ID A0A087SM88_AUXPR Unreviewed; 181 AA.
AC A0A087SM88;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 36.
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=F751_0774 {ECO:0000313|EMBL:KFM26842.1}, g.2947
GN {ECO:0000313|EMBL:JAT74173.1};
OS Auxenochlorella protothecoides (Green microalga) (Chlorella
OS protothecoides).
OC Eukaryota; Viridiplantae; Chlorophyta; core chlorophytes; Trebouxiophyceae;
OC Chlorellales; Chlorellaceae; Auxenochlorella.
OX NCBI_TaxID=3075 {ECO:0000313|EMBL:KFM26842.1, ECO:0000313|Proteomes:UP000028924};
RN [1] {ECO:0000313|EMBL:KFM26842.1, ECO:0000313|Proteomes:UP000028924}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=0710 {ECO:0000313|EMBL:KFM26842.1,
RC ECO:0000313|Proteomes:UP000028924};
RX PubMed=25012212; DOI=10.1186/1471-2164-15-582;
RA Gao C., Wang Y., Shen Y., Yan D., He X., Dai J., Wu Q.;
RT "Oil accumulation mechanisms of the oleaginous microalga Chlorella
RT protothecoides revealed through its genome, transcriptomes, and
RT proteomes.";
RL BMC Genomics 15:582-582(2014).
RN [2] {ECO:0000313|EMBL:JAT74173.1}
RP NUCLEOTIDE SEQUENCE.
RA Babu N.S., Beckwith C.J., Beseler K.G., Brison A., Carone J.V.,
RA Caskin T.P., Diamond M., Durham M.E., Foxe J.M., Go M., Henderson B.A.,
RA Jones I.B., McGettigan J.A., Micheletti S.J., Nasrallah M.E., Ortiz D.,
RA Piller C.R., Privatt S.R., Schneider S.L., Sharp S., Smith T.C.,
RA Stanton J.D., Ullery H.E., Wilson R.J., Serrano M.G., Buck G., Lee V.,
RA Wang Y., Carvalho R., Voegtly L., Shi R., Duckworth R., Johnson A.,
RA Loviza R., Walstead R., Shah Z., Kiflezghi M., Wade K., Ball S.L.,
RA Bradley K.W., Asai D.J., Bowman C.A., Russell D.A., Pope W.H.,
RA Jacobs-Sera D., Hendrix R.W., Hatfull G.F.;
RL Submitted (AUG-2015) to the EMBL/GenBank/DDBJ databases.
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}. 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}.
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; GDKF01004449; JAT74173.1; -; Transcribed_RNA.
DR EMBL; KL662135; KFM26842.1; -; Genomic_DNA.
DR RefSeq; XP_011399790.1; XM_011401488.1.
DR STRING; 3075.A0A087SM88; -.
DR GeneID; 23612165; -.
DR KEGG; apro:F751_0774; -.
DR eggNOG; KOG3342; Eukaryota.
DR OrthoDB; 1114626at2759; -.
DR Proteomes; UP000028924; 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 Gene3D; 2.10.109.10; Umud Fragment, subunit A; 1.
DR InterPro; IPR036286; LexA/Signal_pep-like_sf.
DR InterPro; IPR019758; Pept_S26A_signal_pept_1_CS.
DR InterPro; IPR015927; Peptidase_S24_S26A/B/C.
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 Pfam; PF00717; Peptidase_S24; 1.
DR PRINTS; PR00728; SIGNALPTASE.
DR SUPFAM; SSF51306; LexA/Signal peptidase; 1.
DR PROSITE; PS00761; SPASE_I_3; 1.
PE 3: Inferred from homology;
KW Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00022824};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000028924};
KW Signal-anchor {ECO:0000256|ARBA:ARBA00022968};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 20..40
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 161..178
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 42..105
FT /note="Peptidase S24/S26A/S26B/S26C"
FT /evidence="ECO:0000259|Pfam:PF00717"
SQ SEQUENCE 181 AA; 20264 MW; 0D34F07B60F69BD6 CRC64;
MQLIRSAVAE VKKMQKRQLL LQGVNLGLII TSALMIWKFL VLVTGSESPI VVVLSGSMEP
GFYRGDILFL DQPKGPIETG NIIVFNAGDR EIPIVHRIIK VHERHNNISA VDILTKGDNN
WGDDRSLYPR GVRWLGRHHI MGRVIGYLPY IGQVTIIMND YPIVKVLLIA ALGLFVITSK
E
//
