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Database: UniProt
Entry: C5JJG5
LinkDB: C5JJG5
Original site: C5JJG5 
ID   SEC11_BLAGS             Reviewed;         196 AA.
AC   C5JJG5; A0A179UKU1;
DT   21-SEP-2011, integrated into UniProtKB/Swiss-Prot.
DT   10-MAY-2017, sequence version 2.
DT   10-MAY-2017, entry version 40.
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   Blastomyces gilchristii (strain SLH14081) (Blastomyces dermatitidis).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Ajellomycetaceae; Blastomyces.
OX   NCBI_TaxID=559298;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SLH14081;
RX   PubMed=26439490; DOI=10.1371/journal.pgen.1005493;
RA   Munoz J.F., Gauthier G.M., Desjardins C.A., Gallo J.E., Holder J.,
RA   Sullivan T.D., Marty A.J., Carmen J.C., Chen Z., Ding L., Gujja S.,
RA   Magrini V., Misas E., Mitreva M., Priest M., Saif S., Whiston E.A.,
RA   Young S., Zeng Q., Goldman W.E., Mardis E.R., Taylor J.W.,
RA   McEwen J.G., Clay O.K., Klein B.S., Cuomo C.A.;
RT   "The dynamic genome and transcriptome of the human fungal pathogen
RT   Blastomyces and close relative Emmonsia.";
RL   PLoS Genet. 11:E1005493-E1005493(2015).
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}; Single-pass type II membrane protein {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the peptidase S26B family. {ECO:0000305}.
DR   EMBL; GG657451; OAT07022.1; -; Genomic_DNA.
DR   RefSeq; XP_002626952.1; XM_002626906.1.
DR   STRING; 559298.XP_002626952.1; -.
DR   MEROPS; S26.010; -.
DR   EnsemblFungi; EEQ76605; EEQ76605; BDBG_03129.
DR   GeneID; 8505908; -.
DR   eggNOG; KOG3342; Eukaryota.
DR   eggNOG; COG0681; LUCA.
DR   OrthoDB; EOG092C4ZUJ; -.
DR   Proteomes; UP000002038; Unassembled WGS sequence.
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   InterPro; IPR019756; Pept_S26A_signal_pept_1_Ser-AS.
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; Reference proteome; Signal-anchor; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN         1    196       Signal peptidase complex catalytic
FT                                subunit SEC11.
FT                                /FTId=PRO_0000412311.
FT   TOPO_DOM      1     14       Cytoplasmic. {ECO:0000255}.
FT   TRANSMEM     15     33       Helical; Signal-anchor for type II
FT                                membrane protein. {ECO:0000255}.
FT   TOPO_DOM     34    196       Lumenal. {ECO:0000255}.
FT   ACT_SITE     53     53       {ECO:0000250}.
FT   CARBOHYD    134    134       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
SQ   SEQUENCE   196 AA;  21870 MW;  0241AEE6D61FC5AE CRC64;
     MLSSLSPYMA NPRQTFTQVL NFALVLSTAF MLWKGLSVYT NSASPIVVVL SGSMEPAFQR
     GDLLFLWNRS PRVDVGEIVV YNVRGKDIPI VHRVMRTFPD VPGKDKTKKG GKQDVEASPS
     SLESQKLLTK GDNNLSDDTE LYARGQDYLD RKEDIVGSVR GYIPAVGYVT IMLSEHPWLK
     SVLLGFMGLM VILQRE
//
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