ID E2A6R7_CAMFO Unreviewed; 180 AA.
AC E2A6R7;
DT 30-NOV-2010, integrated into UniProtKB/TrEMBL.
DT 30-NOV-2010, sequence version 1.
DT 27-MAR-2024, entry version 60.
DE RecName: Full=Signal peptidase complex catalytic subunit SEC11 {ECO:0000256|ARBA:ARBA00019685, ECO:0000256|RuleBase:RU362047};
DE EC=3.4.21.89 {ECO:0000256|ARBA:ARBA00013208, ECO:0000256|RuleBase:RU362047};
GN ORFNames=EAG_04271 {ECO:0000313|EMBL:EFN70861.1};
OS Camponotus floridanus (Florida carpenter ant).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Formicoidea;
OC Formicidae; Formicinae; Camponotus.
OX NCBI_TaxID=104421 {ECO:0000313|Proteomes:UP000000311};
RN [1] {ECO:0000313|EMBL:EFN70861.1, ECO:0000313|Proteomes:UP000000311}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C129 {ECO:0000313|Proteomes:UP000000311};
RX PubMed=20798317; DOI=10.1126/science.1192428;
RA Bonasio R., Zhang G., Ye C., Mutti N.S., Fang X., Qin N., Donahue G.,
RA Yang P., Li Q., Li C., Zhang P., Huang Z., Berger S.L., Reinberg D.,
RA Wang J., Liebig J.;
RT "Genomic comparison of the ants Camponotus floridanus and Harpegnathos
RT saltator.";
RL Science 329:1068-1071(2010).
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 ECO:0000256|RuleBase:RU362047};
CC -!- SUBUNIT: Component of the signal peptidase complex.
CC {ECO:0000256|RuleBase:RU362047}.
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, ECO:0000256|RuleBase:RU362047}.
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DR EMBL; GL437197; EFN70861.1; -; Genomic_DNA.
DR RefSeq; XP_011252466.1; XM_011254164.2.
DR AlphaFoldDB; E2A6R7; -.
DR STRING; 104421.E2A6R7; -.
DR MEROPS; S26.010; -.
DR EnsemblMetazoa; XM_011254164.3; XP_011252466.1; LOC105249031.
DR GeneID; 105249031; -.
DR InParanoid; E2A6R7; -.
DR OMA; DNNHIDD; -.
DR OrthoDB; 1114626at2759; -.
DR Proteomes; UP000000311; Unassembled WGS sequence.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0098796; C:membrane protein complex; IEA:UniProt.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-EC.
DR GO; GO:0006465; P:signal peptide processing; IEA:UniProtKB-UniRule.
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; 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 Pfam; PF10502; Peptidase_S26; 1.
DR PRINTS; PR00728; SIGNALPTASE.
DR SUPFAM; SSF51306; LexA/Signal peptidase; 1.
DR PROSITE; PS00501; SPASE_I_1; 1.
DR PROSITE; PS00761; SPASE_I_3; 1.
PE 3: Inferred from homology;
KW Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00022824,
KW ECO:0000256|RuleBase:RU362047}; Hydrolase {ECO:0000256|RuleBase:RU362047};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU362047};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|RuleBase:RU362047};
KW Reference proteome {ECO:0000313|Proteomes:UP000000311};
KW Signal-anchor {ECO:0000256|RuleBase:RU362047};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW ECO:0000256|RuleBase:RU362047};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|RuleBase:RU362047}.
FT TRANSMEM 21..41
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362047"
FT DOMAIN 41..98
FT /note="Peptidase S26"
FT /evidence="ECO:0000259|Pfam:PF10502"
SQ SEQUENCE 180 AA; 20510 MW; 4A9188D888C34F00 CRC64;
MLQSIFDDVR RMNKRQFLYQ VLSFGMIVSS ALMIWKGLMV VTGSESPIVV VLSGSMEPAF
HRGDLLFLTN YQDEPVRVGE IVVFKVEGRD IPIVHRVLKL HEKGDQNNTV KFLTKGDNNS
VDDRGLYAPG QLWLTHKDVV GRARGFLPYV GMVTIYMNEY PKFKYAVLAC LGLYVLVHRE
//
