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Database: UniProt
Entry: A0A135LUB7_PENPA
LinkDB: A0A135LUB7_PENPA
Original site: A0A135LUB7_PENPA 
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
//
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