ID A0A0S3RSX3_PHAAN Unreviewed; 605 AA.
AC A0A0S3RSX3;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 24-JAN-2024, entry version 25.
DE RecName: Full=XPG-I domain-containing protein {ECO:0008006|Google:ProtNLM};
GN Name=Vigan.04G090200 {ECO:0000313|EMBL:BAT83706.1};
GN ORFNames=VIGAN_04090200 {ECO:0000313|EMBL:BAT83706.1};
OS Vigna angularis var. angularis.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC NPAAA clade; indigoferoid/millettioid clade; Phaseoleae; Vigna.
OX NCBI_TaxID=157739 {ECO:0000313|EMBL:BAT83706.1, ECO:0000313|Proteomes:UP000291084};
RN [1] {ECO:0000313|EMBL:BAT83706.1, ECO:0000313|Proteomes:UP000291084}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Shumari {ECO:0000313|Proteomes:UP000291084};
RX PubMed=26616024; DOI=10.1038/srep16780;
RA Sakai H., Naito K., Ogiso-Tanaka E., Takahashi Y., Iseki K., Muto C.,
RA Satou K., Teruya K., Shiroma A., Shimoji M., Hirano T., Itoh T., Kaga A.,
RA Tomooka N.;
RT "The power of single molecule real-time sequencing technology in the de
RT novo assembly of a eukaryotic genome.";
RL Sci. Rep. 5:16780-16780(2015).
CC -!- SIMILARITY: Belongs to the XPG/RAD2 endonuclease family. GEN subfamily.
CC {ECO:0000256|ARBA:ARBA00038112}.
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DR EMBL; AP015037; BAT83706.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0S3RSX3; -.
DR Proteomes; UP000291084; Chromosome 4.
DR GO; GO:0004518; F:nuclease activity; IEA:UniProtKB-KW.
DR CDD; cd09869; PIN_GEN1; 1.
DR Gene3D; 1.10.150.20; 5' to 3' exonuclease, C-terminal subdomain; 1.
DR Gene3D; 3.40.50.1010; 5'-nuclease; 1.
DR InterPro; IPR036279; 5-3_exonuclease_C_sf.
DR InterPro; IPR029060; PIN-like_dom_sf.
DR InterPro; IPR006086; XPG-I_dom.
DR InterPro; IPR006084; XPG/Rad2.
DR InterPro; IPR006085; XPG_DNA_repair_N.
DR PANTHER; PTHR11081; FLAP ENDONUCLEASE FAMILY MEMBER; 1.
DR PANTHER; PTHR11081:SF59; FLAP ENDONUCLEASE GEN HOMOLOG 1; 1.
DR Pfam; PF00867; XPG_I; 1.
DR Pfam; PF00752; XPG_N; 1.
DR PRINTS; PR00853; XPGRADSUPER.
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.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Nuclease {ECO:0000256|ARBA:ARBA00022722};
KW Reference proteome {ECO:0000313|Proteomes:UP000291084}.
FT DOMAIN 1..97
FT /note="XPG N-terminal"
FT /evidence="ECO:0000259|SMART:SM00485"
FT DOMAIN 128..198
FT /note="XPG-I"
FT /evidence="ECO:0000259|SMART:SM00484"
FT REGION 518..605
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 518..533
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 534..557
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 558..582
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 605 AA; 68711 MW; CE9F17854FF50179 CRC64;
MGVGGNFWEL LKPYARREGF DFLRNKRVAV DLSFWIVQHE NAMKATHVRK PHLRLTFFRT
INLFSKFGVL PVFIVDGTPS PLKAQARIAR YFGSCGIELT SLPVSEGVSA ERSSLFSSRV
QECVELVKLL GMPVLQAKGE AEALCAQLNS EGHVDACITA DSDAFLFGAK CIIKCFCPNS
KEPFECYNMS DIEAGLGLKR KHLIAISLLV GNDHDMNGVR GIGLDNALHF AKAFNEDDIL
NRLQEIGKGD TSQIPSCTKF EDNIDVDGNC PNTKQPHCSL CGHPGSKKDH MKFSCESCVT
KDDEGCQRKP EGFKCDCCSC VLNRRHKEQK REENRYSKIC HKIAEEPNFP KDEIIDMYLC
NDNGYFSASD GPRIIWGKPN IEMLIDFLNF HQHWEPSYIR RTMFPMMSTI FLRDMSTPTG
ETLLFGQYEF DSVERVKMRY GYQFYVVKWK RAGVNINTSK VPSNESSVQQ DVVELDEMVD
LLDDAPEIHV DGCNFLFTDE NMDLVGTAFP AEVKSFLQEQ ERKRRKNSKS RCQENEKPAS
PNSRSTQLSI TEFFPSTKIK HRQSKQREES SNDADSEGSK SSKMKRNMSN SDNLPKSVRR
RLLFD
//