ID A0A0D2CHL1_9EURO Unreviewed; 549 AA.
AC A0A0D2CHL1;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 24-JAN-2024, entry version 28.
DE RecName: Full=Carboxypeptidase {ECO:0000256|RuleBase:RU361156};
DE EC=3.4.16.- {ECO:0000256|RuleBase:RU361156};
GN ORFNames=PV07_11239 {ECO:0000313|EMBL:KIW23004.1};
OS Cladophialophora immunda.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae;
OC Cladophialophora.
OX NCBI_TaxID=569365 {ECO:0000313|EMBL:KIW23004.1, ECO:0000313|Proteomes:UP000054466};
RN [1] {ECO:0000313|EMBL:KIW23004.1, ECO:0000313|Proteomes:UP000054466}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 83496 {ECO:0000313|EMBL:KIW23004.1,
RC ECO:0000313|Proteomes:UP000054466};
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 Cladophialophora immunda CBS83496.";
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the peptidase S10 family.
CC {ECO:0000256|ARBA:ARBA00009431, ECO:0000256|RuleBase:RU361156}.
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DR EMBL; KN847046; KIW23004.1; -; Genomic_DNA.
DR RefSeq; XP_016243220.1; XM_016398658.1.
DR AlphaFoldDB; A0A0D2CHL1; -.
DR STRING; 569365.A0A0D2CHL1; -.
DR MEROPS; S10.014; -.
DR GeneID; 27350433; -.
DR VEuPathDB; FungiDB:PV07_11239; -.
DR HOGENOM; CLU_008523_12_3_1; -.
DR OrthoDB; 1647009at2759; -.
DR Proteomes; UP000054466; Unassembled WGS sequence.
DR GO; GO:0004185; F:serine-type carboxypeptidase activity; IEA:UniProtKB-UniRule.
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; IPR018202; Ser_caboxypep_ser_AS.
DR PANTHER; PTHR11802:SF116; 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; PS00131; CARBOXYPEPT_SER_SER; 1.
PE 3: Inferred from homology;
KW Carboxypeptidase {ECO:0000256|ARBA:ARBA00022645,
KW ECO:0000256|RuleBase:RU361156};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU361156};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|RuleBase:RU361156};
KW Reference proteome {ECO:0000313|Proteomes:UP000054466};
KW Signal {ECO:0000256|RuleBase:RU361156}.
FT SIGNAL 1..17
FT /evidence="ECO:0000256|RuleBase:RU361156"
FT CHAIN 18..549
FT /note="Carboxypeptidase"
FT /evidence="ECO:0000256|RuleBase:RU361156"
FT /id="PRO_5006514707"
FT REGION 33..55
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 549 AA; 60075 MW; 0D071B02837FE748 CRC64;
MHFTALLTAS LAAGAFAQSV SNPHKMAAQK LAKRAPAPAP PQERRSVHSL RKRQQSSYLT
SQTEKFAVNG TGVPLVNFDI GESYAGTLSI DGNSSNQNQL FFWFFPSDNP EASDEITIWL
NGGPGCSSLD GLLQEHGPFL WQSGTYAPLP NPFSFTNLTN MVYVDQPIGT GFSPAAKGAP
AKINNEVDVG RQFAGFWKNF MTTFNMTGRK VYITGESYAG QYIPYIASYM IDQNNTDFYN
VAGIQINDPS IGLNSVLNEV PAATHMNNYA NVFALNDTFV AAINKRAEQC GYIEYMENAL
TFPPKGKFQE PVNASNPDCF IWEDIIFAEL YVNPCFNFYH LTDYCPFLND ELGFPSLGNG
PNNYFNRSDV QAAIHAPPTD YVICGDDSLF PNGDQSPPSS FSALPHVIES TNNVIVGSGL
LDYLLMTNGT LMTLNNMTWN GAQGFSKKPS DKFFVPYNPS IGFVIQETTN QPIPATPVGL
VAGGGYMGTT HTERGLTWVT VDMAGHEIPQ YVPGAAYRQL EFLLGRIKSL TQMGDFSTQH
GNYTGTTPL
//
