ID SEC11_AJECN Reviewed; 187 AA.
AC A6QX24;
DT 21-SEP-2011, integrated into UniProtKB/Swiss-Prot.
DT 21-AUG-2007, sequence version 1.
DT 06-MAR-2013, entry version 33.
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=HCAG_01931;
OS Ajellomyces capsulata (strain NAm1 / WU24) (Darling's disease fungus)
OS (Histoplasma capsulatum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Ajellomycetaceae; Ajellomyces.
OX NCBI_TaxID=339724;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NAm1 / WU24;
RX PubMed=19717792; DOI=10.1101/gr.087551.108;
RA Sharpton T.J., Stajich J.E., Rounsley S.D., Gardner M.J.,
RA Wortman J.R., Jordar V.S., Maiti R., Kodira C.D., Neafsey D.E.,
RA Zeng Q., Hung C.-Y., McMahan C., Muszewska A., Grynberg M.,
RA Mandel M.A., Kellner E.M., Barker B.M., Galgiani J.N., Orbach M.J.,
RA Kirkland T.N., Cole G.T., Henn M.R., Birren B.W., Taylor J.W.;
RT "Comparative genomic analyses of the human fungal pathogens
RT Coccidioides and their relatives.";
RL Genome Res. 19:1722-1731(2009).
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; CH476655; EDN04066.1; -; Genomic_DNA.
DR RefSeq; XP_001544884.1; XM_001544834.1.
DR MEROPS; S26.010; -.
DR GeneID; 5450828; -.
DR KEGG; aje:HCAG_01931; -.
DR KO; K13280; -.
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 1 187 Signal peptidase complex catalytic
FT subunit SEC11.
FT /FTId=PRO_0000412309.
FT TOPO_DOM 1 18 Cytoplasmic (Potential).
FT TRANSMEM 19 39 Helical; Signal-anchor for type II
FT membrane protein; (Potential).
FT TOPO_DOM 40 187 Lumenal (Potential).
FT ACT_SITE 53 53 By similarity.
FT CARBOHYD 125 125 N-linked (GlcNAc...) (Potential).
SQ SEQUENCE 187 AA; 20634 MW; 3A0A1CD1BB457D4E CRC64;
MLSSLSPYMA NPRNTLSQVL NFGLVLSSAF MVWKALSVIT NSASPVVVVL SGSMEPAFQR
GDLLFLWNRS PRVDVGEIVV YNVQGKDIPI VHRVMRVFPD VPTTGAKDVE GVEASQKLLT
KGDNNLSDDT ELYAPGQEFL DRKTDLMGSV RGYVPAIGYV TIMLSEHPWL KSVLLGFMGL
MVMLQRE
//
