ID SEC11_PICAD Reviewed; 176 AA.
AC E7R7C4;
DT 21-SEP-2011, integrated into UniProtKB/Swiss-Prot.
DT 05-APR-2011, sequence version 1.
DT 29-MAY-2013, entry version 14.
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_2505;
OS Pichia angusta (strain ATCC 26012 / NRRL Y-7560 / DL-1) (Yeast)
OS (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;
RA Ravin N.V., Mardanov A.V., Eldarov M.A., Kadnikov V.V., Beletsky A.V.,
RA Zvereva M.I., Smekalova E.M., Dontsova O.A., Skryabin K.G.;
RT "Genome sequence of the methylotrophic yeast Hansenula polymorpha
RT DL1.";
RL Submitted (JAN-2011) to the EMBL/GenBank/DDBJ databases.
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).
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) (By
CC similarity).
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass
CC membrane protein (By similarity).
CC -!- SIMILARITY: Belongs to the peptidase S26B family.
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DR EMBL; AEOI01000009; EFW96222.1; -; Genomic_DNA.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR GO; GO:0008236; F:serine-type peptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
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; IPR019759; Peptidase_S24_S26.
DR InterPro; IPR015927; Peptidase_S24_S26A/B/C.
DR InterPro; IPR011056; Peptidase_S24_S26A/B/C_b-rbn.
DR InterPro; IPR001733; Peptidase_S26B.
DR InterPro; IPR027245; Sec11-like.
DR PANTHER; PTHR10806; PTHR10806; 1.
DR PANTHER; PTHR10806:SF2; PTHR10806:SF2; 1.
DR Pfam; PF00717; Peptidase_S24; 1.
DR PRINTS; PR00728; SIGNALPTASE.
DR SUPFAM; SSF51306; Pept_S24_S26_C; 1.
DR TIGRFAMs; TIGR02228; sigpep_I_arch; 1.
DR PROSITE; PS00501; SPASE_I_1; 1.
DR PROSITE; PS00761; SPASE_I_3; FALSE_NEG.
PE 3: Inferred from homology;
KW Complete proteome; Endoplasmic reticulum; Hydrolase; Membrane;
KW Protease; Signal-anchor; Transmembrane; Transmembrane helix.
FT CHAIN 1 176 Signal peptidase complex catalytic
FT subunit SEC11.
FT /FTId=PRO_0000412349.
FT TOPO_DOM 1 9 Cytoplasmic (Potential).
FT TRANSMEM 10 30 Helical; (Potential).
FT TOPO_DOM 31 138 Lumenal (Potential).
FT TRANSMEM 139 159 Helical; (Potential).
FT TOPO_DOM 160 176 Cytoplasmic (Potential).
FT ACT_SITE 44 44 By similarity.
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
//
