ID A0A163IBH4_DIDRA Unreviewed; 570 AA.
AC A0A163IBH4;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 16.
DE SubName: Full=Hydrolase {ECO:0000313|EMBL:KZM25686.1};
GN ORFNames=ST47_g3174 {ECO:0000313|EMBL:KZM25686.1};
OS Didymella rabiei (Chickpea ascochyta blight fungus) (Mycosphaerella
OS rabiei).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Pleosporineae; Didymellaceae; Ascochyta.
OX NCBI_TaxID=5454 {ECO:0000313|EMBL:KZM25686.1, ECO:0000313|Proteomes:UP000076837};
RN [1] {ECO:0000313|EMBL:KZM25686.1, ECO:0000313|Proteomes:UP000076837}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ArDII {ECO:0000313|EMBL:KZM25686.1,
RC ECO:0000313|Proteomes:UP000076837};
RX PubMed=27091329; DOI=10.1038/srep24638;
RA Verma S., Gazara R.K., Nizam S., Parween S., Chattopadhyay D., Verma P.K.;
RT "Draft genome sequencing and secretome analysis of fungal phytopathogen
RT Ascochyta rabiei provides insight into the necrotrophic effector
RT repertoire.";
RL Sci. Rep. 6:24638-24638(2016).
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:KZM25686.1}.
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DR EMBL; JYNV01000122; KZM25686.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A163IBH4; -.
DR STRING; 5454.A0A163IBH4; -.
DR Proteomes; UP000076837; 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, ECO:0000313|EMBL:KZM25686.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000076837};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..25
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 26..570
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5007843096"
FT DOMAIN 93..261
FT /note="AB hydrolase-1"
FT /evidence="ECO:0000259|Pfam:PF00561"
FT DOMAIN 428..529
FT /note="Peptidase S33 tripeptidyl aminopeptidase-like C-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF08386"
SQ SEQUENCE 570 AA; 62644 MW; E9344D7012163DFE CRC64;
MPRSAIASSI FLSISLAFSA DVALSYDTNS LKWAPCDLDF SSEIQLEVAA HAEPLFCATL
PVPLDYTNRK NGQFLDLQLI KIKATKEPFK GSVLTNPGGP GGSGVDWIAT DGPSIRNDLG
GHHDVIGFDP RGTGRTIPFY CIQSNSTSPN NKRAEYNFTI PQDDMYSVLK AKAWRDGGKY
AEDCASTPGN SDIAPYISTP FVARDMLKII DALGEDKLQY WGISYGTVLG QTFAGMFPDR
VKRIVLDSTV RFDDYHAGHW ITVTRDTERA LVNFFTECVN VGSELCPIAN FTGPNATPED
LHNEYAKVFQ ELLDDPVFMP DDYHPLPWWQ PGSITISQIL KYSTLASAYR PRQFGELDII
VDIALRRAWD EWIALSTPLP SNSTTPEVPW NLGSNAFHGI TCGDGAFRAN TPEDMHSLVL
AQASAGTFSD GFAPQIWPCA QWKFEVKERY TGPFTAINTS YPILFVNGNH DPITPLSTAY
EASANFPSSR LVVQNGHGHG TRNHPSACTN RAIADYFNDG TLPAAGTVCQ TDKTAYGVFE
DWLALQLGNS TDNSTIAKRS SENSRKFILV
//
