ID A0A0R3VU12_TAEAS Unreviewed; 742 AA.
AC A0A0R3VU12;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 2.
DT 24-JAN-2024, entry version 34.
DE SubName: Full=XPGN domain-containing protein {ECO:0000313|WBParaSite:TASK_0000077001-mRNA-1};
GN ORFNames=TASK_LOCUS771 {ECO:0000313|EMBL:VDK21765.1};
OS Taenia asiatica (Asian tapeworm).
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Platyhelminthes; Cestoda;
OC Eucestoda; Cyclophyllidea; Taeniidae; Taenia.
OX NCBI_TaxID=60517 {ECO:0000313|Proteomes:UP000046400, ECO:0000313|WBParaSite:TASK_0000077001-mRNA-1};
RN [1] {ECO:0000313|WBParaSite:TASK_0000077001-mRNA-1}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (APR-2016) to UniProtKB.
RN [2] {ECO:0000313|EMBL:VDK21765.1, ECO:0000313|Proteomes:UP000282613}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG Pathogen Informatics;
RL Submitted (NOV-2018) 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}.
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DR EMBL; UYRS01000119; VDK21765.1; -; Genomic_DNA.
DR STRING; 60517.A0A0R3VU12; -.
DR WBParaSite; TASK_0000077001-mRNA-1; TASK_0000077001-mRNA-1; TASK_0000077001.
DR Proteomes; UP000046400; Unplaced.
DR Proteomes; UP000282613; 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; cd09868; PIN_XPG_RAD2; 1.
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; 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; 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.
PE 3: Inferred from homology;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW DNA damage {ECO:0000256|ARBA:ARBA00022763};
KW DNA repair {ECO:0000256|ARBA:ARBA00023204};
KW Endonuclease {ECO:0000256|ARBA:ARBA00022759};
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:UP000282613}.
FT DOMAIN 16..109
FT /note="XPG N-terminal"
FT /evidence="ECO:0000259|SMART:SM00485"
FT DOMAIN 581..656
FT /note="XPG-I"
FT /evidence="ECO:0000259|SMART:SM00484"
FT REGION 330..450
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 469..528
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 544..571
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 330..351
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 352..383
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 412..449
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 477..496
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 742 AA; 83294 MW; D55C3A8EF98F93C2 CRC64;
MIIFFSLAAT RSPQIMGVKG LWQILEPSRR RVDLEHFRGK RVAIDMNIWL YQALKAKAKG
GRNRHLAILF RRICKLLFFG IRPVFVFDGA VPALKKATMT ARRISRITAQ EKSNQARDRL
LRRLFRRLAE NATKSQEQSR KLAAEFLERF NSTEAIRKAE LDVEMFGTQS NPINAVPPTG
VLHLEEEQES ASQLAWDFVD NSHSIDLQSD AFNALPAQVQ LQVILILLNA PIQPSSQSAQ
VGESFSQTQV NRLIARRDLT IKKVEIESKM NEVLLASVVP QNLPSGPDIS VTVQRIASQD
EGHAILLRRR SSKEQADELK ERLNRLLEHP VNGPVRDDEE YLKRENSPRK DVQTIESSNI
GAKARISKTS EEYSSSESEV CQAVHSDAQL AKDEESTDFG KDQVNQVIEL EEPLDQPRES
TTEAKVDDVK EEGDLKPEEG SDSEVSSTDS HEFIDVLNDS AAPKACSDLE QVVSQPEGNE
DVDRERRHEN KQRSVEVETT VVEVPSEVPS SDLGEFADVS EPPTPAQSIE TLPKTQTFLE
PEVEDDLTID DDALRAELEK LERQAQETTT SCVVEAQRLV QLFGFPLVNS PEEAEAQCCH
LQQLGLVDVV ASDDSDVWVF GATLVCRHLF GRDKQRAKSS STSLYCLKDI REQLGLDRQQ
FVRIALLCGS DYTDGLDKIG PIKALEILST FTTTSDPDSI PEEHEILLPL KEFRRKCQER
GCRWASTKFP AGKQTYLKGI IC
//
