GenomeNet

Database: UniProt
Entry: A0A0D2BXA8_9EURO
LinkDB: A0A0D2BXA8_9EURO
Original site: A0A0D2BXA8_9EURO 
ID   A0A0D2BXA8_9EURO        Unreviewed;       619 AA.
AC   A0A0D2BXA8;
DT   29-APR-2015, integrated into UniProtKB/TrEMBL.
DT   29-APR-2015, sequence version 1.
DT   13-SEP-2023, entry version 25.
DE   RecName: Full=Carboxypeptidase {ECO:0008006|Google:ProtNLM};
GN   ORFNames=PV05_05612 {ECO:0000313|EMBL:KIW57006.1};
OS   Exophiala xenobiotica.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Exophiala.
OX   NCBI_TaxID=348802 {ECO:0000313|EMBL:KIW57006.1, ECO:0000313|Proteomes:UP000054342};
RN   [1] {ECO:0000313|EMBL:KIW57006.1, ECO:0000313|Proteomes:UP000054342}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 118157 {ECO:0000313|EMBL:KIW57006.1,
RC   ECO:0000313|Proteomes:UP000054342};
RG   The Broad Institute Genomics Platform;
RA   Cuomo C., de Hoog S., Gorbushina A., Stielow B., Teixiera M.,
RA   Abouelleil A., Chapman S.B., Priest M., Young S.K., Wortman J., Nusbaum C.,
RA   Birren B.;
RT   "The Genome Sequence of Exophiala xenobiotica CBS118157.";
RL   Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the peptidase S10 family.
CC       {ECO:0000256|ARBA:ARBA00009431}.
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; KN847319; KIW57006.1; -; Genomic_DNA.
DR   RefSeq; XP_013317590.1; XM_013462136.1.
DR   AlphaFoldDB; A0A0D2BXA8; -.
DR   STRING; 348802.A0A0D2BXA8; -.
DR   GeneID; 25327520; -.
DR   HOGENOM; CLU_008523_10_3_1; -.
DR   OrthoDB; 1647009at2759; -.
DR   Proteomes; UP000054342; Unassembled WGS sequence.
DR   GO; GO:0004185; F:serine-type carboxypeptidase activity; IEA:InterPro.
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   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.
PE   3: Inferred from homology;
KW   Carboxypeptidase {ECO:0000256|ARBA:ARBA00022645};
KW   Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Protease {ECO:0000256|ARBA:ARBA00022670};
KW   Reference proteome {ECO:0000313|Proteomes:UP000054342};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           20..619
FT                   /note="Carboxypeptidase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5002239311"
SQ   SEQUENCE   619 AA;  69145 MW;  361F381B3BB3C150 CRC64;
     MLLTFTALAW LLTAQLSQAQ FPPKPKNTTI LNSRFGDGVY ISYKEPGICE TTPGVKSYAG
     YVHLPAGTLA DVNATQNYPI NTFLWFFEAR NDPANAPLSI WMNGGPGSSS MLGLLTENGP
     CNVNPDSNST TLNPWSWNNN VNMLYLDQPV QVGFSYDTLQ NITYDLVSGD ITLLNKSDPI
     PKQNLTFQVG TYPSQKQNFT AIGSLNGARA LWHFTQTWFQ EFPAYHPNDS RISIATESYG
     GRYGPSYSAY FEEQNQKIEN GTWNHIGETY IIHLDTLMII NGCIDRQVQW PSYPHIAYNN
     TYGIQAVNQT IYNQMNDAYY GPGGCRDQIT RCRTVATQYD PTQQGVNASV NQICQSAENF
     CVAHVRDPYI EYSGRNYYDY GTLNPDPFLP NWYLGYLNQP HVQSALGVPL NFTSSSSVVA
     AAFRAIGDYP RPGWLEDLSY LLENGVKVAL VYGDRDYACN WIGGEAVSLA VNYTNTTHFH
     DAGYVPIQTN SSYSGGQVRQ YGNFSFSRVY ESGHEVPAYQ PETAYRIFQR ALFNHDIATG
     KVDTSSKNTT YTTSPAGLKD TWSIKNKDPP EPKWVCYVLD LEDTCTTEQI EMVVNGTAVV
     KDWILQDANS TALYPGIFS
//
DBGET integrated database retrieval system