ID A0A1V6T8N2_9EURO Unreviewed; 526 AA.
AC A0A1V6T8N2;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE RecName: Full=Peptidase S33 tripeptidyl aminopeptidase-like C-terminal domain-containing protein {ECO:0000259|Pfam:PF08386};
GN ORFNames=PENSTE_c010G04984 {ECO:0000313|EMBL:OQE22280.1};
OS Penicillium steckii.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=303698 {ECO:0000313|EMBL:OQE22280.1, ECO:0000313|Proteomes:UP000191285};
RN [1] {ECO:0000313|Proteomes:UP000191285}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IBT 24891 {ECO:0000313|Proteomes:UP000191285};
RX PubMed=28368369; DOI=10.1038/nmicrobiol.2017.44;
RA Nielsen J.C., Grijseels S., Prigent S., Ji B., Dainat J., Nielsen K.F.,
RA Frisvad J.C., Workman M., Nielsen J.;
RT "Global analysis of biosynthetic gene clusters reveals vast potential of
RT secondary metabolite production in Penicillium species.";
RL Nat. Microbiol. 2:17044-17044(2017).
CC -!- SIMILARITY: Belongs to the peptidase S33 family.
CC {ECO:0000256|ARBA:ARBA00010088}.
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:OQE22280.1}.
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DR EMBL; MLKD01000010; OQE22280.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1V6T8N2; -.
DR STRING; 303698.A0A1V6T8N2; -.
DR OrthoDB; 1833441at2759; -.
DR Proteomes; UP000191285; Unassembled WGS sequence.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0017000; P:antibiotic biosynthetic process; IEA:UniProt.
DR GO; GO:0072330; P:monocarboxylic acid biosynthetic process; IEA:UniProt.
DR Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR013595; Pept_S33_TAP-like_C.
DR PANTHER; PTHR43248; 2-SUCCINYL-6-HYDROXY-2,4-CYCLOHEXADIENE-1-CARBOXYLATE SYNTHASE; 1.
DR PANTHER; PTHR43248:SF29; AB HYDROLASE-1 DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF08386; Abhydrolase_4; 1.
DR SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Reference proteome {ECO:0000313|Proteomes:UP000191285};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..18
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 19..526
FT /note="Peptidase S33 tripeptidyl aminopeptidase-like C-
FT terminal domain-containing protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5012709199"
FT DOMAIN 407..500
FT /note="Peptidase S33 tripeptidyl aminopeptidase-like C-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF08386"
SQ SEQUENCE 526 AA; 56009 MW; 5CA3D534E5BF4DF9 CRC64;
MQTFIFSYFL SLVVCATAAP STSGVSIHNT RGSGKIQWDP CGDLGVNGTT KLECGNITVP
LDYTEPDSGE TLDLQILRAP APNQPSKGSV FFNFGGPGAS GIPQMSLMGS VLSVFVGGSY
DIVNVVPRGT GSTLPFSCYA DEQERIKSNL RAPVATNASD TSLGEVWAEV KNIADACAHT
QNETGAFIGT AFTARDIMNV VDALEEDGKL RWWGQSYGTL LGSTLIAMFP DKVDKAVLDG
VMNAHEYYHI NVEQVSDADS AFSGFCSQCV ENKDNCPIAG NRTAEELEDG IYRAMEALKS
EPIPVSVDGQ GYIVDYSTIK GTIYNALYFP ATWPRLAQKL DIMFSGNITG ILNDLVAPLP
ATPDAEASKG IKCSDNQDPL KALEDALPGV EARAKLSKIG GDVADFSALQ CARWGMQAKE
QYTGDFKVKT ENPVLLVGTQ NDPITPLTSA KKMSEGFEGS VVLEQEGYGH TITSQGSSCT
IKTIMAYFND GILPEPNTIC EVDAVPFSGD DGLAVVLEGL TNAAGR
//
