ID A0A0D1Z7Z9_EXOME Unreviewed; 609 AA.
AC A0A0D1Z7Z9;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE RecName: Full=Peptidase S33 tripeptidyl aminopeptidase-like C-terminal domain-containing protein {ECO:0000259|Pfam:PF08386};
GN ORFNames=PV10_05491 {ECO:0000313|EMBL:KIV90887.1};
OS Exophiala mesophila (Black yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Exophiala.
OX NCBI_TaxID=212818 {ECO:0000313|EMBL:KIV90887.1, ECO:0000313|Proteomes:UP000054302};
RN [1] {ECO:0000313|EMBL:KIV90887.1, ECO:0000313|Proteomes:UP000054302}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 40295 {ECO:0000313|EMBL:KIV90887.1,
RC ECO:0000313|Proteomes:UP000054302};
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 Exophiala mesophila CBS40295.";
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the peptidase S33 family.
CC {ECO:0000256|ARBA:ARBA00010088}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; KN847523; KIV90887.1; -; Genomic_DNA.
DR RefSeq; XP_016222461.1; XM_016370168.1.
DR AlphaFoldDB; A0A0D1Z7Z9; -.
DR STRING; 212818.A0A0D1Z7Z9; -.
DR GeneID; 27323336; -.
DR VEuPathDB; FungiDB:PV10_05491; -.
DR HOGENOM; CLU_013364_5_2_1; -.
DR OMA; YEILSWD; -.
DR OrthoDB; 1833441at2759; -.
DR Proteomes; UP000054302; Unassembled WGS sequence.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
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:SF25; PEPTIDASE S33 TRIPEPTIDYL AMINOPEPTIDASE-LIKE C-TERMINAL DOMAIN-CONTAINING PROTEIN-RELATED; 1.
DR Pfam; PF08386; Abhydrolase_4; 1.
DR SUPFAM; SSF53474; alpha/beta-Hydrolases; 2.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Reference proteome {ECO:0000313|Proteomes:UP000054302};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..22
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 23..609
FT /note="Peptidase S33 tripeptidyl aminopeptidase-like C-
FT terminal domain-containing protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002247601"
FT DOMAIN 491..600
FT /note="Peptidase S33 tripeptidyl aminopeptidase-like C-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF08386"
SQ SEQUENCE 609 AA; 66904 MW; 51BC7F5170491E96 CRC64;
MAVIWSPCLI LLLALLTTSC QAFVSPVPLP KHESPAVSFD WAGLQSSTGL NFRKCYGGSF
ECARLTVPLD WNDPINPNNI SLAIIRLPAV VDRTDKNFGG TIIINPGGPS GSGTDTLLLG
GRSLQKMIDS ERHFEILSFD PRGVKYTTPN VACFQDQLAR QVQDVFNVAV GGLDGSEDAL
NVKWAISQSL GTSCLDSGSF PDGSNIRQYV STALVARDMI EIVDKLHENL KAELKRTMRN
AGMQKPFDSD SAPYPTLPLL NYYGFSYGTY LGNTFASMFP HRVGRMILDG VVDADDYAAT
GWTTNLSDNM KTWTAFFDDC FAAGSKCPLY NSTFTTSSQL QEHVERFMEH LKENPLPLVV
NGNAALMTHF LLKVAIHSCL YTPNHLSPIL AKLLASLEKG RLGIKPVVLN DVDFRSEADT
IGFLPSLPPV PTLLRGHFGR PVGSPEDDYT WSLEAAVSIL CGDGDDITWR SKANQTDYLR
LLQSQSELDA AVWAEITLRC VHWPQALRPS DINRFTGPFQ SKLSDYHSRA SPLLFIGNTA
DPVTPVRNAH RMSSRHEGSV VLTQDMPGHC SSEISPTTCG FTATKAFFAN GTLPEPGLDC
KRTRWPWDT
//
