ID A0A061DDG4_BABBI Unreviewed; 183 AA.
AC A0A061DDG4;
DT 03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT 03-SEP-2014, sequence version 1.
DT 27-MAR-2024, entry version 44.
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=BBBOND_0301540 {ECO:0000313|EMBL:CDR96250.1};
OS Babesia bigemina.
OC Eukaryota; Sar; Alveolata; Apicomplexa; Aconoidasida; Piroplasmida;
OC Babesiidae; Babesia.
OX NCBI_TaxID=5866 {ECO:0000313|EMBL:CDR96250.1, ECO:0000313|Proteomes:UP000033188};
RN [1] {ECO:0000313|Proteomes:UP000033188}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bond {ECO:0000313|Proteomes:UP000033188};
RX PubMed=24799432; DOI=10.1093/nar/gku322;
RA Jackson A.P., Otto T.D., Darby A., Ramaprasad A., Xia D., Echaide I.E.,
RA Farber M., Gahlot S., Gamble J., Gupta D., Gupta Y., Jackson L.,
RA Malandrin L., Malas T.B., Moussa E., Nair M., Reid AJ., Sanders M.,
RA Sharma J., Tracey A., Quail M.A., Weir W., Wastling J.M., Hall N.,
RA Willadsen P., Lingelbach K., Shiels B., Tait A., Berriman M., Allred D.R.,
RA Pain A.;
RT "The evolutionary dynamics of variant antigen genes in Babesia reveal a
RT history of genomic innovation underlying host-parasite interaction.";
RL Nucleic Acids Res. 42:7113-7131(2014).
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}.
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DR EMBL; LK391709; CDR96250.1; -; Genomic_DNA.
DR RefSeq; XP_012768436.1; XM_012912982.1.
DR AlphaFoldDB; A0A061DDG4; -.
DR STRING; 5866.A0A061DDG4; -.
DR EnsemblProtists; CDR96250; CDR96250; BBBOND_0301540.
DR GeneID; 24564791; -.
DR KEGG; bbig:BBBOND_0301540; -.
DR VEuPathDB; PiroplasmaDB:BBBOND_0301540; -.
DR OMA; DNNHIDD; -.
DR OrthoDB; 1114626at2759; -.
DR Proteomes; UP000033188; Chromosome 3.
DR GO; GO:0005787; C:signal peptidase complex; IEA:UniProt.
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; IPR019756; Pept_S26A_signal_pept_1_Ser-AS.
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; 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:UP000033188};
KW Signal-anchor {ECO:0000256|ARBA:ARBA00022968};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}.
FT DOMAIN 50..103
FT /note="Peptidase S24/S26A/S26B/S26C"
FT /evidence="ECO:0000259|Pfam:PF00717"
SQ SEQUENCE 183 AA; 20623 MW; 8A40E7776FBAEC22 CRC64;
MDIIKREITT FKSEVRQFIR RPRENIEQLL ATACVLFTAL MLWKTANLYT GTDSPVVVVL
SGSMEPAFYR GDILFLMKHD TVSAGDIVVF KVHGRDIPIV HRTLSLHANS NEINVLTKGD
NNDVADRGLY SRGQKWLDGK HLVGTVLMRI PKFGIITIIL NENRALKWSL ISMLIYLVLS
GKG
//
