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Database: UniProt
Entry: A0A0F0HZN5_ASPPU
LinkDB: A0A0F0HZN5_ASPPU
Original site: A0A0F0HZN5_ASPPU 
ID   A0A0F0HZN5_ASPPU        Unreviewed;       525 AA.
AC   A0A0F0HZN5;
DT   24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT   24-JUN-2015, sequence version 1.
DT   27-MAR-2024, entry version 18.
DE   SubName: Full=TAP-like protein {ECO:0000313|EMBL:KJK60954.1};
GN   ORFNames=P875_00042826 {ECO:0000313|EMBL:KJK60954.1};
OS   Aspergillus parasiticus (strain ATCC 56775 / NRRL 5862 / SRRC 143 / SU-1).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX   NCBI_TaxID=1403190 {ECO:0000313|EMBL:KJK60954.1, ECO:0000313|Proteomes:UP000033540};
RN   [1] {ECO:0000313|EMBL:KJK60954.1, ECO:0000313|Proteomes:UP000033540}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 56775 / NRRL 5862 / SRRC 143 / SU-1
RC   {ECO:0000313|Proteomes:UP000033540};
RA   Yu J., Fedorova N., Yin Y., Losada L., Zafar N., Taujale R., Ehrlich K.C.,
RA   Bhatnagar D., Cleveland T.E., Bennett J.W., Nierman W.C.;
RT   "Draft genome sequence of Aspergillus parasiticus SU-1.";
RL   Submitted (FEB-2015) to the EMBL/GenBank/DDBJ databases.
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:KJK60954.1}.
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DR   EMBL; JZEE01000701; KJK60954.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0F0HZN5; -.
DR   STRING; 1403190.A0A0F0HZN5; -.
DR   Proteomes; UP000033540; 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; IPR000073; AB_hydrolase_1.
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; PF00561; Abhydrolase_1; 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:UP000033540};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           24..525
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5002442949"
FT   DOMAIN          110..236
FT                   /note="AB hydrolase-1"
FT                   /evidence="ECO:0000259|Pfam:PF00561"
FT   DOMAIN          403..501
FT                   /note="Peptidase S33 tripeptidyl aminopeptidase-like C-
FT                   terminal"
FT                   /evidence="ECO:0000259|Pfam:PF08386"
SQ   SEQUENCE   525 AA;  56112 MW;  DC426DE1E7E4B63E CRC64;
     MRQSSSFTAG LLSLASLASL TQAELGKIQW KGLCDPTNAT GPMICGTLDV PLDYTDSTSN
     KTLTLDIGKW PATKKATAEP VFVNFGGPGV NSFEGLGSYG KEFQTILGGH SDVITFNPRG
     VGNTIPFSCY SNDSSRELAS LQAPKDGTAS NTARGEIWAQ STNYAQACYA QNGENGSLIG
     TTFAARDTLQ VLDALRGKDA KLNYWGISYG TTVGAVMAAM FPERMGYLAL DGVDNPTEYF
     NGYNAQSVAD VDTVLKGFCS GCFDAPELCP LAKTYSSAAN LEAAIYVMLD ELKFNPIPIP
     SNGGVVTYVD VKSTIDEALY APSSWPLTSE LIYYVQTRNA TVLGSSEVYS TIKSYGLSAS
     LTSSSNEVES GIRCSDKAAS ASMADVLPYS NVRAALSRIA SDGANTDMRC AQWNKKMYAK
     ERYTGDFDVK TPRPVLVLSN RYDPSTPLAA AKNLTATFEG SVLLEQNGYG HTTLSVPSLC
     TAKVVRAYFS NGTLPAEGTI CEIDVPLFTN LTYEDVWPKS FQAGL
//
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