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SEC11_GROCL
ID   SEC11_GROCL             Reviewed;         172 AA.
AC   F0XJH4;
DT   21-SEP-2011, integrated into UniProtKB/Swiss-Prot.
DT   03-MAY-2011, sequence version 1.
DT   25-MAY-2022, entry version 43.
DE   RecName: Full=Signal peptidase complex catalytic subunit SEC11;
DE            EC=3.4.21.89 {ECO:0000250|UniProtKB:P15367};
DE   AltName: Full=Signal peptidase I;
GN   Name=SEC11; ORFNames=CMQ_2301;
OS   Grosmannia clavigera (strain kw1407 / UAMH 11150) (Blue stain fungus)
OS   (Graphiocladiella clavigera).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Sordariomycetidae; Ophiostomatales; Ophiostomataceae; Grosmannia.
OX   NCBI_TaxID=655863;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=kw1407 / UAMH 11150;
RX   PubMed=21262841; DOI=10.1073/pnas.1011289108;
RA   DiGuistini S., Wang Y., Liao N.Y., Taylor G., Tanguay P., Feau N.,
RA   Henrissat B., Chan S.K., Hesse-Orce U., Alamouti S.M., Tsui C.K.M.,
RA   Docking R.T., Levasseur A., Haridas S., Robertson G., Birol I., Holt R.A.,
RA   Marra M.A., Hamelin R.C., Hirst M., Jones S.J.M., Bohlmann J., Breuil C.;
RT   "Genome and transcriptome analyses of the mountain pine beetle-fungal
RT   symbiont Grosmannia clavigera, a lodgepole pine pathogen.";
RL   Proc. Natl. Acad. Sci. U.S.A. 108:2504-2509(2011).
CC   -!- FUNCTION: Catalytic component of the signal peptidase complex (SPC)
CC       which catalyzes the cleavage of N-terminal signal sequences from
CC       nascent proteins as they are translocated into the lumen of the
CC       endoplasmic reticulum (By similarity). Specifically cleaves N-terminal
CC       signal peptides that contain a hydrophobic alpha-helix (h-region)
CC       shorter than 18-20 amino acids (By similarity).
CC       {ECO:0000250|UniProtKB:P15367, ECO:0000250|UniProtKB:P67812}.
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:0000250|UniProtKB:P15367};
CC   -!- SUBUNIT: Component of the signal peptidase complex (SPC) composed of a
CC       catalytic subunit SEC11 and three accessory subunits SPC1, SPC2 and
CC       SPC3 (By similarity). The complex induces a local thinning of the ER
CC       membrane which is used to measure the length of the signal peptide (SP)
CC       h-region of protein substrates. This ensures the selectivity of the
CC       complex towards h-regions shorter than 18-20 amino acids (By
CC       similarity). SPC associates with the translocon complex (By
CC       similarity). {ECO:0000250|UniProtKB:P15367,
CC       ECO:0000250|UniProtKB:P67812}.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC       {ECO:0000250|UniProtKB:P15367}; Single-pass type II membrane protein
CC       {ECO:0000250|UniProtKB:P15367}.
CC   -!- DOMAIN: The C-terminal short (CTS) helix is essential for catalytic
CC       activity. It may be accommodated as a transmembrane helix in the
CC       thinned membrane environment of the complex, similarly to the signal
CC       peptide in the complex substrates. {ECO:0000250|UniProtKB:P67812}.
CC   -!- SIMILARITY: Belongs to the peptidase S26B family. {ECO:0000305}.
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DR   EMBL; GL629782; EFX02252.1; -; Genomic_DNA.
DR   RefSeq; XP_014171734.1; XM_014316259.1.
DR   AlphaFoldDB; F0XJH4; -.
DR   SMR; F0XJH4; -.
DR   STRING; 655863.F0XJH4; -.
DR   PRIDE; F0XJH4; -.
DR   EnsemblFungi; EFX02252; EFX02252; CMQ_2301.
DR   GeneID; 25975276; -.
DR   eggNOG; KOG3342; Eukaryota.
DR   HOGENOM; CLU_089996_0_1_1; -.
DR   InParanoid; F0XJH4; -.
DR   OrthoDB; 1486616at2759; -.
DR   Proteomes; UP000007796; Unassembled WGS sequence.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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; 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   PANTHER; PTHR10806; PTHR10806; 1.
DR   Pfam; PF00717; Peptidase_S24; 1.
DR   PRINTS; PR00728; SIGNALPTASE.
DR   SUPFAM; SSF51306; SSF51306; 1.
DR   TIGRFAMs; TIGR02228; sigpep_I_arch; 1.
DR   PROSITE; PS00501; SPASE_I_1; 1.
PE   3: Inferred from homology;
KW   Endoplasmic reticulum; Hydrolase; Membrane; Protease; Reference proteome;
KW   Signal-anchor; Transmembrane; Transmembrane helix.
FT   CHAIN           1..172
FT                   /note="Signal peptidase complex catalytic subunit SEC11"
FT                   /id="PRO_0000412330"
FT   TOPO_DOM        1..14
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        15..35
FT                   /note="Helical; Signal-anchor for type II membrane protein"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        36..172
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000305"
FT   REGION          158..169
FT                   /note="C-terminal short (CTS) helix"
FT                   /evidence="ECO:0000250|UniProtKB:P67812"
FT   ACT_SITE        49
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250|UniProtKB:P15367"
FT   ACT_SITE        90
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250|UniProtKB:P15367"
FT   ACT_SITE        115
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250|UniProtKB:P15367"
SQ   SEQUENCE   172 AA;  18995 MW;  F7D95AF7093CAFA2 CRC64;
     MLSAVAKPRQ LASQILNFGL ILSTAFMIWK GLSVVSDSSS PIVVVLSGSM EPAFQRGDLL
     FLWNRNLLQE TDVGEIVVYN VRGKDIPIVH RIVRKFGTGP HAKLLTKGDN NAGDDTDLYA
     QGQDYLERKD IVGSVVGYVP FVGYVTILLT EHPWLKKVML GLMGVLVVLQ RE
 
 
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