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Protein

Ribonuclease TTHA0252

Gene

TTHA0252

Organism
Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Has endoribonuclease activity towards 23S and 16S rRNA (in vitro).1 Publication

Cofactori

Zn2+1 PublicationNote: Binds 2 Zn2+ ions.1 Publication

Enzyme regulationi

Inhibited by cadmium, cobalt, manganese, magnesium, calcium and nickel ions.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi59 – 591Zinc 1
Metal bindingi61 – 611Zinc 1
Metal bindingi63 – 631Zinc 2
Metal bindingi64 – 641Zinc 2
Metal bindingi141 – 1411Zinc 1
Metal bindingi162 – 1621Zinc 1
Metal bindingi162 – 1621Zinc 2
Metal bindingi400 – 4001Zinc 2

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Endonuclease, Hydrolase, Nuclease

Keywords - Biological processi

rRNA processing

Keywords - Ligandi

Metal-binding, RNA-binding, Zinc

Enzyme and pathway databases

BioCyciTTHE300852:GH8R-266-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Ribonuclease TTHA0252 (EC:3.1.-.-)
Gene namesi
Ordered Locus Names:TTHA0252
OrganismiThermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)
Taxonomic identifieri300852 [NCBI]
Taxonomic lineageiBacteriaDeinococcus-ThermusDeinococciThermalesThermaceaeThermus
Proteomesi
  • UP000000532 Componenti: Chromosome

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 431431Ribonuclease TTHA0252PRO_0000319322Add
BLAST

Interactioni

Subunit structurei

Monomer.1 Publication

Protein-protein interaction databases

STRINGi300852.TTHA0252.

Structurei

Secondary structure

1
431
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi2 – 54Combined sources
Beta strandi9 – 135Combined sources
Beta strandi17 – 215Combined sources
Beta strandi24 – 285Combined sources
Helixi35 – 428Combined sources
Helixi49 – 513Combined sources
Beta strandi54 – 563Combined sources
Helixi62 – 654Combined sources
Helixi68 – 736Combined sources
Beta strandi80 – 823Combined sources
Helixi84 – 10017Combined sources
Helixi108 – 1169Combined sources
Beta strandi118 – 1203Combined sources
Beta strandi127 – 1293Combined sources
Beta strandi132 – 1387Combined sources
Beta strandi146 – 1527Combined sources
Beta strandi155 – 1595Combined sources
Beta strandi168 – 1714Combined sources
Beta strandi181 – 1866Combined sources
Turni188 – 1914Combined sources
Helixi197 – 21317Combined sources
Beta strandi217 – 2215Combined sources
Turni224 – 2263Combined sources
Helixi227 – 23812Combined sources
Helixi239 – 2413Combined sources
Beta strandi247 – 2504Combined sources
Helixi252 – 2609Combined sources
Helixi261 – 2677Combined sources
Helixi270 – 2778Combined sources
Beta strandi288 – 2903Combined sources
Helixi294 – 3029Combined sources
Beta strandi305 – 3128Combined sources
Beta strandi316 – 3194Combined sources
Helixi320 – 3289Combined sources
Beta strandi335 – 3384Combined sources
Helixi347 – 3526Combined sources
Beta strandi356 – 3605Combined sources
Beta strandi363 – 3664Combined sources
Beta strandi369 – 3735Combined sources
Helixi375 – 3773Combined sources
Helixi383 – 3908Combined sources
Beta strandi394 – 4018Combined sources
Helixi403 – 41513Combined sources
Beta strandi419 – 4224Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2DKFX-ray2.80A/B/C/D1-431[»]
3A4YX-ray2.50A/B/C/D1-431[»]
3IDZX-ray2.50A/B/C/D1-431[»]
3IE0X-ray2.73A/B/C/D1-431[»]
3IE1X-ray2.85A/B/C/D1-431[»]
3IE2X-ray2.80A/B/C/D1-431[»]
3IEKX-ray2.05A/B/C/D1-431[»]
3IELX-ray2.35A/B/C/D1-431[»]
3IEMX-ray2.50A/B/C/D1-431[»]
ProteinModelPortaliQ5SLP1.
SMRiQ5SLP1. Positions 1-431.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ5SLP1.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiENOG4105CY0. Bacteria.
COG1236. LUCA.
HOGENOMiHOG000244774.
KOiK07576.
OMAiNLRLRNW.
PhylomeDBiQ5SLP1.

