ID A0A162Y7D5_DIDRA Unreviewed; 1329 AA.
AC A0A162Y7D5;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE SubName: Full=Endonuclease {ECO:0000313|EMBL:KZM19858.1};
GN ORFNames=EKO05_003369 {ECO:0000313|EMBL:KAF9709664.1}, ST47_g9195
GN {ECO:0000313|EMBL:KZM19858.1};
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:KZM19858.1, ECO:0000313|Proteomes:UP000076837};
RN [1] {ECO:0000313|EMBL:KZM19858.1, ECO:0000313|Proteomes:UP000076837}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ArDII {ECO:0000313|EMBL:KZM19858.1,
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).
RN [2] {ECO:0000313|EMBL:KAF9709664.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Me14 {ECO:0000313|EMBL:KAF9709664.1};
RA Syme R.A., Farfan-Caceres L., Lichtenzveig J.;
RL Submitted (DEC-2018) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:KAF9709664.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Me14 {ECO:0000313|EMBL:KAF9709664.1};
RX PubMed=32345704; DOI=10.1534/g3.120.401265;
RA Shah R.M., Williams A.H., Hane J.K., Lawrence J.A., Farfan-Caceres L.M.,
RA Debler J.W., Oliver R.P., Lee R.C.;
RT "Reference Genome Assembly for Australian Ascochyta rabiei Isolate
RT ArME14.";
RL G3 (Bethesda) 10:2131-2140(2020).
RN [4] {ECO:0000313|EMBL:KAF9709664.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Me14 {ECO:0000313|EMBL:KAF9709664.1};
RA Shah R.M., Williams A.H., Hane J.K., Lawrence J.A., Farfan-Caceres L.M.,
RA Debler J.W., Oliver R.P., Lee R.C.;
RL Submitted (MAY-2020) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC -!- SIMILARITY: Belongs to the XPG/RAD2 endonuclease family. XPG subfamily.
CC {ECO:0000256|ARBA:ARBA00005283}.
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:KZM19858.1}.
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DR EMBL; RYYQ01000006; KAF9709664.1; -; Genomic_DNA.
DR EMBL; JYNV01000290; KZM19858.1; -; Genomic_DNA.
DR STRING; 5454.A0A162Y7D5; -.
DR OrthoDB; 5479162at2759; -.
DR Proteomes; UP000076837; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0004519; F:endonuclease activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0003697; F:single-stranded DNA binding; IEA:InterPro.
DR GO; GO:0006289; P:nucleotide-excision repair; IEA:InterPro.
DR CDD; cd09904; H3TH_XPG; 1.
DR CDD; cd09868; PIN_XPG_RAD2; 2.
DR Gene3D; 1.10.150.20; 5' to 3' exonuclease, C-terminal subdomain; 1.
DR Gene3D; 3.40.50.1010; 5'-nuclease; 2.
DR InterPro; IPR036279; 5-3_exonuclease_C_sf.
DR InterPro; IPR008918; HhH2.
DR InterPro; IPR029060; PIN-like_dom_sf.
DR InterPro; IPR003903; UIM_dom.
DR InterPro; IPR006086; XPG-I_dom.
DR InterPro; IPR006084; XPG/Rad2.
DR InterPro; IPR001044; XPG/Rad2_eukaryotes.
DR InterPro; IPR019974; XPG_CS.
DR InterPro; IPR006085; XPG_DNA_repair_N.
DR PANTHER; PTHR16171:SF7; DNA EXCISION REPAIR PROTEIN ERCC-5; 1.
DR PANTHER; PTHR16171; DNA REPAIR PROTEIN COMPLEMENTING XP-G CELLS-RELATED; 1.
DR Pfam; PF00867; XPG_I; 1.
DR Pfam; PF00752; XPG_N; 1.
DR PRINTS; PR00853; XPGRADSUPER.
DR PRINTS; PR00066; XRODRMPGMNTG.
DR SMART; SM00279; HhH2; 1.
DR SMART; SM00726; UIM; 2.
DR SMART; SM00484; XPGI; 1.
DR SMART; SM00485; XPGN; 1.
DR SUPFAM; SSF47807; 5' to 3' exonuclease, C-terminal subdomain; 1.
DR SUPFAM; SSF88723; PIN domain-like; 1.
