ID A0A2V1BWE3_9HELO Unreviewed; 1170 AA.
AC A0A2V1BWE3;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 27-MAR-2024, entry version 17.
DE SubName: Full=PIN domain-like protein {ECO:0000313|EMBL:PVH77678.1};
DE Flags: Fragment;
GN ORFNames=DL98DRAFT_495303 {ECO:0000313|EMBL:PVH77678.1};
OS Cadophora sp. DSE1049.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Helotiales; Helotiales incertae sedis; Cadophora.
OX NCBI_TaxID=1485229 {ECO:0000313|EMBL:PVH77678.1, ECO:0000313|Proteomes:UP000244409};
RN [1] {ECO:0000313|EMBL:PVH77678.1, ECO:0000313|Proteomes:UP000244409}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSE1049 {ECO:0000313|EMBL:PVH77678.1,
RC ECO:0000313|Proteomes:UP000244409};
RX PubMed=29679020; DOI=10.1038/s41598-018-24686-4;
RA Knapp D.G., Nemeth J.B., Barry K., Hainaut M., Henrissat B., Johnson J.,
RA Kuo A., Lim J.H.P., Lipzen A., Nolan M., Ohm R.A., Tamas L.,
RA Grigoriev I.V., Spatafora J.W., Nagy L.G., Kovacs G.M.;
RT "Comparative genomics provides insights into the lifestyle and reveals
RT functional heterogeneity of dark septate endophytic fungi.";
RL Sci. Rep. 8:6321-6321(2018).
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}.
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DR EMBL; KZ804173; PVH77678.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2V1BWE3; -.
DR STRING; 1485229.A0A2V1BWE3; -.
DR Proteomes; UP000244409; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0004519; F:endonuclease activity; IEA:InterPro.
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; PF02809; UIM; 2.
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; 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 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:UP000244409}.
FT DOMAIN 1..98
FT /note="XPG N-terminal"
FT /evidence="ECO:0000259|SMART:SM00485"
FT DOMAIN 913..982
FT /note="XPG-I"
FT /evidence="ECO:0000259|SMART:SM00484"
FT REGION 113..139
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 421..485
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 499..656
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 680..821
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1148..1170
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 425..439
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 506..535
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 578..592
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 613..651
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1155..1170
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1170
FT /evidence="ECO:0000313|EMBL:PVH77678.1"
SQ SEQUENCE 1170 AA; 130227 MW; A4EB7A63C0102134 CRC64;
MGVTGLWPIL APSARPTPLP TLNKKRLAVD ASIWIYQFLK AVRDKEGNAL RNSHVVGFFR
RICKLLFFGI KPVFVFDGGA PVLKRQTIQG RKRRREGRRE DAVRTAGKLL AVQMKRRGEE
EEEKRKRDAK RERERGGRPA VQIEEEVIPE GADLVYVGEM GMSSAERNKN RTFRKTDAYH
LPELTNGIEG MGQPNDPRIM SAEDLEEYAR QFHNGEDVNL YDFSKIDFNG EFFLSLPAGD
RYNILNAARL RSRLRMGHSK EQLDGMFPDR MAFSRFQIDR VRERNELTQR LMNLNGMNDL
PGVGGGRIAG ERGREYVLVK NEGAEGGYAL GVVSTDKGLG GKDKPIDIDA IPKRVKEDSE
SEDEFEDVPV EGLNRLPKLS TKDKLNLTYT EFQAQELAEQ RKKKLFDEEE DDLNQAIALS
LQKDGNDAES DEDDHLNRAI AMSLQKNHAP ESDPEDEMDF EDVPMPEYEQ KAAAESAKPI
SGSSGGMIAH IVNNRANAAI PKRKAVSVDA DSDSDSDMDM KAALAKARKQ KAPEKRNQPA
PIALNKKNPF DGPLPFESLG SIFAKKSKPI QQPDESGNGS PDDEDMAGGF DNEPEEDAPR
SLPPWLSGGD IRNQVEEQKE RDRELNAEDR EQADEEERMY RKAHGPIQID SSDDDSDFEI
VDALEPKRTS ENLEVLVDMA ESRQASPKST GDVVGAPVSD QAIPETFGEL AEDVRAEPPV
SSIPDNRPRS AEQSSKEMED EEVEWSDSEY GDTLTSKKAV DADQPAGRND ASLSKSASPE
FEDVEMPAPE VEAGNGSPPA GSPSPLFNDA GLPDTLPAQL PDDDSFAIRE RAEIDAEFDD
FSDPEDEELL AQLAVEAETH AQFTNALNNR TEQETQATFE QELKSLRNQQ KKDRRDADEV
TQVMINECQA LLRLFGIPYI TAPMEAEAQC AELVRLGLVD GVVTDDCDIF LFGGTRVYKN
MFNSNKFVEC YLSTDIEKEL SLSRDQLISI AHLLGSDYTE GLPGVGPVTA VEILSEFPTS
TGLQEFKEWW SIVQINGPPL NTEPTTFRKK FRRAQGTKLF LPPTFPSPAV TEAYLKPDVD
SSPDAFQWGV PDLDRLREFL MATIGWTQER TDEVLVPVIR DMNRREQEGT QANITRYFDG
AVGAGVNTGG GGRDKVTSKR MKDAVGKLRA
//
