SECY_CYAPA
ID SECY_CYAPA Reviewed; 492 AA.
AC P25014;
DT 01-MAR-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 2.
DT 25-MAY-2022, entry version 86.
DE RecName: Full=Protein translocase subunit SecY;
GN Name=secY;
OS Cyanophora paradoxa.
OG Plastid; Cyanelle.
OC Eukaryota; Glaucocystophyceae; Cyanophoraceae; Cyanophora.
OX NCBI_TaxID=2762;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2126059; DOI=10.1007/bf00271555;
RA Michalowski C.B., Pfanzagl B., Loeffelhardt W., Bohnert H.J.;
RT "The cyanelle S10 spc ribosomal protein gene operon from Cyanophora
RT paradoxa.";
RL Mol. Gen. Genet. 224:222-231(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UTEX LB 555 / Pringsheim;
RA Stirewalt V.L., Michalowski C.B., Loeffelhardt W., Bohnert H.J.,
RA Bryant D.A.;
RT "Nucleotide sequence of the cyanelle DNA from Cyanophora paradoxa.";
RL Plant Mol. Biol. Rep. 13:327-332(1995).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UTEX LB 555 / Pringsheim;
RA Loeffelhardt W., Stirewalt V.L., Michalowski C.B., Annarella M.,
RA Farley J.Y., Schluchter W.M., Chung S., Newmann-Spallart C., Steiner J.M.,
RA Jakowitsch J., Bohnert H.J., Bryant D.A.;
RT "The complete sequence of the cyanelle genome of Cyanophora paradoxa: the
RT genetic complexity of a primitive plastid.";
RL (In) Schenk H.E.A., Herrmann R., Jeon K.W., Mueller N.E., Schwemmler W.
RL (eds.);
RL Eukaryotism and symbiosis, pp.40-48, Springer-Verlag, Heidelberg (1997).
RN [4]
RP SUBCELLULAR LOCATION.
RC STRAIN=UTEX LB 555 / Pringsheim;
RX PubMed=18976493; DOI=10.1186/1471-2148-8-304;
RA Yusa F., Steiner J.M., Loffelhardt W.;
RT "Evolutionary conservation of dual Sec translocases in the cyanelles of
RT Cyanophora paradoxa.";
RL BMC Evol. Biol. 8:304-304(2008).
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 Sec protein translocase complex, which is
CC composed of at least SecY and SecE. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Plastid, cyanelle thylakoid membrane
CC {ECO:0000269|PubMed:18976493}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:18976493}. Plastid, cyanelle inner membrane
CC {ECO:0000269|PubMed:18976493}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:18976493}.
CC -!- SIMILARITY: Belongs to the SecY/SEC61-alpha family. {ECO:0000305}.
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DR EMBL; M30487; AAA63630.1; -; Genomic_DNA.
DR EMBL; U30821; AAA81218.1; -; Genomic_DNA.
DR PIR; T06875; T06875.
DR RefSeq; NP_043187.1; NC_001675.1.
DR AlphaFoldDB; P25014; -.
DR TCDB; 3.A.5.6.1; the general secretory pathway (sec) family.
DR GeneID; 801593; -.
DR GO; GO:0036012; C:cyanelle inner membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0033115; C:cyanelle thylakoid membrane; IDA:UniProtKB.
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 Cyanelle; Membrane; Plastid; Plastid inner membrane; Protein transport;
KW Thylakoid; Translocation; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..492
FT /note="Protein translocase subunit SecY"
FT /id="PRO_0000131774"
FT TRANSMEM 1..21
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 54..74
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 96..116
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 159..179
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 183..203
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 206..226
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 247..267
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 303..323
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 357..377
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 409..429
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 435..455
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 468..492
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 472..492
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 492 AA; 55927 MW; 8736219112EBFC0D CRC64;
MLSRLIISIF IIFETIYLQI FKPVNKTFKQ GEAKLKRTLQ TLQSRELSEI RKRAISTLCL
IFLIRIGTFL PIPGTALNFD LESFQQNNSR NELANILNLL SGGAFLEIGF FTLGILPYMN
ASFFLQVLTK ILPSLERFQK EQEEIAQREF KKWTRYLTVI WAFIQSIVIS WIWIRPYALN
WDFFLGLKVV VALTLGAVIV MIIAEQITEI GLTNGSSLLI FINIIARIPN SIEQLFNSNI
NWTFPMISSL ILSLSLSFIT MFVIIGLQES GRPVPVLIAR QEAERQKFNE PITEAERRKT
QAYIFFQLLP AGIMPVIFAS TIFDLALPAF TNFLLQQGNW GYQLIKSFPF NSLFKDFCYL
ITIMLFSSNY ALTIMINPKT LAENLNSMNA LIPGVRPGSE TKVYSEQLIH RLNFIGSFVL
ALVCILPSIV ERSLGLPKLQ ILSPVSISIA LGVAVDTTRR ITSYLGSSSP FKRDSSKREP
LKRDFSKRRS AN
