位置:首页 > 蛋白库 > SEC11_TALSN
SEC11_TALSN
ID   SEC11_TALSN             Reviewed;         191 AA.
AC   B8M5K5;
DT   21-SEP-2011, integrated into UniProtKB/Swiss-Prot.
DT   03-MAR-2009, sequence version 1.
DT   03-AUG-2022, entry version 64.
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=TSTA_031580;
OS   Talaromyces stipitatus (strain ATCC 10500 / CBS 375.48 / QM 6759 / NRRL
OS   1006) (Penicillium stipitatum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Trichocomaceae; Talaromyces;
OC   Talaromyces sect. Talaromyces.
OX   NCBI_TaxID=441959;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 10500 / CBS 375.48 / QM 6759 / NRRL 1006;
RX   PubMed=25676766; DOI=10.1128/genomea.01559-14;
RA   Nierman W.C., Fedorova-Abrams N.D., Andrianopoulos A.;
RT   "Genome sequence of the AIDS-associated pathogen Penicillium marneffei
RT   (ATCC18224) and its near taxonomic relative Talaromyces stipitatus
RT   (ATCC10500).";
RL   Genome Announc. 3:E0155914-E0155914(2015).
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}.
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; EQ962654; EED19899.1; -; Genomic_DNA.
DR   RefSeq; XP_002480333.1; XM_002480288.1.
DR   AlphaFoldDB; B8M5K5; -.
DR   SMR; B8M5K5; -.
DR   STRING; 441959.B8M5K5; -.
DR   MEROPS; S26.010; -.
DR   EnsemblFungi; EED19899; EED19899; TSTA_031580.
DR   GeneID; 8107769; -.
DR   VEuPathDB; FungiDB:TSTA_031580; -.
DR   eggNOG; KOG3342; Eukaryota.
DR   HOGENOM; CLU_089996_0_0_1; -.
DR   InParanoid; B8M5K5; -.
DR   OMA; YNVRGKD; -.
DR   OrthoDB; 1486616at2759; -.
DR   PhylomeDB; B8M5K5; -.
DR   Proteomes; UP000001745; 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; Glycoprotein; Hydrolase; Membrane; Protease;
KW   Reference proteome; Signal-anchor; Transmembrane; Transmembrane helix.
FT   CHAIN           1..191
FT                   /note="Signal peptidase complex catalytic subunit sec11"
FT                   /id="PRO_0000412367"
FT   TOPO_DOM        1..18
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        19..39
FT                   /note="Helical; Signal-anchor for type II membrane protein"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        40..191
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   REGION          177..188
FT                   /note="C-terminal short (CTS) helix"
FT                   /evidence="ECO:0000250|UniProtKB:P67812"
FT   ACT_SITE        53
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250|UniProtKB:P15367"
FT   ACT_SITE        92
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250|UniProtKB:P15367"
FT   ACT_SITE        133
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250|UniProtKB:P15367"
FT   CARBOHYD        41
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   191 AA;  21110 MW;  32D23773221156C7 CRC64;
     MLSALGGNLS NARQSIAQVL NFALVLSTAF MLWKGVSIVS NSSSPIVVVL SGSMEPAFQR
     GDLLFLWNRG ERAEVGEIVV YNVRGKDIPI VHRVVRSYTE EDKKLKAKKT KAGLPYVAPQ
     KLLTKGDNNL ADDTELYARG QEFLDRKEDI VGSVRGYIPG VGYVTIMLSE HPWLKTVLLG
     VMGLMVVFQR E
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2024