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Database: UniProt
Entry: C5JJG5
LinkDB: C5JJG5
Original site: C5JJG5 
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   19-FEB-2014, entry version 25.
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   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: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; 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; 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
//
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