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Database: UniProt
Entry: A1CVU5_NEOFI
LinkDB: A1CVU5_NEOFI
Original site: A1CVU5_NEOFI 
ID   A1CVU5_NEOFI            Unreviewed;       594 AA.
AC   A1CVU5;
DT   23-JAN-2007, integrated into UniProtKB/TrEMBL.
DT   23-JAN-2007, sequence version 1.
DT   08-MAY-2019, entry version 71.
DE   SubName: Full=Tripeptidyl peptidase A {ECO:0000313|EMBL:EAW24747.1};
GN   ORFNames=NFIA_102320 {ECO:0000313|EMBL:EAW24747.1};
OS   Neosartorya fischeri (strain ATCC 1020 / DSM 3700 / CBS 544.65 / FGSC
OS   A1164 / JCM 1740 / NRRL 181 / WB 181) (Aspergillus fischerianus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX   NCBI_TaxID=331117 {ECO:0000313|EMBL:EAW24747.1, ECO:0000313|Proteomes:UP000006702};
RN   [1] {ECO:0000313|Proteomes:UP000006702}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 1020 / DSM 3700 / CBS 544.65 / FGSC A1164 / JCM 1740 /
RC   NRRL 181 / WB 181 {ECO:0000313|Proteomes:UP000006702};
RX   PubMed=18404212; DOI=10.1371/journal.pgen.1000046;
RA   Fedorova N.D., Khaldi N., Joardar V.S., Maiti R., Amedeo P.,
RA   Anderson M.J., Crabtree J., Silva J.C., Badger J.H., Albarraq A.,
RA   Angiuoli S., Bussey H., Bowyer P., Cotty P.J., Dyer P.S., Egan A.,
RA   Galens K., Fraser-Liggett C.M., Haas B.J., Inman J.M., Kent R.,
RA   Lemieux S., Malavazi I., Orvis J., Roemer T., Ronning C.M.,
RA   Sundaram J.P., Sutton G., Turner G., Venter J.C., White O.R.,
RA   Whitty B.R., Youngman P., Wolfe K.H., Goldman G.H., Wortman J.R.,
RA   Jiang B., Denning D.W., Nierman W.C.;
RT   "Genomic islands in the pathogenic filamentous fungus Aspergillus
RT   fumigatus.";
RL   PLoS Genet. 4:E1000046-E1000046(2008).
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};
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DR   EMBL; DS027685; EAW24747.1; -; Genomic_DNA.
DR   RefSeq; XP_001266644.1; XM_001266643.1.
DR   STRING; 36630.CADNFIAP00009858; -.
DR   MEROPS; S53.010; -.
DR   EnsemblFungi; EAW24747; EAW24747; NFIA_102320.
DR   GeneID; 4593803; -.
DR   KEGG; nfi:NFIA_102320; -.
DR   EuPathDB; FungiDB:NFIA_102320; -.
DR   HOGENOM; HOG000171253; -.
DR   KO; K01279; -.
DR   OMA; TVEFNAI; -.
DR   OrthoDB; 1294880at2759; -.
DR   Proteomes; UP000006702; 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; 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; 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:UP000006702};
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:UP000006702};
KW   Serine protease {ECO:0000256|PROSITE-ProRule:PRU01032};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL        1     20       {ECO:0000256|SAM:SignalP}.
FT   CHAIN        21    594       {ECO:0000256|SAM:SignalP}.
FT                                /FTId=PRO_5002633220.
FT   DOMAIN      197    594       Peptidase S53. {ECO:0000259|PROSITE:
FT                                PS51695}.
FT   ACT_SITE    272    272       Charge relay system.
FT                                {ECO:0000256|PROSITE-ProRule:PRU01032}.
FT   ACT_SITE    276    276       Charge relay system.
FT                                {ECO:0000256|PROSITE-ProRule:PRU01032}.
FT   ACT_SITE    494    494       Charge relay system.
FT                                {ECO:0000256|PROSITE-ProRule:PRU01032}.
FT   METAL       536    536       Calcium. {ECO:0000256|PROSITE-ProRule:
FT                                PRU01032}.
FT   METAL       537    537       Calcium; via carbonyl oxygen.
FT                                {ECO:0000256|PROSITE-ProRule:PRU01032}.
FT   METAL       572    572       Calcium; via carbonyl oxygen.
FT                                {ECO:0000256|PROSITE-ProRule:PRU01032}.
FT   METAL       574    574       Calcium. {ECO:0000256|PROSITE-ProRule:
FT                                PRU01032}.
SQ   SEQUENCE   594 AA;  63692 MW;  2C2BF3CFB1E30E66 CRC64;
     MLSSTLYAGL LCSLAAPALG VVHEKLSAVP SGWTLVEDAS ESDTTTLSIA LARQNLDQLE
     SKLTTLATPG NAEYGKWLDQ SDIESLFPTA SDDAVIQWLK DAGVTQVSRQ GSLVNFATTV
     GTANKLFDTK FSYYRNGASQ KLRTTQYSIP DSLTESIDLI APTVFFGKEQ DSALPPHAVK
     LPALPRRAAT NSSCANLITP DCLVEMYNLG DYKPDASSGS RVGFGSFLNQ SANYADLAAY
     EQLFNIPPQN FSVELINGGA NDQNWATASL GEANLDVELI VAVSHALPVV EFITGGSPPF
     VPNVDEPTAA DNQNEPYLQY YEYLLSKPNS HLPQVISNSY GDDEQTVPEY YARRVCNLIG
     LMGLRGITVL ESSGDTGIGS ACMSNDGTNT PQFTPTFPGT CPFITAVGGT QSYAPEVAWD
     ASSGGFSNYF SRPWYQYFAV ENYLNNHITK DTKKYYSQYT NFKGRGFPDV SAHSLTPDYE
     VVLTGKHYKS GGTSAACPVF AGIVGLLNDA RLRAGKSTLG FLNPLLYSIL AEGFTDITAG
     SSIGCNGINP QTGKPVPGGG IIPYAHWNAT AGWDPVTGLG VPDFMKLKEL VLSL
//
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