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Database: UniProt
Entry: A0A166XEZ3_9PEZI
LinkDB: A0A166XEZ3_9PEZI
Original site: A0A166XEZ3_9PEZI 
ID   A0A166XEZ3_9PEZI        Unreviewed;       620 AA.
AC   A0A166XEZ3;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 1.
DT   24-JAN-2024, entry version 19.
DE   SubName: Full=Carboxypeptidase S1 {ECO:0000313|EMBL:KZL76537.1};
GN   ORFNames=CT0861_05694 {ECO:0000313|EMBL:KZL76537.1};
OS   Colletotrichum tofieldiae.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum;
OC   Colletotrichum spaethianum species complex.
OX   NCBI_TaxID=708197 {ECO:0000313|EMBL:KZL76537.1, ECO:0000313|Proteomes:UP000076552};
RN   [1] {ECO:0000313|EMBL:KZL76537.1, ECO:0000313|Proteomes:UP000076552}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=0861 {ECO:0000313|EMBL:KZL76537.1,
RC   ECO:0000313|Proteomes:UP000076552};
RA   Hacquard S., Kracher B., Hiruma K., Weinman A., Muench P., Garrido Oter R.,
RA   Ver Loren van Themaat E., Dallerey J.-F., Damm U., Henrissat B.,
RA   Lespinet O., Thon M., Kemen E., McHardy A.C., Schulze-Lefert P.,
RA   O'Connell R.J.;
RT   "Survival trade-offs in plant roots during colonization by closely related
RT   pathogenic and mutualistic fungi.";
RL   Submitted (JUN-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the peptidase S10 family.
CC       {ECO:0000256|ARBA:ARBA00009431}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KZL76537.1}.
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DR   EMBL; LFIV01000014; KZL76537.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A166XEZ3; -.
DR   STRING; 708197.A0A166XEZ3; -.
DR   OrthoDB; 1647009at2759; -.
DR   Proteomes; UP000076552; Unassembled WGS sequence.
DR   GO; GO:0004185; F:serine-type carboxypeptidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1.
DR   InterPro; IPR029058; AB_hydrolase.
DR   InterPro; IPR001563; Peptidase_S10.
DR   InterPro; IPR033124; Ser_caboxypep_his_AS.
DR   PANTHER; PTHR11802:SF189; CARBOXYPEPTIDASE; 1.
DR   PANTHER; PTHR11802; SERINE PROTEASE FAMILY S10 SERINE CARBOXYPEPTIDASE; 1.
DR   Pfam; PF00450; Peptidase_S10; 1.
DR   PRINTS; PR00724; CRBOXYPTASEC.
DR   SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
DR   PROSITE; PS00560; CARBOXYPEPT_SER_HIS; 1.
PE   3: Inferred from homology;
KW   Carboxypeptidase {ECO:0000256|ARBA:ARBA00022645,
KW   ECO:0000313|EMBL:KZL76537.1}; Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Protease {ECO:0000256|ARBA:ARBA00022670};
KW   Reference proteome {ECO:0000313|Proteomes:UP000076552};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           21..620
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5007882277"
SQ   SEQUENCE   620 AA;  68406 MW;  A562B065B7A15B25 CRC64;
     MRSQLSILAL AGALLRCSVA QFPPTPEGVT VLKSKFGEGI EISYKEPGLC EEAEGVKSYA
     GYIKLPPGTL EGVGQEQDYE INTFFWFFEA KHDPENAPLS IWMNGGPGSS SMLGLFNENG
     PCYINPDSNS TRPSEWSWNN KVNMLYIDQP VQVGFSYDSL RNVTRNLLGG TQTLNASSPI
     PAQNVTFQTG TLASGNRNTT SWGSRNAAIA LWHFSQVWFQ EFPGYHPNDD RISIATQSYG
     GRYGPAFAAY FQEQNEKIRN GTWEGTEGEK YILNLDTLLI VNGCIDRQVQ WPSYPEMAFN
     NTYGIETVNA TVYQGMVDAY HREGGCRDQI DACREVSAVY DPENIGINAT VNRVCEAAES
     YCTRYVRDPY LDISGRDYYD VTQVDPTLFP PPFTAGFLNQ PYVQSALGVP LNWTGSSSAS
     SSAFRGIGDY PRPGWIEDIA YLLHNGIKVS LLYGDRDFAC NWIGGEEVAL AIPWAGQEKF
     AAAGYEPLQT NCTYEGGQVR QYGNLSYIRV YQAGHAVPSY QPESAYRIFN RALFNKDIAT
     GRIDTATNLT YSTQGPADTF GIKSEIPPQY EDFCYVLDTS TCSSAQIAAL RAGTAVIENY
     IMIEPASEQG AALGIKARDV
//
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