SECY_CYAM1
ID SECY_CYAM1 Reviewed; 340 AA.
AC Q85FU6;
DT 14-DEC-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 86.
DE RecName: Full=Protein translocase subunit SecY {ECO:0000255|HAMAP-Rule:MF_01465};
GN Name=secY {ECO:0000255|HAMAP-Rule:MF_01465};
OS Cyanidioschyzon merolae (strain NIES-3377 / 10D) (Unicellular red alga).
OG Plastid; Chloroplast.
OC Eukaryota; Rhodophyta; Bangiophyceae; Cyanidiales; Cyanidiaceae;
OC Cyanidioschyzon.
OX NCBI_TaxID=280699;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NIES-3377 / 10D;
RX PubMed=12755171; DOI=10.1093/dnares/10.2.67;
RA Ohta N., Matsuzaki M., Misumi O., Miyagishima S.-Y., Nozaki H., Tanaka K.,
RA Shin-i T., Kohara Y., Kuroiwa T.;
RT "Complete sequence and analysis of the plastid genome of the unicellular
RT red alga Cyanidioschyzon merolae.";
RL DNA Res. 10:67-77(2003).
CC -!- FUNCTION: The central subunit of the protein translocation channel
CC SecYE. Consists of two halves. These two domains form a lateral gate at
CC the front which open onto the bilayer between TMs 2 and 7, and are
CC clamped together by SecE at the back. The channel is closed by both a
CC pore ring composed of hydrophobic SecY resides and a short helix (helix
CC 2A) on the extracellular side of the membrane which forms a plug (By
CC similarity). {ECO:0000250}.
CC -!- SUBUNIT: Component of the plastid Sec protein translocase complex,
CC which is composed of at least SecY and SecE. {ECO:0000255|HAMAP-
CC Rule:MF_01465}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid membrane
CC {ECO:0000255|HAMAP-Rule:MF_01465}; Multi-pass membrane protein
CC {ECO:0000255|HAMAP-Rule:MF_01465}.
CC -!- SIMILARITY: Belongs to the SecY/SEC61-alpha family. {ECO:0000255|HAMAP-
CC Rule:MF_01465}.
CC -!- CAUTION: Bioinformatics prediction programs detect only 8 instead of 10
CC transmembrane regions. {ECO:0000305}.
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DR EMBL; AB002583; BAC76248.1; -; Genomic_DNA.
DR RefSeq; NP_849086.1; NC_004799.1.
DR AlphaFoldDB; Q85FU6; -.
DR SMR; Q85FU6; -.
DR STRING; 45157.CMV181CT; -.
DR EnsemblPlants; CMV181CT; CMV181CT; CMV181C.
DR GeneID; 845021; -.
DR Gramene; CMV181CT; CMV181CT; CMV181C.
DR KEGG; cme:CymeCp154; -.
DR eggNOG; ENOG502QSNV; Eukaryota.
DR HOGENOM; CLU_030313_0_0_1; -.
DR Proteomes; UP000007014; Chloroplast.
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; IPR030659; SecY_CS.
DR InterPro; IPR023201; SecY_dom_sf.
DR PANTHER; PTHR10906; PTHR10906; 2.
DR Pfam; PF00344; SecY; 1.
DR SUPFAM; SSF103491; SSF103491; 1.
DR PROSITE; PS00756; SECY_2; 1.
PE 3: Inferred from homology;
KW Chloroplast; Membrane; Plastid; Protein transport; Reference proteome;
KW Thylakoid; Translocation; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..340
FT /note="Protein translocase subunit SecY"
FT /id="PRO_0000414216"
FT TRANSMEM 10..30
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01465"
FT TRANSMEM 42..62
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01465"
FT TRANSMEM 106..126
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01465"
FT TRANSMEM 152..172
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01465"
FT TRANSMEM 204..224
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01465"
FT TRANSMEM 225..245
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01465"
FT TRANSMEM 282..302
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01465"
FT TRANSMEM 304..324
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01465"
SQ SEQUENCE 340 AA; 38022 MW; 5BD6AB333913FB0B CRC64;
MQDNWPTRLA ITCLLVAIER LGMYIPVGLI SNPQANWLNG GGWFVLGIIP TINASIVMQI
LISIVPALTR LQKEEGEMGQ KQIQKYTRYL TFFLAGIQAF TLSQQWCTWL LIVSGAMLVM
WLAEQMTHKG IGNGTSIFVC SNIAANFLHH PIEAPWSLAM VVLIFTMLGM IALQEAVRAI
PILSAKQLIQ SIAQVYLLPM RLNQGGVMPI IFASSTLALL HTWSIWWLYV ACIIFFSHFY
NLVIANPKEL SENLNKMAVV IPSIRPGAET QQYLNRTLNR MSWIGGIALS LIALLPWLFS
SLKIFSGFGA TSLLIVIGVS IDTMRQIRTY FIANAYEKMI