SECY_EMIHU
ID SECY_EMIHU Reviewed; 422 AA.
AC Q4G351;
DT 14-DEC-2011, integrated into UniProtKB/Swiss-Prot.
DT 30-AUG-2005, sequence version 1.
DT 03-AUG-2022, entry version 54.
DE RecName: Full=Protein translocase subunit SecY;
GN Name=secY;
OS Emiliania huxleyi (Coccolithophore) (Pontosphaera huxleyi).
OG Plastid; Chloroplast.
OC Eukaryota; Haptista; Haptophyta; Prymnesiophyceae; Isochrysidales;
OC Noelaerhabdaceae; Emiliania.
OX NCBI_TaxID=2903;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCMP373 / CSIRO-CS-57 / BT6;
RX PubMed=16303746; DOI=10.1093/dnares/12.2.151;
RA Sanchez-Puerta M.V., Bachvaroff T.R., Delwiche C.F.;
RT "The complete plastid genome sequence of the haptophyte Emiliania huxleyi:
RT a comparison to other plastid genomes.";
RL DNA Res. 12:151-156(2005).
CC -!- FUNCTION: The central subunit of the protein translocation channel
CC SecYE. Consists of two halves formed by TMs 1-5 and 6-10. These two
CC domains form a lateral gate at the front which open onto the bilayer
CC between TMs 2 and 7, and are clamped together by SecE at the back. The
CC channel is closed by both a pore ring composed of hydrophobic SecY
CC resides and a short helix (helix 2A) on the extracellular side of the
CC membrane which forms a plug (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Component of the plastid Sec protein translocase complex,
CC which is composed of at least SecY, SecE and SecG. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid membrane
CC {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the SecY/SEC61-alpha family. {ECO:0000305}.
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DR EMBL; AY741371; AAX13915.1; -; Genomic_DNA.
DR RefSeq; YP_277416.1; NC_007288.1.
DR AlphaFoldDB; Q4G351; -.
DR SMR; Q4G351; -.
DR GeneID; 3562500; -.
DR Proteomes; UP000013827; Unassembled WGS sequence.
DR GO; GO:0009535; C:chloroplast thylakoid membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0065002; P:intracellular protein transmembrane transport; IEA:UniProtKB-UniRule.
DR GO; GO:0006605; P:protein targeting; IEA:UniProtKB-UniRule.
DR Gene3D; 1.10.3370.10; -; 1.
DR HAMAP; MF_01465; SecY; 1.
DR InterPro; IPR026593; SecY.
DR InterPro; IPR002208; SecY/SEC61-alpha.
DR InterPro; IPR023201; SecY_dom_sf.
DR PANTHER; PTHR10906; PTHR10906; 1.
DR Pfam; PF00344; SecY; 1.
DR PIRSF; PIRSF004557; SecY; 1.
DR SUPFAM; SSF103491; SSF103491; 1.
DR TIGRFAMs; TIGR00967; 3a0501s007; 1.
PE 3: Inferred from homology;
KW Chloroplast; Membrane; Plastid; Protein transport; Reference proteome;
KW Thylakoid; Translocation; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..422
FT /note="Protein translocase subunit SecY"
FT /id="PRO_0000414215"
FT TRANSMEM 17..37
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 61..81
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 114..134
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 141..161
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 166..186
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 202..222
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 265..285
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 306..326
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 364..384
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 394..414
FT /note="Helical"
FT /evidence="ECO:0000255"
SQ SEQUENCE 422 AA; 46182 MW; 6F8B7D72BF1AF7D5 CRC64;
MEQSTTRSLL KGKILKILTL LLLVRLGLYI PVPGVELDIL TQGQTSNPMF GFAKTLVGNS
FLGIGSLGIL PYINASIIIQ LLTPLFPNLE RLQKEEGELG RQQISRYTRY LTCIWAIVLS
SAIAFFLIKP ITFGWSLKLG LEIVLSLTVG SILSMWFAEL ITEESLGNGS SMIIFINIVG
GIPNNLSSLS KTFSAANLAS AIPLLLTGLG IYLGIVLIII FFQESYKKIT IVSAKQLNLT
TSAQTQSERL ANNSFIPLKL NQGGIMPLVF SSTIAVVFMY PAQILLSSAL LTNAAGLASK
LLTIYSFGIN FVLVIFFSCF YVSLVLKPKD MSENLGKMAY SIPGIRQGKE TTKYLEKVIN
RLAFIGGLFL AFLAFFPLFV GNFIQFGLFK NLTSLLILIG VITDTTSQIT GYLVSTRYEG
LK