ray3.10X2-241[»]
1QVGX-ray2.90X2-241[»]
1S72X-ray2.40Y1-241[»]
1VQ4X-ray2.70Y1-241[»]
1VQ5X-ray2.60Y1-241[»]
1VQ6X-ray2.70Y1-241[»]
1VQ7X-ray2.50Y1-241[»]
1VQ8X-ray2.20Y1-241[»]
1VQ9X-ray2.40Y1-241[»]
1VQKX-ray2.30Y1-241[»]
1VQLX-ray2.30Y1-241[»]
1VQMX-ray2.30Y1-241[»]
1VQNX-ray2.40Y1-241[»]
1VQOX-ray2.20Y1-241[»]
1VQPX-ray2.25Y1-241[»]
1W2BX-ray3.50X2-241[»]
1YHQX-ray2.40Y1-241[»]
1YI2X-ray2.65Y1-241[»]
1YIJX-ray2.60Y1-241[»]
1YITX-ray2.80Y1-241[»]
1YJ9X-ray2.90Y1-241[»]
1YJNX-ray3.00Y1-241[»]
1YJWX-ray2.90Y1-241[»]
2OTJX-ray2.90Y1-241[»]
2OTLX-ray2.70Y1-241[»]
2QA4X-ray3.00Y1-241[»]
2QEXX-ray2.90Y1-241[»]
3CC2X-ray2.40Y1-241[»]
3CC4X-ray2.70Y1-241[»]
3CC7X-ray2.70Y1-241[»]
3CCEX-ray2.75Y1-241[»]
3CCJX-ray2.70Y1-241[»]
3CCLX-ray2.90Y1-241[»]
3CCMX-ray2.55Y1-241[»]
3CCQX-ray2.90Y1-241[»]
3CCRX-ray3.00Y1-241[»]
3CCSX-ray2.95Y1-241[»]
3CCUX-ray2.80Y1-241[»]
3CCVX-ray2.90Y1-241[»]
3CD6X-ray2.75Y1-241[»]
3CMAX-ray2.80Y1-240[»]
3CMEX-ray2.95Y1-240[»]
3CPWX-ray2.70X1-241[»]
3CXCX-ray3.00X2-241[»]
3G4SX-ray3.20Y96-237[»]
3G6EX-ray2.70Y96-237[»]
3G71X-ray2.85Y96-237[»]
3I55X-ray3.11Y1-241[»]
3I56X-ray2.90Y1-241[»]
3OW2X-ray2.70X96-237[»]
4ADXelectron microscopy6.60Y1-241[»]
4HUBX-ray2.40Y1-241[»]
ProteinModelPortalP12736.
SMRP12736. Positions 96-237.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING272569.rrnAC1595.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAV46513; AAV46513; rrnAC1595.
GeneID3128514.
KEGGhma:rrnAC1595.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG1717.
HOGENOMHOG000038489.
KOK02912.
OMAKPQFNRQ.

Enzyme and pathway databases

BioCycHMAR272569:GJDH-1451-MONOMER.

Family and domain databases

HAMAPMF_00810. Ribosomal_L32e.
InterProIPR010995. DNA_repair_Rad51/TF_NusA_a-hlx.
IPR003583. Hlx-hairpin-Hlx_DNA-bd_motif.
IPR001515. Ribosomal_L32e.
IPR023654. Ribosomal_L32e_arc.
IPR018263. Ribosomal_L32e_CS.
[Graphical view]
PfamPF01655. Ribosomal_L32e. 1 hit.
[Graphical view]
ProDomPD003823. Ribosomal_L32e. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SMARTSM00278. HhH1. 2 hits.
[Graphical view]
SUPFAMSSF47794. SSF47794. 1 hit.
SSF52042. SSF52042. 1 hit.
PROSITEPS00580. RIBOSOMAL_L32E. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP12736.

Entry information

Entry nameRL32_HALMA
AccessionPrimary (citable) accession number: P12736
Secondary accession number(s): Q5V1T9
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1989
Last sequence update: January 23, 2007
Last modified: July 9, 2014
This is version 113 of the entry and version 3 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