GenomeNet

Database: UniProt
Entry: A0A177D4E0_ALTAL
LinkDB: A0A177D4E0_ALTAL
Original site: A0A177D4E0_ALTAL 
ID   A0A177D4E0_ALTAL        Unreviewed;       614 AA.
AC   A0A177D4E0;
DT   07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT   07-SEP-2016, sequence version 1.
DT   10-APR-2019, entry version 11.
DE   SubName: Full=Tripeptidyl-peptidase 1 {ECO:0000313|EMBL:OAG14524.1};
GN   ORFNames=CC77DRAFT_948433 {ECO:0000313|EMBL:OAG14524.1};
OS   Alternaria alternata (Alternaria rot fungus) (Torula alternata).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina;
OC   Dothideomycetes; Pleosporomycetidae; Pleosporales; Pleosporineae;
OC   Pleosporaceae; Alternaria; Alternaria sect. Alternaria;
OC   Alternaria alternata complex.
OX   NCBI_TaxID=5599 {ECO:0000313|EMBL:OAG14524.1, ECO:0000313|Proteomes:UP000077248};
RN   [1] {ECO:0000313|EMBL:OAG14524.1, ECO:0000313|Proteomes:UP000077248}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SRC1lrK2f {ECO:0000313|EMBL:OAG14524.1,
RC   ECO:0000313|Proteomes:UP000077248};
RG   DOE Joint Genome Institute;
RA   Zeiner C.A., Purvine S.O., Zink E.M., Wu S., Pasa-Tolic L.,
RA   Chaput D.L., Haridas S., Grigoriev I.V., Santelli C.M., Hansel C.M.;
RT   "Comparative analysis of secretome profiles of manganese(II)-oxidizing
RT   ascomycete fungi.";
RL   Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC         Evidence={ECO:0000256|PROSITE-ProRule:PRU01032};
CC       Note=Binds 1 Ca(2+) ion per subunit. {ECO:0000256|PROSITE-
CC       ProRule:PRU01032};
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; KV441499; OAG14524.1; -; Genomic_DNA.
DR   RefSeq; XP_018379945.1; XM_018535200.1.
DR   EnsemblFungi; OAG14524; OAG14524; CC77DRAFT_948433.
DR   GeneID; 29120794; -.
DR   KEGG; aalt:CC77DRAFT_948433; -.
DR   KO; K01279; -.
DR   Proteomes; UP000077248; Unassembled WGS sequence.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-UniRule.
DR   CDD; cd04056; Peptidases_S53; 1.
DR   CDD; cd11377; Pro-peptidase_S53; 1.
DR   Gene3D; 3.40.50.200; -; 1.
DR   InterPro; IPR000209; Peptidase_S8/S53_dom.
DR   InterPro; IPR036852; Peptidase_S8/S53_dom_sf.
DR   InterPro; IPR023828; Peptidase_S8_Ser-AS.
DR   InterPro; IPR015366; S53_propep.
DR   InterPro; IPR030400; Sedolisin_dom.
DR   Pfam; PF00082; Peptidase_S8; 1.
DR   Pfam; PF09286; Pro-kuma_activ; 1.
DR   SMART; SM00944; Pro-kuma_activ; 1.
DR   SUPFAM; SSF52743; SSF52743; 1.
DR   PROSITE; PS51695; SEDOLISIN; 1.
DR   PROSITE; PS00138; SUBTILASE_SER; 1.
PE   4: Predicted;
KW   Calcium {ECO:0000256|PROSITE-ProRule:PRU01032};
KW   Complete proteome {ECO:0000313|Proteomes:UP000077248};
KW   Hydrolase {ECO:0000256|PROSITE-ProRule:PRU01032};
KW   Metal-binding {ECO:0000256|PROSITE-ProRule:PRU01032};
KW   Protease {ECO:0000256|PROSITE-ProRule:PRU01032};
KW   Reference proteome {ECO:0000313|Proteomes:UP000077248};
KW   Serine protease {ECO:0000256|PROSITE-ProRule:PRU01032};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL        1     19       {ECO:0000256|SAM:SignalP}.
FT   CHAIN        20    614       {ECO:0000256|SAM:SignalP}.
FT                                /FTId=PRO_5008058975.
FT   DOMAIN      217    612       Peptidase S53. {ECO:0000259|PROSITE:
FT                                PS51695}.
FT   ACT_SITE    303    303       Charge relay system.
FT                                {ECO:0000256|PROSITE-ProRule:PRU01032}.
FT   ACT_SITE    307    307       Charge relay system.
FT                                {ECO:0000256|PROSITE-ProRule:PRU01032}.
FT   ACT_SITE    529    529       Charge relay system.
FT                                {ECO:0000256|PROSITE-ProRule:PRU01032}.
FT   METAL       571    571       Calcium. {ECO:0000256|PROSITE-ProRule:
FT                                PRU01032}.
FT   METAL       572    572       Calcium; via carbonyl oxygen.
FT                                {ECO:0000256|PROSITE-ProRule:PRU01032}.
FT   METAL       590    590       Calcium; via carbonyl oxygen.
FT                                {ECO:0000256|PROSITE-ProRule:PRU01032}.
FT   METAL       592    592       Calcium. {ECO:0000256|PROSITE-ProRule:
FT                                PRU01032}.
SQ   SEQUENCE   614 AA;  67946 MW;  84C50F714BBE6371 CRC64;
     MQIFATVVLA AVAARDALAS PIQARSPYVV KETHFAPREW TKLERAHGGK TIQLQIGLKQ
     GRFEELDRHL HEVSDPDHKR YGQHLSADEV DELVAPSSET HDLVHEWLRE SGIDTDNVGY
     SSAKDWVIVH LPIEMVESLL DTEYHTYKHK DGSIVARTTA WSLPRHLHAH IDTIQPTTSF
     FRVAPNEATF VDEAVEVPAS YHTPQNSSIS AVCNVTSVTP ECFQTLYKTK WYHTKASRKN
     SVGFTNYLGE IPIRPDTKMF LEKYRPEAVS QAYAFKQISI DNGPTQDGPL TYNQSTVEGI
     SREANLDVQA ISGISWKTPI TSFSTGGSPP FTPDVSTPTN TNEPYLVWVN WLLSQHSIPR
     IISTSYGDSE QTVPKSYAER VCKQFAQVGA RGTTLFFSSG DRGLGGTDTC YTNDGRNKYQ
     FQPNFPASCP YVTTVGATMN FEPEESAYRP SRNTSAGFRD LYSSGSGFSN YFPRPWYQDS
     VVPQYVDSLG DTYEGLYNKT GRGYPDLAAQ GLYFAYFWNG TEGTISGTSA SCPLTAGIFS
     LVNDALLASG KPTLGFLNPW LYKKGHKGLT DITKGFSHGC NVEGFPVTEG WDPITGFGTP
     DFPKLVKLAG AHVH
//
DBGET integrated database retrieval system