ID A0A163DF33_DIDRA Unreviewed; 577 AA.
AC A0A163DF33;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE SubName: Full=Threonine-type endopeptidase {ECO:0000313|EMBL:KZM23119.1};
GN ORFNames=ST47_g5769 {ECO:0000313|EMBL:KZM23119.1};
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:KZM23119.1, ECO:0000313|Proteomes:UP000076837};
RN [1] {ECO:0000313|EMBL:KZM23119.1, ECO:0000313|Proteomes:UP000076837}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ArDII {ECO:0000313|EMBL:KZM23119.1,
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:KZM23119.1}.
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; JYNV01000200; KZM23119.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A163DF33; -.
DR STRING; 5454.A0A163DF33; -.
DR Proteomes; UP000076837; Unassembled WGS sequence.
DR GO; GO:0005839; C:proteasome core complex; IEA:InterPro.
DR GO; GO:0051603; P:proteolysis involved in protein catabolic process; IEA:InterPro.
DR CDD; cd03760; proteasome_beta_type_4; 1.
DR CDD; cd08946; SDR_e; 1.
DR Gene3D; 3.60.20.10; Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR InterPro; IPR001509; Epimerase_deHydtase.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR029055; Ntn_hydrolases_N.
DR InterPro; IPR016295; Proteasome_beta4.
DR InterPro; IPR001353; Proteasome_sua/b.
DR InterPro; IPR023333; Proteasome_suB-type.
DR PANTHER; PTHR43103; NUCLEOSIDE-DIPHOSPHATE-SUGAR EPIMERASE; 1.
DR PANTHER; PTHR43103:SF6; PUTATIVE-RELATED; 1.
DR Pfam; PF01370; Epimerase; 1.
DR Pfam; PF00227; Proteasome; 1.
DR SUPFAM; SSF56235; N-terminal nucleophile aminohydrolases (Ntn hydrolases); 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR PROSITE; PS51476; PROTEASOME_BETA_2; 1.
PE 4: Predicted;
KW Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023277};
KW Reference proteome {ECO:0000313|Proteomes:UP000076837}.
FT DOMAIN 265..455
FT /note="NAD-dependent epimerase/dehydratase"
FT /evidence="ECO:0000259|Pfam:PF01370"
SQ SEQUENCE 577 AA; 64484 MW; 5E00E493EA08A40F CRC64;
MNHLPQAWGR PRDDVYGAYD HSHFQSMGPT QHSQQPIVTG TSVLAAKFKD GVVIAADNLA
SYGSLARFTD VKRLRKFNDE VVVGFGGDVS DMQYLDRLLN SLDIRENYSS TDDSLNAKNL
HTYLAKVMYN RRSKFDPLWN HLLIAGLDGE GKPFLASADL LGTTFSSPSI ATGFGAHLAQ
PIMRTILPDE ASVQNVTKEQ AVEKVKECMK VLFYRDARSM DRYSIAVITK DGVDLNEDVK
LENQSWAFAE RIRGYGTQTA SKKRIVITGG SGVVGRCVIE KLLSYGHEIL NVDQTPLDNP
KVHTLKADLT DGAQAFNALS CHFQISEPFL EEMRAPDVVI HLAGIPQPNR IPDNETFRVN
MLSSYAIIEA ACKLGIKKII LASSITVYGV TYAEGNVSFP HFPITEATPT EPMDVYATSK
VCMERVAASF EKRFRAMARP VDMYCLRFGA VVTPGCHQRT MTAYLDRPRD WKVHAWSYVD
ARDLGNLVQC CIETDGLGFE VFNAVNDENT LPDGDAHTID WLRHFCPESE ILDEEALSGK
KAPISNRKAK ELLGFKEEFP WRAERTKWVA QGIRDER
//