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Protein

Protein translocase subunit SecY

Gene

secY

Organism
Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Protein inferred from homologyi

Functioni

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.UniRule annotation

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Protein transport, Translocation, Transport

Enzyme and pathway databases

BioCyciPHOR70601:GJWR-1754-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Protein translocase subunit SecYUniRule annotation
Alternative name(s):
Protein transport protein SEC61 subunit alpha homologUniRule annotation
Gene namesi
Name:secYUniRule annotation
Ordered Locus Names:PH1754
OrganismiPyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3)
Taxonomic identifieri70601 [NCBI]
Taxonomic lineageiArchaeaEuryarchaeotaThermococciThermococcalesThermococcaceaePyrococcus
Proteomesi
  • UP000000752 Componenti: Chromosome

Subcellular locationi

  • Cell membrane UniRule annotation; Multi-pass membrane protein UniRule annotation

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 2020CytoplasmicBy similarityAdd
BLAST
Transmembranei21 – 4727Helical; Name=Helix 1UniRule annotationAdd
BLAST
Topological domaini48 – 5811ExtracellularBy similarityAdd
BLAST
Transmembranei59 – 8729Discontinuously helical; Name=Helix 2By similarityAdd
BLAST
Intramembranei59 – 668Helical; Name=Helix 2ABy similarity
Intramembranei67 – 7812By similarityAdd
BLAST
Intramembranei79 – 879Helical; Name=Helix 2BBy similarity
Topological domaini88 – 10821CytoplasmicBy similarityAdd
BLAST
Transmembranei109 – 13325Helical; Name=Helix 3UniRule annotationAdd
BLAST
Topological domaini134 – 14411ExtracellularBy similarityAdd
BLAST
Transmembranei145 – 16925Helical; Name=Helix 4UniRule annotationAdd
BLAST
Topological domaini170 – 1756CytoplasmicBy similarity
Transmembranei176 – 19419Helical; Name=Helix 5UniRule annotationAdd
BLAST
Topological domaini195 – 23945ExtracellularBy similarityAdd
BLAST
Transmembranei240 – 26122Helical; Name=Helix 6UniRule annotationAdd
BLAST
Topological domaini262 – 28524CytoplasmicBy similarityAdd
BLAST
Transmembranei286 – 30722Helical; Name=Helix 7UniRule annotationAdd
BLAST
Topological domaini308 – 34639ExtracellularBy similarityAdd
BLAST
Transmembranei347 – 36620Helical; Name=Helix 8UniRule annotationAdd
BLAST
Topological domaini367 – 40943CytoplasmicBy similarityAdd
BLAST
Transmembranei410 – 42819Helical; Name=Helix 9UniRule annotationAdd
BLAST
Topological domaini429 – 4313ExtracellularBy similarity
Transmembranei432 – 44615Helical; Name=Helix 10UniRule annotationAdd
BLAST
Topological domaini447 – 46822CytoplasmicBy similarityAdd
BLAST

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 468468Protein translocase subunit SecYPRO_0000131769Add
BLAST

Interactioni

Subunit structurei

Component of the Sec protein translocase complex. Heterotrimer consisting of alpha (SecY), beta (SecG) and gamma (SecE) subunits. The heterotrimers can form oligomers, although 1 heterotrimer is thought to be able to translocate proteins. Interacts with the ribosome. May interact with SecDF, and other proteins may be involved.UniRule annotation

Protein-protein interaction databases

STRINGi70601.PH1754.

Structurei

3D structure databases

ProteinModelPortaliO59442.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the SecY/SEC61-alpha family.UniRule annotation

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiarCOG04169. Archaea.
COG0201. LUCA.
HOGENOMiHOG000231248.
KOiK03076.
OMAiRYIPYVT.