DR PROSITE; PS50330; UIM; 2.
DR PROSITE; PS00841; XPG_1; 1.
DR PROSITE; PS00842; XPG_2; 1.
PE 3: Inferred from homology;
KW DNA damage {ECO:0000256|ARBA:ARBA00022763};
KW DNA repair {ECO:0000256|ARBA:ARBA00023204};
KW Endonuclease {ECO:0000313|EMBL:KZM19858.1};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nuclease {ECO:0000256|ARBA:ARBA00022722};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000076837}.
FT DOMAIN 1..98
FT /note="XPG N-terminal"
FT /evidence="ECO:0000259|SMART:SM00485"
FT DOMAIN 978..1047
FT /note="XPG-I"
FT /evidence="ECO:0000259|SMART:SM00484"
FT REGION 120..140
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 363..586
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 605..912
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1209..1329
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 372..392
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 451..467
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 468..486
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 605..686
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 788..805
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1280..1299
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1329 AA; 149587 MW; 694B846315F3DB21 CRC64;
MGVTGLWTVL QPCARPIKIE TLNKRRIAVD ASIWIYQFLK AVRDKEGNAL RNSHIVGFFR
RVCKLLFIGI KPVFVFDGGA PALKRQTISH RKSRREGKRD DAVRTAGKLL AIQMQKAAEE
EERKRKEAGR RPREEQEEEL PENLVYAEEI LQTQQERTEN RKFKKKDQYH LPDLGVPMSE
LGGDDPRIMS LEELEDYARQ FDRGEDINVY DFSKIDFDGI FFQSLPPADR YNILNAARLR
SRLRMGYSKD QLDAMFPDRM AFSRFQIERV RERSDLTQRL MNLNGMNDDT TFGTNRIAGD
KNREYVLVKN DGVEGGWALG VVTNKDEGKA HKPIDVDLPS RAAKVEEDWE SEDEFEDVPI
EGLNRLPKAK PGPSRETVEG REFISNELRR RRQTFYKSRK SRPTQAQPKR AVPVREDPDS
LFLAEDNEEE QWENVPTNGE NDLFEATGDN AEEEQLQQAI ALSMQQNNEK EAEDEVDERP
ALEEHQQQRA LETNPFKAAK GYRGSAIGRL ANQRANKLAP KGPFEGSDSE EDEMDLQAAL
AESRQSKRPT KPQRLPVPPR APASAVETDE QPESINTHGF DGPLPFEKLN LGTSLLGKKK
MEKIQQDTAG GFEKDTEEKK ESVPLPPWFK GERDIAQELD EYRDEEKREW EKDRKDEKEQ
FQFQQLPRLR KQEAREVIDL DADPSQSQKE KQIIAMDSDE EDDAEMEDVS TSYGQADNPT
EDDQVRMSDM ADTVRAEPPK LLADDQRAPP IQDPKLVKKM PFADDSDEDP VDWSESEPED
GKRAPSQRVQ YKTAQKVSSP SKSPSPEFED VPMNTDLTPA SAPAEIAQKS TSPEFEDVPM
HTEPADAPKS PSPDFEDVPI AAPARRPRRE PSPAFLQSPD DLEIPVVPHG GLADDNAPLD
LPGNDSDQYS DPEDEELFAS LAAEAEEHNR FAQEINNAAS HVDFETELKQ LRAQQKKDRR
DADEVTQTMI SECQHLLSLF GLPYITAPME AEAQCAELVT LGLVDGIVTD DSDTFLFGGT
RVYKNMFNAA KFVECYLAND LTSEFSLTRE KLIAIAQLLG SDYTTGIPGI GPVTALEIIS
EFPNLEDFKD WWTGVQNNTI PKEVDASNVF RRRFRKSQAT KLFLPPGFPD PRVADAYLNP
EVDSDPQPFQ WGVPDLAALR SFLSAQIGWS SERTDEVLVP VIKDMNRREK EGTQANITRF
FEGNVGAGAF APRVRGNTTG SGPSGKKKGK AAAGKRLGAA LTRLAEREGA RGGIDEEDDD
DKDTADVPTT GASTEPTETV AAKRSKRKAP ISLAALDDEH REEDNDDDED AAYQEPKKKK
AKRTRKAKA
//
