ID A0A0D2ADP9_9PEZI Unreviewed; 567 AA.
AC A0A0D2ADP9;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE RecName: Full=Carboxypeptidase {ECO:0000256|RuleBase:RU361156};
DE EC=3.4.16.- {ECO:0000256|RuleBase:RU361156};
GN ORFNames=PV09_03674 {ECO:0000313|EMBL:KIW05118.1};
OS Verruconis gallopava.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Venturiales; Sympoventuriaceae; Verruconis.
OX NCBI_TaxID=253628 {ECO:0000313|EMBL:KIW05118.1, ECO:0000313|Proteomes:UP000053259};
RN [1] {ECO:0000313|EMBL:KIW05118.1, ECO:0000313|Proteomes:UP000053259}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 43764 {ECO:0000313|EMBL:KIW05118.1,
RC ECO:0000313|Proteomes:UP000053259};
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 Ochroconis gallopava CBS43764.";
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; KN847538; KIW05118.1; -; Genomic_DNA.
DR RefSeq; XP_016214987.1; XM_016356898.1.
DR AlphaFoldDB; A0A0D2ADP9; -.
DR STRING; 253628.A0A0D2ADP9; -.
DR MEROPS; S10.014; -.
DR GeneID; 27311647; -.
DR VEuPathDB; FungiDB:PV09_03674; -.
DR HOGENOM; CLU_008523_12_3_1; -.
DR InParanoid; A0A0D2ADP9; -.
DR OrthoDB; 1647009at2759; -.
DR Proteomes; UP000053259; 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:UP000053259};
KW Signal {ECO:0000256|RuleBase:RU361156}.
FT SIGNAL 1..22
FT /evidence="ECO:0000256|RuleBase:RU361156"
FT CHAIN 23..567
FT /note="Carboxypeptidase"
FT /evidence="ECO:0000256|RuleBase:RU361156"
FT /id="PRO_5006514704"
SQ SEQUENCE 567 AA; 62598 MW; 92513E1692B64BCB CRC64;
MPSMKVALTF LTSLVLAGSS GAAPNILAKS KGLSEKRQSG YGSASPWLTE KTKQFAVNGS
AIPDVPFDVG ESYAGLLPIS SDPNEERKLY FWFFPSSNPN ATNEVGMWFN GGPGCSSLSG
LLTENGPFIW QDGTLAPVQN PYSWHNLTNY VWIEQPVGVG FTTGVPNITN EVELGQQFIG
FWKNFVDTFD MHNFDMYLTG ESYAGFYVPY IADAFIGAND TVYYNLKGIA INDPIIGDET
NQGQVTIMPY VHAFQELLYL NDTFLETMDQ WNDHCNYSSY MEKYLTFPPP NEIFPVLPDP
YYSDTYECDI FDDIYAAALE VNPCFNIYHI TETCPHPYSE LGIINPGDYS PPGAQVYFNR
TDVQEAINAP VGTNWQQCTD VNVFGNQPTR TTNYSAGHDL SLGPAQNGVL QRVIEYTNNV
IIGSGNLDFL LNTNGTLLAI QNMTWNGLQG LQEYPGTPFY VPYHPEYNGG ALAGAGILGY
WGAERGLTFY QVQLAGHELP GYAAGAGYRA LELLLGRVSS FSDESSFTTQ SGNFTGEGII
YKQTATRDPR KQRLLNARIG GRAQRIV
//
