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A1AHV2 (A1AHV2_ECOK1) Unreviewed, UniProtKB/TrEMBL

Last modified May 1, 2013. Version 53. Feed History...

Clusters with 100%, 90%, 50% identity | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Transcription termination factor Rho HAMAP-Rule MF_01884

EC=3.6.4.- HAMAP-Rule MF_01884
Alternative name(s):
ATP-dependent helicase Rho HAMAP-Rule MF_01884
Gene names
Name:rho HAMAP-Rule MF_01884 EMBL ABJ03242.1
Ordered Locus Names:Ecok1_37480
ORF Names:APECO1_2691 EMBL ABJ03242.1
OrganismEscherichia coli O1:K1 / APEC [Complete proteome] [HAMAP]
Taxonomic identifier405955 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length443 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Facilitates transcription termination by a mechanism that involves Rho binding to the nascent RNA, activation of Rho's RNA-dependent ATPase activity, and release of the mRNA from the DNA template By similarity. HAMAP-Rule MF_01884

Subunit structure

Homohexamer. The homohexamer assembles into an open ring structure By similarity. HAMAP-Rule MF_01884

Sequence similarities

Belongs to the Rho family. HAMAP-Rule MF_01884

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Regions

Nucleotide binding193 – 1986ATP By similarity HAMAP-Rule MF_01884
Nucleotide binding205 – 2106ATP By similarity HAMAP-Rule MF_01884
Region85 – 906RNA-binding 1 By similarity HAMAP-Rule MF_01884
Region102 – 1043RNA-binding 1 By similarity HAMAP-Rule MF_01884
Region132 – 1343RNA-binding 1 By similarity HAMAP-Rule MF_01884
Region308 – 3125RNA-binding 2 By similarity HAMAP-Rule MF_01884

Sites

Binding site2361ATP By similarity HAMAP-Rule MF_01884
Site3501RNA-binding 2 By similarity HAMAP-Rule MF_01884

Sequences

Sequence LengthMass (Da)Tools
A1AHV2 [UniParc].

Last modified January 23, 2007. Version 1.
Checksum: F968699095510E87

FASTA44349,679
        10         20         30         40         50         60 
MDDPAIPFTT LSSRFTPSLR THTTMNLTEL KNTPVSELIT LGENMGLENL ARMRKQDIIF 

        70         80         90        100        110        120 
AILKQHAKSG EDIFGDGVLE ILQDGFGFLR SADSSYLAGP DDIYVSPSQI RRFNLRTGDT 

       130        140        150        160        170        180 
ISGKIRPPKE GERYFALLKV NEVNFDKPEN ARNKILFENL TPLHANSRLR MERGNGSTED 

       190        200        210        220        230        240 
LTARVLDLAS PIGRGQRGLI VAPPKAGKTM LLQNIAQSIA YNHPDCVLMV LLIDERPEEV 

       250        260        270        280        290        300 
TEMQRLVKGE VVASTFDEPA SRHVQVAEMV IEKAKRLVEH KKDVIILLDS ITRLARAYNT 

       310        320        330        340        350        360 
VVPASGKVLT GGVDANALHR PKRFFGAARN VEEGGSLTII ATALIDTGSK MDEVIYEEFK 

       370        380        390        400        410        420 
GTGNMELHLS RKIAEKRVFP AIDYNRSGTR KEELLTTQEE LQKMWILRKI IHPMGEIDAM 

       430        440 
EFLINKLAMT KTNDDFFEMM KRS 

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References

[1]"The genome sequence of avian pathogenic Escherichia coli strain O1:K1:H7 shares strong similarities with human extraintestinal pathogenic E. coli genomes."
Johnson T.J., Kariyawasam S., Wannemuehler Y., Mangiamele P., Johnson S.J., Doetkott C., Skyberg J.A., Lynne A.M., Johnson J.R., Nolan L.K.
J. Bacteriol. 189:3228-3236(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000468 Genomic DNA. Translation: ABJ03242.1.
RefSeqYP_859366.1. NC_008563.1.

3D structure databases

ProteinModelPortalA1AHV2.
SMRA1AHV2. Positions 25-441.
ModBaseSearch...

Protein-protein interaction databases

STRING405955.APECO1_2691.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABJ03242; ABJ03242; APECO1_2691.
GeneID4493003.
KEGGecv:APECO1_2691.
PATRIC18220019. VBIEscCol127180_4228.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG1158.
HOGENOMHOG000076952.
KOK03628.
OMAFGFLRAP.
ProtClustDBPRK09376.

Family and domain databases

Gene3D2.40.50.140. 1 hit.
HAMAPMF_01884. Rho.
InterProIPR003593. AAA+_ATPase.
IPR000194. ATPase_F1/V1/A1_a/bsu_nucl-bd.
IPR011129. Cold_shock_prot.
IPR012340. NA-bd_OB-fold.
IPR011112. Rho_N.
IPR011113. Rho_RNA-bd.
IPR004665. Term_rho.
[Graphical view]
PfamPF00006. ATP-synt_ab. 1 hit.
PF07498. Rho_N. 1 hit.
PF07497. Rho_RNA_bind. 1 hit.
[Graphical view]
SMARTSM00382. AAA. 1 hit.
SM00357. CSP. 1 hit.
SM00959. Rho_N. 1 hit.
[Graphical view]
SUPFAMSSF50249. Nucleic_acid_OB. 1 hit.
SSF68912. Rho_N. 1 hit.
TIGRFAMsTIGR00767. rho. 1 hit.
ProtoNetSearch...

Entry information

Entry nameA1AHV2_ECOK1
AccessionPrimary (citable) accession number: A1AHV2
Entry history
Integrated into UniProtKB/TrEMBL: January 23, 2007
Last sequence update: January 23, 2007
Last modified: May 1, 2013
This is version 53 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)