ID A0A0J8U6W2_COCIT Unreviewed; 179 AA.
AC A0A0J8U6W2;
DT 14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT 14-OCT-2015, sequence version 1.
DT 27-MAR-2024, entry version 41.
DE RecName: Full=Signal peptidase complex catalytic subunit SEC11 {ECO:0000256|ARBA:ARBA00019685};
DE EC=3.4.21.89 {ECO:0000256|ARBA:ARBA00013208};
DE AltName: Full=Signal peptidase I {ECO:0000256|ARBA:ARBA00033305};
DE AltName: Full=Signal peptidase complex catalytic subunit sec11 {ECO:0000256|ARBA:ARBA00021755};
GN ORFNames=CIHG_00545 {ECO:0000313|EMBL:KMU82763.1};
OS Coccidioides immitis H538.4.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Onygenaceae; Coccidioides.
OX NCBI_TaxID=396776 {ECO:0000313|EMBL:KMU82763.1, ECO:0000313|Proteomes:UP000054563};
RN [1] {ECO:0000313|Proteomes:UP000054563}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=H538.4 {ECO:0000313|Proteomes:UP000054563};
RX PubMed=20516208; DOI=10.1101/gr.103911.109;
RA Neafsey D.E., Barker B.M., Sharpton T.J., Stajich J.E., Park D.J.,
RA Whiston E., Hung C.-Y., McMahan C., White J., Sykes S., Heiman D.,
RA Young S., Zeng Q., Abouelleil A., Aftuck L., Bessette D., Brown A.,
RA FitzGerald M., Lui A., Macdonald J.P., Priest M., Orbach M.J.,
RA Galgiani J.N., Kirkland T.N., Cole G.T., Birren B.W., Henn M.R.,
RA Taylor J.W., Rounsley S.D.;
RT "Population genomic sequencing of Coccidioides fungi reveals recent
RT hybridization and transposon control.";
RL Genome Res. 20:938-946(2010).
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. {ECO:0000256|ARBA:ARBA00029411}.
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:0000256|ARBA:ARBA00000677};
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.
CC {ECO:0000256|ARBA:ARBA00029478}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000256|ARBA:ARBA00004648}; Single-pass type II membrane protein
CC {ECO:0000256|ARBA:ARBA00004648}. Membrane
CC {ECO:0000256|ARBA:ARBA00004606}; Single-pass type II membrane protein
CC {ECO:0000256|ARBA:ARBA00004606}.
CC -!- SIMILARITY: Belongs to the peptidase S26B family.
CC {ECO:0000256|ARBA:ARBA00011035}.
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DR EMBL; DS016981; KMU82763.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0J8U6W2; -.
DR STRING; 396776.A0A0J8U6W2; -.
DR VEuPathDB; FungiDB:CIHG_00545; -.
DR Proteomes; UP000054563; Unassembled WGS sequence.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-EC.
DR GO; GO:0006465; P:signal peptide processing; IEA:InterPro.
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 NCBIfam; TIGR02228; sigpep_I_arch; 1.
DR PANTHER; PTHR10806; SIGNAL PEPTIDASE COMPLEX CATALYTIC SUBUNIT SEC11; 1.
DR PANTHER; PTHR10806:SF6; SIGNAL PEPTIDASE COMPLEX CATALYTIC SUBUNIT SEC11; 1.
DR SUPFAM; SSF51306; LexA/Signal peptidase; 1.
DR PROSITE; PS00501; SPASE_I_1; 1.
PE 3: Inferred from homology;
KW Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00022824};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022670};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000054563};
KW Signal-anchor {ECO:0000256|ARBA:ARBA00022968};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}.
SQ SEQUENCE 179 AA; 19633 MW; 77A6F750E3647369 CRC64;
MLAGLSPHLS NLRRSLTQVL NFALVLSTAF MMWKGLSIYT NSSSPIVVVL SGSMEPAFQR
GDLLFLWNRS PRAEVGEIVV YNVRGKDIPI VHRVVRAFGD DEKSPKETNG QKKKKVMSSG
KKDSIAAGAL HSDSALVSHR ILTRATIILL MIRSYMLKGR IILTGTGLGG QCTRVYSCN
//
