(data stored in ACNUC7421 zone)

SWISSPROT: A2Q7G0_ASPNC

ID   A2Q7G0_ASPNC            Unreviewed;       143 AA.
AC   A2Q7G0;
DT   06-MAR-2007, integrated into UniProtKB/TrEMBL.
DT   06-MAR-2007, sequence version 1.
DT   11-DEC-2019, entry version 82.
DE   RecName: Full=Signal peptidase complex catalytic subunit SEC11 {ECO:0000256|RuleBase:RU362047};
DE            EC=3.4.21.89 {ECO:0000256|RuleBase:RU362047};
GN   ORFNames=An01g00560 {ECO:0000313|EMBL:CAK43444.1};
OS   Aspergillus niger (strain CBS 513.88 / FGSC A1513).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX   NCBI_TaxID=425011 {ECO:0000313|Proteomes:UP000006706};
RN   [1] {ECO:0000313|EMBL:CAK43444.1, ECO:0000313|Proteomes:UP000006706}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 513.88 / FGSC A1513 {ECO:0000313|Proteomes:UP000006706};
RX   PubMed=17259976; DOI=10.1038/nbt1282;
RA   Pel H.J., de Winde J.H., Archer D.B., Dyer P.S., Hofmann G., Schaap P.J.,
RA   Turner G., de Vries R.P., Albang R., Albermann K., Andersen M.R.,
RA   Bendtsen J.D., Benen J.A., van den Berg M., Breestraat S., Caddick M.X.,
RA   Contreras R., Cornell M., Coutinho P.M., Danchin E.G., Debets A.J.,
RA   Dekker P., van Dijck P.W., van Dijk A., Dijkhuizen L., Driessen A.J.,
RA   d'Enfert C., Geysens S., Goosen C., Groot G.S., de Groot P.W.,
RA   Guillemette T., Henrissat B., Herweijer M., van den Hombergh J.P.,
RA   van den Hondel C.A., van der Heijden R.T., van der Kaaij R.M., Klis F.M.,
RA   Kools H.J., Kubicek C.P., van Kuyk P.A., Lauber J., Lu X.,
RA   van der Maarel M.J., Meulenberg R., Menke H., Mortimer M.A., Nielsen J.,
RA   Oliver S.G., Olsthoorn M., Pal K., van Peij N.N., Ram A.F., Rinas U.,
RA   Roubos J.A., Sagt C.M., Schmoll M., Sun J., Ussery D., Varga J.,
RA   Vervecken W., van de Vondervoort P.J., Wedler H., Wosten H.A., Zeng A.P.,
RA   van Ooyen A.J., Visser J., Stam H.;
RT   "Genome sequencing and analysis of the versatile cell factory Aspergillus
RT   niger CBS 513.88.";
RL   Nat. Biotechnol. 25:221-231(2007).
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|RuleBase:RU362047,
CC         ECO:0000256|SAAS:SAAS01126240};
CC   -!- SUBUNIT: Component of the signal peptidase complex.
CC       {ECO:0000256|RuleBase:RU362047}.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC       {ECO:0000256|RuleBase:RU362047}.
CC   -!- SIMILARITY: Belongs to the peptidase S26B family.
CC       {ECO:0000256|RuleBase:RU362047, ECO:0000256|SAAS:SAAS00551860}.
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DR   EMBL; AM269950; CAK43444.1; -; Genomic_DNA.
DR   MEROPS; S26.010; -.
DR   PaxDb; A2Q7G0; -.
DR   EnsemblFungi; CAK43444; CAK43444; An01g00560.
DR   HOGENOM; HOG000111516; -.
DR   Proteomes; UP000006706; Chromosome 2R.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-UniRule.
DR   GO; GO:0005787; C:signal peptidase complex; IEA:EnsemblFungi.
DR   GO; GO:0008236; F:serine-type peptidase activity; IEA:InterPro.
DR   GO; GO:0045047; P:protein targeting to ER; IEA:EnsemblFungi.
DR   GO; GO:0006465; P:signal peptide processing; IEA:UniProtKB-UniRule.
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; 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;
DR   PRODOM; A2Q7G0.
DR   SWISS-2DPAGE; A2Q7G0.
KW   Endoplasmic reticulum {ECO:0000256|RuleBase:RU362047};
KW   Hydrolase {ECO:0000256|RuleBase:RU362047, ECO:0000256|SAAS:SAAS00474280};
KW   Membrane {ECO:0000256|RuleBase:RU362047, ECO:0000256|SAAS:SAAS00474288};
KW   Protease {ECO:0000256|RuleBase:RU362047, ECO:0000256|SAAS:SAAS00474277};
KW   Signal-anchor {ECO:0000256|RuleBase:RU362047};
KW   Transmembrane {ECO:0000256|RuleBase:RU362047,
KW   ECO:0000256|SAAS:SAAS00474282};
KW   Transmembrane helix {ECO:0000256|RuleBase:RU362047,
KW   ECO:0000256|SAAS:SAAS00474285}.
FT   TRANSMEM        102..118
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362047"
FT   DOMAIN          18..74
FT                   /note="Peptidase_S24"
FT                   /evidence="ECO:0000259|Pfam:PF00717"
SQ   SEQUENCE   143 AA;  15905 MW;  A6A0F5D057566817 CRC64;
     MWKGLSVLTN SPSPIVVVLS GSMEPAFQRG DLLFLRNTQP TLNVGEIVVY QVKDKDIPIV
     HRVVRQFGEG SEAKLLTKGD NNIADDTELY ARGQDYLDRD DVVGSVFGYI PFVGYVTILL
     SEHPWLKTAM LGVMGLLVLL QRE
//

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