ID A0A135LUB7_PENPA Unreviewed; 530 AA.
AC A0A135LUB7;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=Carboxypeptidase {ECO:0000256|RuleBase:RU361156};
DE EC=3.4.16.- {ECO:0000256|RuleBase:RU361156};
GN ORFNames=PGRI_088390 {ECO:0000313|EMBL:KXG52555.1};
OS Penicillium patulum (Penicillium griseofulvum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=5078 {ECO:0000313|EMBL:KXG52555.1, ECO:0000313|Proteomes:UP000070168};
RN [1] {ECO:0000313|EMBL:KXG52555.1, ECO:0000313|Proteomes:UP000070168}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PG3 {ECO:0000313|EMBL:KXG52555.1,
RC ECO:0000313|Proteomes:UP000070168};
RX PubMed=26729047; DOI=10.1186/s12864-015-2347-x;
RA Banani H., Marcet-Houben M., Ballester A.R., Abbruscato P.,
RA Gonzalez-Candelas L., Gabaldon T., Spadaro D.;
RT "Genome sequencing and secondary metabolism of the postharvest pathogen
RT Penicillium griseofulvum.";
RL BMC Genomics 17:19-19(2016).
CC -!- SIMILARITY: Belongs to the peptidase S10 family.
CC {ECO:0000256|ARBA:ARBA00009431, ECO:0000256|RuleBase:RU361156}.
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:KXG52555.1}.
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DR EMBL; LHQR01000026; KXG52555.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A135LUB7; -.
DR STRING; 5078.A0A135LUB7; -.
DR OMA; LNSTCYG; -.
DR OrthoDB; 1647009at2759; -.
DR Proteomes; UP000070168; Unassembled WGS sequence.
DR GO; GO:0004185; F:serine-type carboxypeptidase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0017000; P:antibiotic biosynthetic process; IEA:UniProt.
DR GO; GO:0072330; P:monocarboxylic acid biosynthetic process; IEA:UniProt.
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:UP000070168};
KW Signal {ECO:0000256|RuleBase:RU361156}.
FT SIGNAL 1..22
FT /evidence="ECO:0000256|RuleBase:RU361156"
FT CHAIN 23..530
FT /note="Carboxypeptidase"
FT /evidence="ECO:0000256|RuleBase:RU361156"
FT /id="PRO_5007747032"
SQ SEQUENCE 530 AA; 58264 MW; 1ABD1322BF6DB480 CRC64;
MNISAFLYFF HVLWAAPGFV LSRGIGAHDT SRFRVHALPG VSDLPSSWAG RLPVPETENG
NEIFFWLFES EKRAYDDNLI IWFNGGPGCS SLIGLTTGNG PISFDGNSTR FIRNPHSWTK
LGNVLYVDQP VGTGFSTASF PYPVKDNGRI TTDFTQWLRG FFEYFPHLQS KQIHLMGESY
AGIYIPYFAS ELLEGNNSLS LNVRSMSLGD GSWGNGAAMA AVAMGKYIRS QLGLLQIPEN
VLSVFDEADR TCGFNDVLAK SAIYPPQAKI HIPGNPEYFN LRRRDLTNAA NGACNISPTT
PEEVRTSIFN STCYGPCATF STASDYLTAI STNRTTRGCF DIYDISHDCN AVSELPLMAE
YFGRADVQTA LHVENSGPYS ACNSTILNTL LSAPSPVPPE YYILPSLVTK HNISLHIYSG
EWDMLINHFG AELSLQNMTW RGVQGFAQKP TKPFFADNAA PSKTKQLLLE HTPAATTLST
ATPTAVAGTW AMERGVSYHL FRGAGHSIFV NKPREMFSFV RDVVVARGGL
//