SECY_PYRSA
ID SECY_PYRSA Reviewed; 412 AA.
AC P38397;
DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1994, sequence version 1.
DT 25-MAY-2022, entry version 81.
DE RecName: Full=Protein translocase subunit SecY {ECO:0000255|HAMAP-Rule:MF_01465};
DE Flags: Fragment;
GN Name=secY {ECO:0000255|HAMAP-Rule:MF_01465};
OS Pyrenomonas salina.
OG Plastid; Chloroplast.
OC Eukaryota; Cryptophyceae; Pyrenomonadales; Pyrenomonadaceae; Pyrenomonas.
OX NCBI_TaxID=3034;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=7820283; DOI=10.1006/mpev.1994.1021;
RA Rensing S.A., Maier U.-G.;
RT "The SecY protein family: comparative analysis and phylogenetic
RT relationships.";
RL Mol. Phylogenet. Evol. 3:187-191(1994).
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. {ECO:0000255|HAMAP-Rule:MF_01465}.
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}.
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DR EMBL; X74773; CAA52783.1; -; Genomic_DNA.
DR AlphaFoldDB; P38397; -.
DR SMR; P38397; -.
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:0015031; P:protein transport; IEA:UniProtKB-KW.
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; 1.
DR Pfam; PF00344; SecY; 1.
DR PIRSF; PIRSF004557; SecY; 1.
DR SUPFAM; SSF103491; SSF103491; 1.
DR TIGRFAMs; TIGR00967; 3a0501s007; 1.
DR PROSITE; PS00755; SECY_1; 1.
DR PROSITE; PS00756; SECY_2; 1.
PE 3: Inferred from homology;
KW Chloroplast; Membrane; Plastid; Protein transport; Thylakoid;
KW Translocation; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..>412
FT /note="Protein translocase subunit SecY"
FT /id="PRO_0000131779"
FT TRANSMEM 17..37
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01465"
FT TRANSMEM 58..78
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01465"
FT TRANSMEM 117..137
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01465"
FT TRANSMEM 143..163
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01465"
FT TRANSMEM 170..190
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01465"
FT TRANSMEM 251..271
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01465"
FT TRANSMEM 293..313
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01465"
FT TRANSMEM 350..370
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01465"
FT TRANSMEM 372..392
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01465"
FT NON_TER 412
SQ SEQUENCE 412 AA; 45869 MW; 79763DB2CBE6B90D CRC64;
MESIRRNSRK EGIKERIFLT IGLLVLSRLG TFIPVPGVDH DAFYQSISTN PIVTFLNIFS
GGGFASIGIF ALGIVPYINA SIVIQLATTS IPNLEKLQKE EGEAGRQKIS QITRYRALGW
AAIQSLGVSF WVRPYVFNWD SQFVVQMTLA LTTGSMLIMW FSEQITEKGI GNGPSLLIFI
NIIAGLPKLI QQKSNAISST NQTTELVVLA SISVYDSRIF IRDRRYYILQ TVGRHCKQTS
YLPLRLNQGG VMPIIFASAI LVLPAYLGQV IQNQFVLKLV TLLSPNSSDK NLYLIFYFSL
ILFFSYFYAS LIINPNDVSQ NLKKMESSIP GVRPGKATTD YLQKTLNRLT FLGALFLAFI
AVVPSIIENI TSISTFKGLG ATSLLILVGV AIDTSRQIQT YLISRNYENI MK