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Database: UniProt
Entry: R4G542_RHOPR
LinkDB: R4G542_RHOPR
Original site: R4G542_RHOPR 
ID   R4G542_RHOPR            Unreviewed;       178 AA.
AC   R4G542;
DT   26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT   26-JUN-2013, sequence version 1.
DT   24-JAN-2024, entry version 61.
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};
OS   Rhodnius prolixus (Triatomid bug).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Paraneoptera; Hemiptera; Heteroptera; Panheteroptera;
OC   Cimicomorpha; Reduviidae; Triatominae; Rhodnius.
OX   NCBI_TaxID=13249 {ECO:0000313|EMBL:JAA76695.1};
RN   [1] {ECO:0000313|EMBL:JAA76695.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Ribeiro J.M.C., Genta F.A., Sorgine M.H.F., Paiva-Silva G.O.,
RA   Majerowicz D., Medeiros M., Koerich L., Terra W.R., Ferreira C.,
RA   Pimentel A.C., Bisch P.M., Diniz M.M.P., Nascimento R., Salmon D.,
RA   Silber A.M., Alves M., Oliveira M.F., Gondim K.C., Silva Neto M.A.C.,
RA   Atella G.C., Araujo H., Dias F.S., Polycarpo C.R., Fampa P., Melo A.C.,
RA   Tanaka A.S., Balczun C., Oliveira J.H.M., Goncalves R., Lazoski C.,
RA   Pereira M.A., Rivera-Pomar R., Diambra L., Schaub G.A., Garcia E.S.,
RA   Azambuja P., Braz G.R.C., Oliveira P.L.;
RT   "An insight into the transcriptome of the digestive tract of the blood
RT   sucking bug, Rhodnius prolixus.";
RL   Submitted (APR-2013) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Proteomes:UP000015103}
RP   NUCLEOTIDE SEQUENCE.
RA   Wilson R.K., Warren W., Dotson E., Oliveira P.L.;
RL   Submitted (APR-2015) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|EnsemblMetazoa:RPRC002798-PA}
RP   IDENTIFICATION.
RG   EnsemblMetazoa;
RL   Submitted (MAY-2015) to UniProtKB.
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}. 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, ECO:0000256|RuleBase:RU362047}.
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DR   EMBL; ACPB03018001; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; GAHY01000815; JAA76695.1; -; mRNA.
DR   AlphaFoldDB; R4G542; -.
DR   STRING; 13249.R4G542; -.
DR   EnsemblMetazoa; RPRC002798-RA; RPRC002798-PA; RPRC002798.
DR   VEuPathDB; VectorBase:RPRC002798; -.
DR   eggNOG; KOG3342; Eukaryota.
DR   HOGENOM; CLU_089996_0_0_1; -.
DR   InParanoid; R4G542; -.
DR   OMA; WLKTAML; -.
DR   OrthoDB; 1114626at2759; -.
DR   Proteomes; UP000015103; Unassembled WGS sequence.
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: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; 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.
DR   PROSITE; PS00761; SPASE_I_3; 1.
PE   2: Evidence at transcript level;
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:UP000015103};
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        17..35
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362047"
FT   DOMAIN          36..121
FT                   /note="Peptidase S24/S26A/S26B/S26C"
FT                   /evidence="ECO:0000259|Pfam:PF00717"
SQ   SEQUENCE   178 AA;  20230 MW;  2DC77BE37E2BC12E CRC64;
     MIQGALDELR RMNKRQFLYQ CLSFGMIVSS ALMIWKGLMV VTGSESPIVV VLSGSMEPAF
     HRGDLLFLTN FQDDPVRVGE IVVFKVEGRD IPIVHRVLKL HEKRNGTVKF LTKGDNNSVD
     DRGLYAPGQF WLTKKDVVGR ARGFLPYVGM VTIYMNEYPK FKYAVLACLG LYVLVHRE
//
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