SEC11_PARBA
ID SEC11_PARBA Reviewed; 197 AA.
AC C1GU90;
DT 21-SEP-2011, integrated into UniProtKB/Swiss-Prot.
DT 26-MAY-2009, sequence version 1.
DT 03-AUG-2022, entry version 67.
DE RecName: Full=Signal peptidase complex catalytic subunit SEC11;
DE EC=3.4.21.89 {ECO:0000250|UniProtKB:P15367};
DE AltName: Full=Signal peptidase I;
GN Name=SEC11; ORFNames=PAAG_02085;
OS Paracoccidioides lutzii (strain ATCC MYA-826 / Pb01) (Paracoccidioides
OS brasiliensis).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Onygenales incertae sedis; Paracoccidioides.
OX NCBI_TaxID=502779;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-826 / Pb01;
RX PubMed=22046142; DOI=10.1371/journal.pgen.1002345;
RA Desjardins C.A., Champion M.D., Holder J.W., Muszewska A., Goldberg J.,
RA Bailao A.M., Brigido M.M., Ferreira M.E., Garcia A.M., Grynberg M.,
RA Gujja S., Heiman D.I., Henn M.R., Kodira C.D., Leon-Narvaez H.,
RA Longo L.V.G., Ma L.-J., Malavazi I., Matsuo A.L., Morais F.V., Pereira M.,
RA Rodriguez-Brito S., Sakthikumar S., Salem-Izacc S.M., Sykes S.M.,
RA Teixeira M.M., Vallejo M.C., Walter M.E., Yandava C., Young S., Zeng Q.,
RA Zucker J., Felipe M.S., Goldman G.H., Haas B.J., McEwen J.G., Nino-Vega G.,
RA Puccia R., San-Blas G., Soares C.M., Birren B.W., Cuomo C.A.;
RT "Comparative genomic analysis of human fungal pathogens causing
RT paracoccidioidomycosis.";
RL PLoS Genet. 7:E1002345-E1002345(2011).
CC -!- FUNCTION: Catalytic component of the signal peptidase complex (SPC)
CC which catalyzes the cleavage of N-terminal signal sequences from
CC nascent proteins as they are translocated into the lumen of the
CC endoplasmic reticulum (By similarity). Specifically cleaves N-terminal
CC signal peptides that contain a hydrophobic alpha-helix (h-region)
CC shorter than 18-20 amino acids (By similarity).
CC {ECO:0000250|UniProtKB:P15367, ECO:0000250|UniProtKB:P67812}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Cleavage of hydrophobic, N-terminal signal or leader sequences
CC from secreted and periplasmic proteins.; EC=3.4.21.89;
CC Evidence={ECO:0000250|UniProtKB:P15367};
CC -!- SUBUNIT: Component of the signal peptidase complex (SPC) composed of a
CC catalytic subunit SEC11 and three accessory subunits SPC1, SPC2 and
CC SPC3 (By similarity). The complex induces a local thinning of the ER
CC membrane which is used to measure the length of the signal peptide (SP)
CC h-region of protein substrates. This ensures the selectivity of the
CC complex towards h-regions shorter than 18-20 amino acids (By
CC similarity). SPC associates with the translocon complex (By
CC similarity). {ECO:0000250|UniProtKB:P15367,
CC ECO:0000250|UniProtKB:P67812}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:P15367}; Single-pass type II membrane protein
CC {ECO:0000250|UniProtKB:P15367}.
CC -!- DOMAIN: The C-terminal short (CTS) helix is essential for catalytic
CC activity. It may be accommodated as a transmembrane helix in the
CC thinned membrane environment of the complex, similarly to the signal
CC peptide in the complex substrates. {ECO:0000250|UniProtKB:P67812}.
CC -!- SIMILARITY: Belongs to the peptidase S26B family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; KN293995; EEH39896.1; -; Genomic_DNA.
DR RefSeq; XP_002796197.1; XM_002796151.1.
DR AlphaFoldDB; C1GU90; -.
DR SMR; C1GU90; -.
DR STRING; 502779.C1GU90; -.
DR MEROPS; S26.010; -.
DR EnsemblFungi; EEH39896; EEH39896; PAAG_02085.
DR GeneID; 9099583; -.
DR KEGG; pbl:PAAG_02085; -.
DR VEuPathDB; FungiDB:PAAG_02085; -.
DR eggNOG; KOG3342; Eukaryota.
DR HOGENOM; CLU_089996_0_0_1; -.
DR OMA; YNVRGKD; -.
DR OrthoDB; 1486616at2759; -.
DR Proteomes; UP000002059; Partially assembled WGS sequence.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005787; C:signal peptidase complex; IEA:EnsemblFungi.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-EC.
DR GO; GO:0045047; P:protein targeting to ER; IEA:EnsemblFungi.
DR GO; GO:0006465; P:signal peptide processing; IEA:EnsemblFungi.
DR CDD; cd06530; S26_SPase_I; 1.
DR InterPro; IPR036286; LexA/Signal_pep-like_sf.
DR InterPro; IPR019756; Pept_S26A_signal_pept_1_Ser-AS.
DR InterPro; IPR019533; Peptidase_S26.
DR InterPro; IPR001733; Peptidase_S26B.
DR PANTHER; PTHR10806; PTHR10806; 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 Endoplasmic reticulum; Glycoprotein; Hydrolase; Membrane; Protease;
KW Reference proteome; Signal-anchor; Transmembrane; Transmembrane helix.
FT CHAIN 1..197
FT /note="Signal peptidase complex catalytic subunit SEC11"
FT /id="PRO_0000412345"
FT TOPO_DOM 1..14
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 15..33
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 34..197
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT REGION 102..134
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 183..194
FT /note="C-terminal short (CTS) helix"
FT /evidence="ECO:0000250|UniProtKB:P67812"
FT COMPBIAS 102..118
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 119..133
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 53
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:P15367"
FT ACT_SITE 92
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:P15367"
FT ACT_SITE 139
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:P15367"
FT CARBOHYD 41
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 197 AA; 21902 MW; 699C220EEDB24C50 CRC64;
MLSSLAPYMA NPRQTLTQVL NFALVLSTAF MLWKGLSVVT NSTSPIVVVL SGSMEPAFQR
GDLLFLWNRS PRVDVGEIVV YNVRGKDIPI VHRVMRSFPE LPGREDKKSV KKGGEEGEET
SSTPSQKLLT KGDNNMADDT ELYAQGQEYL DRKEDIVGSV RGYVPGVGYV TILLSEHPWL
RSVLLGFMGL MVVLQRE
