ID A0A395NSS2_TRIAR Unreviewed; 543 AA.
AC A0A395NSS2;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 16.
DE RecName: Full=Alpha/beta-hydrolase {ECO:0008006|Google:ProtNLM};
GN ORFNames=TARUN_3236 {ECO:0000313|EMBL:RFU79005.1};
OS Trichoderma arundinaceum.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Hypocreaceae; Trichoderma.
OX NCBI_TaxID=490622 {ECO:0000313|EMBL:RFU79005.1, ECO:0000313|Proteomes:UP000266272};
RN [1] {ECO:0000313|EMBL:RFU79005.1, ECO:0000313|Proteomes:UP000266272}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IBT 40837 {ECO:0000313|EMBL:RFU79005.1,
RC ECO:0000313|Proteomes:UP000266272};
RX PubMed=29649280; DOI=10.1371/journal.ppat.1006946;
RA Proctor R.H., McCormick S.P., Kim H.S., Cardoza R.E., Stanley A.M.,
RA Lindo L., Kelly A., Brown D.W., Lee T., Vaughan M.M., Alexander N.J.,
RA Busman M., Gutierrez S.;
RT "Evolution of structural diversity of trichothecenes, a family of toxins
RT produced by plant pathogenic and entomopathogenic fungi.";
RL PLoS Pathog. 14:e1006946-e1006946(2018).
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:RFU79005.1}.
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; PXOA01000181; RFU79005.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A395NSS2; -.
DR STRING; 490622.A0A395NSS2; -.
DR Proteomes; UP000266272; 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:UP000266272};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..28
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 29..543
FT /note="Alpha/beta-hydrolase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5017344964"
FT DOMAIN 109..261
FT /note="AB hydrolase-1"
FT /evidence="ECO:0000259|Pfam:PF00561"
FT DOMAIN 441..529
FT /note="Peptidase S33 tripeptidyl aminopeptidase-like C-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF08386"
SQ SEQUENCE 543 AA; 59737 MW; D4726AA940822D0F CRC64;
MTGSSGTSPS RKGAALAWLL AVTGFVCTNN GLAQASPLQF ARHEDGAVTY PGEHIAWAPC
GSATGHLLEC SAIKVPMDQF NKENSGNKTF DLSLIRIRGN NTRAGSKNIL YNPGGPGASG
VGSFYSLGPE LISIVGENFN IIAFDPRGIN GSTPLGSCYA NENIRMGMSN IPLDNLVTDA
PFMGSWAPNF AKSCAQISGE HGKYINTPQV AADMNSILDA IGQEDMWYWG QSYGTLIGQT
YAGLFPNRTA RMAIDGIVDQ FDWYQNTLPW KDYQDGKRVF WGFFDECIKA GVELCPLAAL
TKKPDVLNRL VENFGTRIKY EQMTVYVDET NFGAVSYAYL WFAAILPSLY SYLAWQPLGF
VLFDAMQGNA TLAYEAYGGS ESYSTAGIPP WEAIYFYRLN DGASGKEFWP QTNRGMIKML
EPFYIMNPFM YAANSFYWAK AQWLIPKTHT YVPRQGVKTK YPLLVLSNQH DPVCSLDSAK
SALASFADAR LVTLDAYGHC TFYQNSACAN NYVKEYFASG SLPEQDATCQ VGSDQYFPPL
PTV
//