Family and domain databases

Gene3Di3.60.15.10. 1 hit.
InterProiIPR022712. Beta_Casp.
IPR001279. Metallo-B-lactamas.
IPR011108. RMMBL.
[Graphical view]
PfamiPF10996. Beta-Casp. 1 hit.
PF00753. Lactamase_B. 1 hit.
PF07521. RMMBL. 1 hit.
[Graphical view]
SMARTiSM01027. Beta-Casp. 1 hit.
SM00849. Lactamase_B. 1 hit.
[Graphical view]
SUPFAMiSSF56281. SSF56281. 1 hit.

Sequencei

Sequence statusi: Complete.

Q5SLP1-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MRIVPFGAAR EVTGSAHLLL AGGRRVLLDC GMFQGKEEAR NHAPFGFDPK
60 70 80 90 100
EVDAVLLTHA HLDHVGRLPK LFREGYRGPV YATRATVLLM EIVLEDALKV
110 120 130 140 150
MDEPFFGPED VEEALGHLRP LEYGEWLRLG ALSLAFGQAG HLPGSAFVVA
160 170 180 190 200
QGEGRTLVYS GDLGNREKDV LPDPSLPPLA DLVLAEGTYG DRPHRPYRET
210 220 230 240 250
VREFLEILEK TLSQGGKVLI PTFAVERAQE ILYVLYTHGH RLPRAPIYLD
260 270 280 290 300
SPMAGRVLSL YPRLVRYFSE EVQAHFLQGK NPFRPAGLEV VEHTEASKAL
310 320 330 340 350
NRAPGPMVVL AGSGMLAGGR ILHHLKHGLS DPRNALVFVG YQPQGGLGAE
360 370 380 390 400
IIARPPAVRI LGEEVPLRAS VHTLGGFSGH AGQDELLDWL QGEPRVVLVH
410 420 430
GEEEKLLALG KLLALRGQEV SLARFGEGVP V
Length:431
Mass (Da):47,055
Last modified:December 21, 2004 - v1
Checksum:i89BB88D1F61D4BFC
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AP008226 Genomic DNA. Translation: BAD70075.1.
RefSeqiWP_011227806.1. NC_006461.1.
YP_143518.1. NC_006461.1.

Genome annotation databases

EnsemblBacteriaiBAD70075; BAD70075; BAD70075.
GeneIDi3170139.
KEGGittj:TTHA0252.
PATRICi23955459. VBITheThe93045_0252.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AP008226 Genomic DNA. Translation: BAD70075.1.
RefSeqiWP_011227806.1. NC_006461.1.
YP_143518.1. NC_006461.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2DKFX-ray2.80A/B/C/D1-431[»]
3A4YX-ray2.50A/B/C/D1-431[»]
3IDZX-ray2.50A/B/C/D1-431[»]
3IE0X-ray2.73A/B/C/D1-431[»]
3IE1X-ray2.85A/B/C/D1-431[»]
3IE2X-ray2.80A/B/C/D1-431[»]
3IEKX-ray2.05A/B/C/D1-431[»]
3IELX-ray2.35A/B/C/D1-431[»]
3IEMX-ray2.50A/B/C/D1-431[»]
ProteinModelPortaliQ5SLP1.
SMRiQ5SLP1. Positions 1-431.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi300852.TTHA0252.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiBAD70075; BAD70075; BAD70075.
GeneIDi3170139.
KEGGittj:TTHA0252.
PATRICi23955459. VBITheThe93045_0252.

Phylogenomic databases

eggNOGiENOG4105CY0. Bacteria.
COG1236. LUCA.
HOGENOMiHOG000244774.
KOiK07576.
OMAiNLRLRNW.
PhylomeDBiQ5SLP1.

Enzyme and pathway databases

BioCyciTTHE300852:GH8R-266-MONOMER.

Miscellaneous databases

EvolutionaryTraceiQ5SLP1.

Family and domain databases

Gene3Di3.60.15.10. 1 hit.
InterProiIPR022712. Beta_Casp.
IPR001279. Metallo-B-lactamas.
IPR011108. RMMBL.
[Graphical view]
PfamiPF10996. Beta-Casp. 1 hit.
PF00753. Lactamase_B. 1 hit.
PF07521. RMMBL. 1 hit.
[Graphical view]
SMARTiSM01027. Beta-Casp. 1 hit.
SM00849. Lactamase_B. 1 hit.
[Graphical view]
SUPFAMiSSF56281. SSF56281. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiRNSE_THET8
AccessioniPrimary (citable) accession number: Q5SLP1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 26, 2008
Last sequence update: December 21, 2004
Last modified: September 7, 2016
This is version 72 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. 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.