ID A0A163J5U5_DIDRA Unreviewed; 585 AA.
AC A0A163J5U5;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE SubName: Full=Hydrolase {ECO:0000313|EMBL:KZM26165.1};
GN ORFNames=ST47_g2712 {ECO:0000313|EMBL:KZM26165.1};
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:KZM26165.1, ECO:0000313|Proteomes:UP000076837};
RN [1] {ECO:0000313|EMBL:KZM26165.1, ECO:0000313|Proteomes:UP000076837}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ArDII {ECO:0000313|EMBL:KZM26165.1,
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 -!- 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:KZM26165.1}.
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DR EMBL; JYNV01000113; KZM26165.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A163J5U5; -.
DR STRING; 5454.A0A163J5U5; -.
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; IPR019339; CIR_N_dom.
DR InterPro; IPR002925; Dienelactn_hydro.
DR InterPro; IPR039875; LENG1-like.
DR PANTHER; PTHR22093; LEUKOCYTE RECEPTOR CLUSTER LRC MEMBER 1; 1.
DR PANTHER; PTHR22093:SF0; LEUKOCYTE RECEPTOR CLUSTER MEMBER 1; 1.
DR Pfam; PF10197; Cir_N; 1.
DR Pfam; PF01738; DLH; 1.
DR SMART; SM01083; Cir_N; 1.
DR SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
PE 4: Predicted;
KW Hydrolase {ECO:0000313|EMBL:KZM26165.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000076837}.
FT DOMAIN 10..46
FT /note="CBF1-interacting co-repressor CIR N-terminal"
FT /evidence="ECO:0000259|SMART:SM01083"
FT REGION 52..90
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 198..258
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 65..90
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 198..212
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 214..228
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 244..258
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 585 AA; 65504 MW; C2A477A7734FD304 CRC64;
MPLHLLGKKS WNVYNPANIA RVRADEEAAA ARDAAADQRM QDLDAERRAA LLRGRTPPPL
PEEPATHSDR TRAREGGHDT KRRKLAGEDD TDMDIRLAAS VANPTHGDHT DAKLLKLRTP
TSDAPLTDHA GNIDLFPVDV KEALKREKNA DAEKEKRRRE LAFEDQYTMR FSNAGGNNGL
QEPWYTARQK IAHPTYATTA APESSGFDTK NVWGNQDPRR KEREQARISS NDPFAFMQKA
QTQLKKSKQD RKKWSDERNR ELGELRDAQE KEERVQADIK IVIAIVDTHI VGPLHRDITG
VEALVAGHDK TSTLTHDQQV IHELYTSGSF PNHQCCVIGV KHEGTPKGDI KNIGDIRAYI
TYPENRSTQN AILIMTDVLG FEFPNVQLIA DQFAANGYFT IIPDVFNGNT VPLNPGPDFD
FPTWKATKMP REAAVDPIYA TVIKHLRGEL GVKRLGGVGY CFGGKYVCRW LKEGGLDAGY
TAHPSFVEVH ELKGIKGPLS VAAAETDFIF PAEKRRVTED VLKEMSVPYQ MTLYSDVEHG
FGVKGDLSHQ RARFAKELAF LQAVLWFDEY VKKETHDTPI PNPSC
//
