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Q9X1J7 (RRMF_THEMA) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 81. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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:
Probable rRNA maturation factor
Gene names
Ordered Locus Names:TM_1509
OrganismThermotoga maritima
Taxonomic identifier2336 [NCBI]
Taxonomic lineageBacteriaThermotogaeThermotogalesThermotogaceaeThermotoga

Protein attributes

Sequence length150 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Involved in rRNA and/or ribosome maturation and assembly. Required for normal 5' and 3' processing of 16S, 23S and 5S rRNAs. May have metal-dependent hydrolase activity By similarity. Ref.2

Cofactor

Binds 1 zinc ion.

Subcellular location

Cytoplasm By similarity HAMAP MF_00009.

Sequence similarities

Belongs to the rRNA maturation factor YbeY family.

Ontologies

Keywords
   Biological processRibosome biogenesis
rRNA processing
   Cellular componentCytoplasm
   LigandMetal-binding
Zinc
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological processrRNA processing

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionmetal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

metalloendopeptidase activity

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 150150Probable rRNA maturation factor HAMAP MF_00009
PRO_0000102553

Sites

Metal binding1021Zinc; catalytic By similarity
Metal binding1061Zinc; catalytic By similarity
Metal binding1121Zinc; catalytic By similarity

Secondary structure

....................... 150
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q9X1J7 [UniParc].

Last modified November 1, 1999. Version 1.
Checksum: 5BDE227C0BE6DCC5

FASTA15017,550
        10         20         30         40         50         60 
MIRILGEGKG SKLLENLKEK LEEIVKKEIG DVHVNVILVS EDEIKELNQQ FRGQDRPTDV 

        70         80         90        100        110        120 
LTFPLMEEDV YGEIYVCPLI VEENAREFNN TFEKELLEVV IHGILHLAGY DHEFEDKNSK 

       130        140        150 
EMFEKQKKYV EEVWGEWRSN PSEDSDPGKR 

« Hide

References

« Hide 'large scale' references
[1]"Evidence for lateral gene transfer between Archaea and Bacteria from genome sequence of Thermotoga maritima."
Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., Stewart A.M., Cotton M.D., Pratt M.S. expand/collapse author list , Phillips C.A., Richardson D.L., Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.
Nature 399:323-329(1999) [PubMed: 10360571] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 43589 / MSB8 / DSM 3109 / JCM 10099.
[2]"NMR solution structure of Thermotoga maritima protein TM1509 reveals a Zn-metalloprotease-like tertiary structure."
Penhoat C.H., Li Z., Atreya H.S., Kim S., Yee A., Xiao R., Murray D., Arrowsmith C.H., Szyperski T.
J. Struct. Funct. Genomics 6:51-62(2005) [PubMed: 15965736] [Abstract]
Cited for: STRUCTURE BY NMR, FUNCTION, ZINC BINDING.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE000512 Genomic DNA. Translation: AAD36576.1.
PIRF72244.
RefSeqNP_229309.1. NC_000853.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1TVINMR-A1-150[»]
ProteinModelPortalQ9X1J7.
SMRQ9X1J7. Positions 1-150.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID898186.
GenomeReviewsGene locus TM_1509 in contig AE000512_GR.
KEGGtma:TM1509.
NMPDRfig|243274.1.peg.1493.
PATRIC23937976. VBITheMar51294_1526.
TIGRTM_1509.

Phylogenomic databases

HOGENOMHBG734136.
OMADVLTFVY.
PhylomeDBQ9X1J7.
ProtClustDBCLSK875802.

Enzyme and pathway databases

BioCycTMAR243274:TM_1509-MONOMER.

Family and domain databases

HAMAPMF_00009. rRNA_matur_factor.
[Tree]
InterProIPR023091. MetalPrtase_cat_dom_prd.
IPR020549. UPF0054_CS.
IPR002036. UPF0054_metalloprotease_prd.
[Graphical view]
Gene3DG3DSA:3.40.390.30. MetalPrtase_cat_dom_prd. 1 hit.
KOK07042.
PfamPF02130. UPF0054. 1 hit.
[Graphical view]
TIGRFAMsTIGR00043. TIGR00043. 1 hit.
PROSITEPS01306. UPF0054. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameRRMF_THEMA
AccessionPrimary (citable) accession number: Q9X1J7
Entry history
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: November 1, 1999
Last modified: January 25, 2012
This is version 81 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families