ID A0A0N1IAJ6_LEPSE Unreviewed; 180 AA.
AC A0A0N1IAJ6;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 27-MAR-2024, entry version 33.
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 complex catalytic subunit sec11 {ECO:0000256|ARBA:ARBA00021755};
GN ORFNames=ABL78_0227 {ECO:0000313|EMBL:KPI90631.1};
OS Leptomonas seymouri.
OC Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC Trypanosomatida; Trypanosomatidae; Leishmaniinae; Leptomonas.
OX NCBI_TaxID=5684 {ECO:0000313|EMBL:KPI90631.1, ECO:0000313|Proteomes:UP000038009};
RN [1] {ECO:0000313|EMBL:KPI90631.1, ECO:0000313|Proteomes:UP000038009}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 30220 {ECO:0000313|EMBL:KPI90631.1,
RC ECO:0000313|Proteomes:UP000038009};
RX PubMed=26317207;
RA Kraeva N., Butenko A., Hlavacova J., Kostygov A., Myskova J., Grybchuk D.,
RA Lestinova T., Votypka J., Volf P., Opperdoes F., Flegontov P., Lukes J.,
RA Yurchenko V.;
RT "Leptomonas seymouri: Adaptations to the Dixenous Life Cycle Analyzed by
RT Genome Sequencing, Transcriptome Profiling and Co-infection with Leishmania
RT donovani.";
RL PLoS Pathog. 11:E1005127-E1005127(2015).
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 -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000256|ARBA:ARBA00004648}; Single-pass type II membrane protein
CC {ECO:0000256|ARBA:ARBA00004648}.
CC -!- SIMILARITY: Belongs to the peptidase S26B family.
CC {ECO:0000256|ARBA:ARBA00011035}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KPI90631.1}.
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DR EMBL; LJSK01000003; KPI90631.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0N1IAJ6; -.
DR EnsemblProtists; KPI90631; KPI90631; ABL78_0227.
DR VEuPathDB; TriTrypDB:Lsey_0003_0240; -.
DR OMA; DNNHIDD; -.
DR OrthoDB; 1114626at2759; -.
DR Proteomes; UP000038009; 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; 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 PRINTS; PR00728; SIGNALPTASE.
DR SUPFAM; SSF51306; LexA/Signal peptidase; 1.
PE 3: Inferred from homology;
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 16..40
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 147..175
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
SQ SEQUENCE 180 AA; 20525 MW; E5A9889BB6F501BE CRC64;
MQDIIENILS LRRRDVIHVV TTTAFFLSII LVAWCATTLY TSCDAPIVVV LSGSMEPGYY
RGDVLLLHSV KQYPAEVGDI IVYSLSERSI PIVHRVHRIH QRAEDGKRFY LTKGDNNVHD
DDFLFKGGRQ WLEEDMIIGK TFAYVPLIGY LTIAFNEVFI IKYICLVLIA VLLLASNDEF
//
