ID SEC11_AJEDS Reviewed; 188 AA.
AC C5JJG5;
DT 21-SEP-2011, integrated into UniProtKB/Swiss-Prot.
DT 28-JUL-2009, sequence version 1.
DT 06-MAR-2013, 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=BDBG_03129;
OS Ajellomyces dermatitidis (strain SLH14081) (Blastomyces dermatitidis).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Ajellomycetaceae; Ajellomyces.
OX NCBI_TaxID=559298;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SLH14081;
RA Champion M., Cuomo C.A., Ma L.-J., Henn M.R., Klein B., Goldman B.,
RA Young S.K., Kodira C.D., Zeng Q., Koehrsen M., Alvarado L.,
RA Berlin A.M., Heiman D.I., Hepburn T.A., Saif S., Shea T.D., Shenoy N.,
RA Sykes S., Galagan J.E., Nusbaum C., Birren B.W.;
RT "The genome sequence of Blastomyces dermatitidis strain SLH14081.";
RL Submitted (FEB-2009) 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; Single-pass
CC type II membrane protein (By similarity).
CC -!- SIMILARITY: Belongs to the peptidase S26B family.
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DR EMBL; GG657451; EEQ76605.1; -; Genomic_DNA.
DR RefSeq; XP_002626952.1; XM_002626906.1.
DR MEROPS; S26.010; -.
DR GeneID; 8505908; -.
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 PANTHER; PTHR10806; PTHR10806; 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; Glycoprotein; Hydrolase;
KW Membrane; Protease; Signal-anchor; Transmembrane; Transmembrane helix.
FT CHAIN 1 188 Signal peptidase complex catalytic
FT subunit SEC11.
FT /FTId=PRO_0000412311.
FT TOPO_DOM 1 6 Cytoplasmic (Potential).
FT TRANSMEM 7 25 Helical; Signal-anchor for type II
FT membrane protein; (Potential).
FT TOPO_DOM 26 188 Lumenal (Potential).
FT ACT_SITE 45 45 By similarity.
FT CARBOHYD 126 126 N-linked (GlcNAc...) (Potential).
SQ SEQUENCE 188 AA; 20991 MW; 36A4F4534B595FD4 CRC64;
MANPRQTFTQ VLNFALVLST AFMLWKGLSV YTNSASPIVV VLSGSMEPAF QRGDLLFLWN
RSPRVDVGEI VVYNVRGKDI PIVHRVMRTF PDVPGKDKTK KGGKQDVEAS PSSLESQKLL
TKGDNNLSDD TELYARGQDY LDRKEDIVGS VRGYIPAVGY VTIMLSEHPW LKSVLLGFMG
LMVILQRE
//
