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D6YRY8 (D6YRY8_WADCW) Unreviewed, UniProtKB/TrEMBL

Last modified February 19, 2014. Version 26. 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 attributes

Sequence length456 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

The central subunit of the protein translocation channel SecYEG. Consists of two halves formed by TMs 1-5 and 6-10. These two domains form a lateral gate at the front which open onto the bilayer between TMs 2 and 7, and are clamped together by SecE at the back. The channel is closed by both a pore ring composed of hydrophobic SecY resides and a short helix (helix 2A) on the extracellular side of the membrane which forms a plug. The plug probably moves laterally to allow the channel to open. The ring and the pore may move independently By similarity. RuleBase RU000537 HAMAP-Rule MF_01465

Subunit structure

Component of the Sec protein translocase complex. Heterotrimer consisting of SecY, SecE and SecG subunits. The heterotrimers can form oligomers, although 1 heterotrimer is thought to be able to translocate proteins. Interacts with the ribosome. Interacts with SecDF, and other proteins may be involved. Interacts with SecA By similarity. HAMAP-Rule MF_01465

Subcellular location

Cell inner membrane; Multi-pass membrane protein By similarity HAMAP-Rule MF_01465.

Membrane; Multi-pass membrane protein By similarity RuleBase RU003484.

Sequence similarities

Belongs to the SecY/SEC61-alpha family. HAMAP-Rule MF_01465 RuleBase RU004349

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Regions

Transmembrane18 – 3821Helical; By similarity HAMAP-Rule MF_01465
Transmembrane73 – 9321Helical; By similarity HAMAP-Rule MF_01465
Transmembrane121 – 14121Helical; By similarity HAMAP-Rule MF_01465
Transmembrane163 – 18321Helical; By similarity HAMAP-Rule MF_01465
Transmembrane196 – 21621Helical; By similarity HAMAP-Rule MF_01465
Transmembrane231 – 25121Helical; By similarity HAMAP-Rule MF_01465
Transmembrane288 – 30821Helical; By similarity HAMAP-Rule MF_01465
Transmembrane326 – 34621Helical; By similarity HAMAP-Rule MF_01465
Transmembrane386 – 40621Helical; By similarity HAMAP-Rule MF_01465
Transmembrane412 – 43221Helical; By similarity HAMAP-Rule MF_01465

Sequences

Sequence LengthMass (Da)Tools
D6YRY8 [UniParc].

Last modified August 10, 2010. Version 1.
Checksum: 85C3FF5BEC463541

FASTA45650,748
        10         20         30         40         50         60 
MIQALQRVFS IPELRQKISF TLLMLVVCRI GAFIPVPGIN GEVAIQYLRH LTGGEQNLFR 

        70         80         90        100        110        120 
MVDTFTGGAF SQMTVIALGV VPYISASIMM QLFTALIPSL QREIQENPTL GRRKVNRLTR 

       130        140        150        160        170        180 
LVTLILAFIQ SAMFAKYAIQ MNITKPGIIA GDLLNIQMFG HPVLFYAVMI FTMTTGTLFL 

       190        200        210        220        230        240 
MWIGEQITEN GIGNGMSLII TLGIISSFPT AIGMIFQQLN LDSQEAGQLN FAIVAVIMAV 

       250        260        270        280        290        300 
FVLVTIGTIL IVQGHRRIPL QYARRVVGRK EVQGGNSYIP LKVNYAGVIP VIFASSLLMF 

       310        320        330        340        350        360 
PATIATFIGQ GTWLESVAMW FRQDRTAYMV MYVGLIIFFT YFWTATQFRP DQIASDMKKN 

       370        380        390        400        410        420 
GAFIPGIRQG RPTQEYLEHT MNRITLIGAV FLALIAILPT ITGRVLGVSQ TISYFFGGTA 

       430        440        450 
LLILVGVVLD TMKQIESHLL MKRYEGFMKK GRARGR 

« Hide

References

[1]"The Waddlia genome: a window into chlamydial biology."
Bertelli C., Collyn F., Croxatto A., Ruckert C., Polkinghorne A., Kebbi-Beghdadi C., Goesmann A., Vaughan L., Greub G.
PLoS ONE 5:E10890-E10890(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC VR-1470 / WSU 86-1044.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP001928 Genomic DNA. Translation: ADI38833.1.
RefSeqYP_003709839.1. NC_014225.1.

3D structure databases

ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaADI38833; ADI38833; wcw_1484.
GeneID9278463.
KEGGwch:wcw_1484.
PATRIC38314956. VBIWadCho156037_1440.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHOG000080586.
KOK03076.

Enzyme and pathway databases

BioCycWCHO716544:GHGA-1484-MONOMER.

Family and domain databases

Gene3D1.10.3370.10. 1 hit.
HAMAPMF_01465. SecY.
InterProIPR026593. SecY.
IPR002208. SecY/SEC61-alpha.
IPR023201. SecY_su_dom.
[Graphical view]
PANTHERPTHR10906. PTHR10906. 1 hit.
PfamPF00344. SecY. 1 hit.
[Graphical view]
PIRSFPIRSF004557. SecY. 1 hit.
SUPFAMSSF103491. SSF103491. 1 hit.
TIGRFAMsTIGR00967. 3a0501s007. 1 hit.
PROSITEPS00755. SECY_1. 1 hit.
PS00756. SECY_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameD6YRY8_WADCW
AccessionPrimary (citable) accession number: D6YRY8
Entry history
Integrated into UniProtKB/TrEMBL: August 10, 2010
Last sequence update: August 10, 2010
Last modified: February 19, 2014
This is version 26 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)