Family and domain databases

Gene3Di1.10.3370.10. 1 hit.
HAMAPiMF_01465. SecY. 1 hit.
InterProiIPR026593. SecY.
IPR002208. SecY/SEC61-alpha.
IPR030659. SecY_CS.
IPR023201. SecY_su_dom.
IPR019561. Translocon_Sec61/SecY_plug_dom.
[Graphical view]
PANTHERiPTHR10906. PTHR10906. 1 hit.
PfamiPF10559. Plug_translocon. 1 hit.
PF00344. SecY. 1 hit.
[Graphical view]
PIRSFiPIRSF004557. SecY. 1 hit.
SUPFAMiSSF103491. SSF103491. 1 hit.
TIGRFAMsiTIGR00967. 3a0501s007. 1 hit.
PROSITEiPS00755. SECY_1. 1 hit.
PS00756. SECY_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

O59442-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGARDVIYAM EKWFPEVERP KKHVPLKEKF VWTGLALVLY YVLAEIPVYG
60 70 80 90 100
IPKKIQDYFQ FLRVVLAGRN GSILTLGIGP IVTAGIILQL LVGSELIRLD
110 120 130 140 150
LANPEDRRFY QALQRVFSVF MCFFEAAIWV LGGAFGRVGV DVTYTIATLM
160 170 180 190 200
IIQLALGGII LIVLDELVSK WGIGSGISLF IAAGVSQRIL TRSLNPLTDP
210 220 230 240 250
NIIDPLTGKP AIVGAIPYFI QHILDGDLKG ALYRGGSAPD MIAVTATIIV
260 270 280 290 300
FLVVVYFESM RVEIPLGYRG VTIRGRYPIK FLYVSNIPII LTFALYANIQ
310 320 330 340 350
LWARVLDRFG HPWLGRFDPV TGNPIGGFVL YVIPPRNIFT VIDNPVRAII
360 370 380 390 400
YLILTIIFSL LFGFLWVELT GLDARTIARQ LQRAGLQIPG FRRDPRTLER
410 420 430 440 450
VLQKYIPYVT FWGSLTVALI SVLADFLGAL GTGTGILLTV GILYRFYEEI
460
AREQITEMFP ALRRLFKG
Length:468
Mass (Da):52,314
Last modified:August 1, 1998 - v1
Checksum:i707E102D59392C6C
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BA000001 Genomic DNA. Translation: BAA30868.1.
PIRiE71184.
RefSeqiWP_010885818.1. NC_000961.1.

Genome annotation databases

EnsemblBacteriaiBAA30868; BAA30868; BAA30868.
GeneIDi1442599.
KEGGipho:PH1754.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BA000001 Genomic DNA. Translation: BAA30868.1.
PIRiE71184.
RefSeqiWP_010885818.1. NC_000961.1.

3D structure databases

ProteinModelPortaliO59442.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi70601.PH1754.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiBAA30868; BAA30868; BAA30868.
GeneIDi1442599.
KEGGipho:PH1754.

Phylogenomic databases

eggNOGiarCOG04169. Archaea.
COG0201. LUCA.
HOGENOMiHOG000231248.
KOiK03076.
OMAiRYIPYVT.

Enzyme and pathway databases

BioCyciPHOR70601:GJWR-1754-MONOMER.

Family and domain databases

Gene3Di1.10.3370.10. 1 hit.
HAMAPiMF_01465. SecY. 1 hit.
InterProiIPR026593. SecY.
IPR002208. SecY/SEC61-alpha.
IPR030659. SecY_CS.
IPR023201. SecY_su_dom.
IPR019561. Translocon_Sec61/SecY_plug_dom.
[Graphical view]
PANTHERiPTHR10906. PTHR10906. 1 hit.
PfamiPF10559. Plug_translocon. 1 hit.
PF00344. SecY. 1 hit.
[Graphical view]
PIRSFiPIRSF004557. SecY. 1 hit.
SUPFAMiSSF103491. SSF103491. 1 hit.
TIGRFAMsiTIGR00967. 3a0501s007. 1 hit.
PROSITEiPS00755. SECY_1. 1 hit.
PS00756. SECY_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiSECY_PYRHO
AccessioniPrimary (citable) accession number: O59442
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 11, 2001
Last sequence update: August 1, 1998
Last modified: November 11, 2015
This is version 96 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

Complete proteome

Documents

  1. 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.