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Database: UniProt
Entry: E7R7C4
LinkDB: E7R7C4
Original site: E7R7C4 
ID   SEC11_OGAPD             Reviewed;         176 AA.
AC   E7R7C4; W1QE96;
DT   21-SEP-2011, integrated into UniProtKB/Swiss-Prot.
DT   05-APR-2011, sequence version 1.
DT   01-OCT-2014, entry version 22.
DE   RecName: Full=Signal peptidase complex catalytic subunit SEC11;
DE            EC=3.4.21.89;
DE   AltName: Full=Signal peptidase I;
GN   Name=SEC11; ORFNames=HPODL_04472;
OS   Ogataea parapolymorpha (strain DL-1 / ATCC 26012 / NRRL Y-7560)
OS   (Yeast) (Hansenula polymorpha).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
OC   Saccharomycetes; Saccharomycetales; Saccharomycetales incertae sedis;
OC   Ogataea.
OX   NCBI_TaxID=871575;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 26012 / NRRL Y-7560 / DL-1;
RX   PubMed=24279325; DOI=10.1186/1471-2164-14-837;
RA   Ravin N.V., Eldarov M.A., Kadnikov V.V., Beletsky A.V., Schneider J.,
RA   Mardanova E.S., Smekalova E.M., Zvereva M.I., Dontsova O.A.,
RA   Mardanov A.V., Skryabin K.G.;
RT   "Genome sequence and analysis of methylotrophic yeast Hansenula
RT   polymorpha DL1.";
RL   BMC Genomics 14:837-837(2013).
CC   -!- FUNCTION: Catalytic component of the signal peptidase complex
CC       (SPC), which catalyzes the cleavage of N-terminal signal sequences
CC       of proteins targeted to the endoplasmic reticulum. Signal peptide
CC       cleavage occurs during the translocation (cotranslationally or
CC       post-translationally) through the translocon pore into the
CC       endoplasmic reticulum (By similarity). {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY: Cleavage of hydrophobic, N-terminal signal or
CC       leader sequences from secreted and periplasmic proteins.
CC   -!- SUBUNIT: Component of the signal peptidase complex (SPC).
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC       {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the peptidase S26B family. {ECO:0000305}.
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DR   EMBL; AEOI02000008; ESW98869.1; -; Genomic_DNA.
DR   MEROPS; S26.010; -.
DR   OrthoDB; EOG7BCNQ4; -.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0008236; F:serine-type peptidase activity; IEA:InterPro.
DR   GO; GO:0006465; P:signal peptide processing; IEA:InterPro.
DR   Gene3D; 2.10.109.10; -; 1.
DR   InterPro; IPR019756; Pept_S26A_signal_pept_1_Ser-AS.
DR   InterPro; IPR028360; Peptidase_S24/S26_b-rbn.
DR   InterPro; IPR019759; Peptidase_S24_S26.
DR   InterPro; IPR015927; Peptidase_S24_S26A/B/C.
DR   InterPro; IPR001733; Peptidase_S26B.
DR   PANTHER; PTHR10806; PTHR10806; 1.
DR   Pfam; PF00717; Peptidase_S24; 1.
DR   PRINTS; PR00728; SIGNALPTASE.
DR   SUPFAM; SSF51306; SSF51306; 1.
DR   TIGRFAMs; TIGR02228; sigpep_I_arch; 1.
DR   PROSITE; PS00501; SPASE_I_1; 1.
PE   3: Inferred from homology;
KW   Complete proteome; Endoplasmic reticulum; Hydrolase; Membrane;
KW   Protease; Reference proteome; Signal-anchor; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN         1    176       Signal peptidase complex catalytic
FT                                subunit SEC11.
FT                                /FTId=PRO_0000412349.
FT   TOPO_DOM      1      9       Cytoplasmic. {ECO:0000255}.
FT   TRANSMEM     10     30       Helical. {ECO:0000255}.
FT   TOPO_DOM     31    138       Lumenal. {ECO:0000255}.
FT   TRANSMEM    139    159       Helical. {ECO:0000255}.
FT   TOPO_DOM    160    176       Cytoplasmic. {ECO:0000255}.
FT   ACT_SITE     44     44       {ECO:0000250}.
SQ   SEQUENCE   176 AA;  20150 MW;  1E2B9D861EA9AD51 CRC64;
     MNLRQQLGSG LSMAMVLASA FAFWKLFSIV TMSNSPIVVV LSGSMEPAFQ RGDVLFLWNR
     EEYVGVGDVV VYKLQEKDIP IVHRVVREHR VMEKDRKTKK KVQKQLLLTK GDNNERDDLP
     LYAYGQQYLE RKKDILGRVF GYVPLVGYVT ILITENVYFK YALMALLGLS ALVQDE
//
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