SECY_GUITH
ID SECY_GUITH Reviewed; 420 AA.
AC P28527;
DT 01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 2.
DT 25-MAY-2022, entry version 107.
DE RecName: Full=Protein translocase subunit SecY;
GN Name=secY;
OS Guillardia theta (Cryptophyte) (Cryptomonas phi).
OG Plastid; Chloroplast.
OC Eukaryota; Cryptophyceae; Pyrenomonadales; Geminigeraceae; Guillardia.
OX NCBI_TaxID=55529;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1544427; DOI=10.1016/0014-5793(92)80029-g;
RA Douglas S.E.;
RT "A secY homologue is found in the plastid genome of Cryptomonas phi.";
RL FEBS Lett. 298:93-96(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=9137835; DOI=10.1080/15216549700202101;
RA Wang S.L., Liu X.-Q., Douglas S.E.;
RT "The large ribosomal protein gene cluster of a cryptomonad plastid: gene
RT organization, sequence and evolutionary implications.";
RL Biochem. Mol. Biol. Int. 41:1035-1044(1997).
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; AF041468; AAC35720.1; -; Genomic_DNA.
DR RefSeq; NP_050786.1; NC_000926.1.
DR AlphaFoldDB; P28527; -.
DR SMR; P28527; -.
DR GeneID; 857094; -.
DR HOGENOM; CLU_030313_0_0_1; -.
DR OMA; FAMWLGE; -.
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; 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..420
FT /note="Protein translocase subunit SecY"
FT /id="PRO_0000131775"
FT TRANSMEM 17..37
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 58..78
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 117..137
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 141..161
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 170..190
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 203..223
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 259..279
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 300..320
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 357..377
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 378..398
FT /note="Helical"
FT /evidence="ECO:0000255"
SQ SEQUENCE 420 AA; 46937 MW; 7967611DB9EF59F6 CRC64;
MNTSIKSIKK QDLKDRIVFT LFLIVMSRLG TFLPIPGVDH DAFYQSIISN PLVNFLNVFS
GGGFASIGVF ALGIVPYINA SIIVQLATNS IPSLEKLQKE EGELGRQKIV QLTRYVALVW
ALIQSIGVSF WVRPYVFNWD LNFVFAMSLT LTIGSMLIMW FSEQITEKGI GNGPSLLIFI
NIISGLPKLL QSQIQSTRLN IQALDIFVLV FIFSVMIIGI IFIQEGIKRI PIISARQLGK
GQMDNKTSYL PLKLNQSGVM PIIFASAVLV LPAYLAQLVS NEQLRTVLHL FDGTSNNKLL
YLLFYFTLIL FFSYFYTSLI LNPNDVSKNL KKMESSIYGV RPGKATTEYL QKTLNRLTFL
GALFLAFIAI VPNIIETLTN LSVFKGLGGT SLLIIVGVQV DTSKQIQTYL ISKNYETIVR