ID A0A0R0L7Y9_SOYBN Unreviewed; 1590 AA.
AC A0A0R0L7Y9;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 45.
DE RecName: Full=XPG-I domain-containing protein {ECO:0000259|SMART:SM00484};
GN Name=100820295 {ECO:0000313|EnsemblPlants:KRH75306};
GN ORFNames=GLYMA_01G077200 {ECO:0000313|EMBL:KRH75306.1};
OS Glycine max (Soybean) (Glycine hispida).
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; Glycine;
OC Glycine subgen. Soja.
OX NCBI_TaxID=3847 {ECO:0000313|EMBL:KRH75306.1};
RN [1] {ECO:0000313|EMBL:KRH75306.1, ECO:0000313|EnsemblPlants:KRH75306}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Williams 82 {ECO:0000313|EnsemblPlants:KRH75306};
RC TISSUE=Callus {ECO:0000313|EMBL:KRH75306.1};
RX PubMed=20075913; DOI=10.1038/nature08670;
RA Schmutz J., Cannon S.B., Schlueter J., Ma J., Mitros T., Nelson W.,
RA Hyten D.L., Song Q., Thelen J.J., Cheng J., Xu D., Hellsten U., May G.D.,
RA Yu Y., Sakurai T., Umezawa T., Bhattacharyya M.K., Sandhu D.,
RA Valliyodan B., Lindquist E., Peto M., Grant D., Shu S., Goodstein D.,
RA Barry K., Futrell-Griggs M., Abernathy B., Du J., Tian Z., Zhu L., Gill N.,
RA Joshi T., Libault M., Sethuraman A., Zhang X.-C., Shinozaki K.,
RA Nguyen H.T., Wing R.A., Cregan P., Specht J., Grimwood J., Rokhsar D.,
RA Stacey G., Shoemaker R.C., Jackson S.A.;
RT "Genome sequence of the palaeopolyploid soybean.";
RL Nature 463:178-183(2010).
RN [2] {ECO:0000313|EnsemblPlants:KRH75306}
RP IDENTIFICATION.
RC STRAIN=Williams 82 {ECO:0000313|EnsemblPlants:KRH75306};
RG EnsemblPlants;
RL Submitted (FEB-2018) to UniProtKB.
RN [3] {ECO:0000313|EMBL:KRH75306.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Callus {ECO:0000313|EMBL:KRH75306.1};
RA Schmutz J., Cannon S., Schlueter J., Ma J., Mitros T., Nelson W., Hyten D.,
RA Song Q., Thelen J., Cheng J., Xu D., Hellsten U., May G., Yu Y.,
RA Sakurai T., Umezawa T., Bhattacharyya M., Sandhu D., Valliyodan B.,
RA Lindquist E., Peto M., Grant D., Shu S., Goodstein D., Barry K.,
RA Futrell-Griggs M., Abernathy B., Du J., Tian Z., Zhu L., Gill N., Joshi T.,
RA Libault M., Sethuraman A., Zhang X., Shinozaki K., Nguyen H., Wing R.,
RA Cregan P., Specht J., Grimwood J., Rokhsar D., Stacey G., Shoemaker R.,
RA Jackson S.;
RT "WGS assembly of Glycine max.";
RL Submitted (JUL-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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DR EMBL; CM000834; KRH75306.1; -; Genomic_DNA.
DR RefSeq; XP_014629463.1; XM_014773977.1.
DR EnsemblPlants; KRH75306; KRH75306; GLYMA_01G077200.
DR GeneID; 100820295; -.
DR Gramene; KRH75306; KRH75306; GLYMA_01G077200.
DR OrthoDB; 26655at2759; -.
DR Proteomes; UP000008827; Chromosome 1.
DR ExpressionAtlas; A0A0R0L7Y9; baseline and differential.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0004518; F:nuclease activity; IEA:InterPro.
DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR GO; GO:0006259; P:DNA metabolic process; IEA:UniProt.
DR CDD; cd09904; H3TH_XPG; 1.
DR CDD; cd09868; PIN_XPG_RAD2; 1.
DR Gene3D; 6.10.250.1630; -; 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; IPR008918; HhH2.
DR InterPro; IPR025527; HUWE1/Rev1_UBM.
DR InterPro; IPR029060; PIN-like_dom_sf.
DR InterPro; IPR006086; XPG-I_dom.
DR InterPro; IPR006084; XPG/Rad2.
DR InterPro; IPR019974; XPG_CS.
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; PF14377; UBM; 2.
DR Pfam; PF00867; XPG_I; 1.
DR PRINTS; PR00853; XPGRADSUPER.
DR SMART; SM00279; HhH2; 1.
DR SMART; SM00484; XPGI; 1.
DR SUPFAM; SSF47807; 5' to 3' exonuclease, C-terminal subdomain; 1.
DR SUPFAM; SSF88723; PIN domain-like; 1.
DR PROSITE; PS00842; XPG_2; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000008827};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 920..989
FT /note="XPG-I"
FT /evidence="ECO:0000259|SMART:SM00484"
FT REGION 14..44
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 361..406
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1047..1067
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1210..1406
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1501..1550
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1565..1590
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 876..910
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 14..34
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 361..398
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1219..1257
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1263..1282
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1283..1299
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1300..1314
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1347..1398
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1590 AA; 177104 MW; 727BFB4929A980A0 CRC64;
MRLKALRLKE LADDLKNQRM KKNSDTKGQK KSNQKDFVGS DLGGSHVKEL DEMSVAKYAA
KEDGNSSQAT ILTTYNQEEL HEMLAASIAA EKNGIHARKG MPSIVINPLE EERDADEQII
LPSVNAEVDM AVLAALPQSM QLDILAQLKG KKTEGLVKEV DNQNQHDVNY RGKGKGILLI
EADMVGCSSR HDNVTSRSDN QHSIDEMLAA SIAMEENEEL VNNTSTSVGA SAIEEEEVDY
DEDEEMILPA MHGKIDPAVL ASLPPSMQLD LLVQMRERLI AENRQKYQKV KKDPAKFSEL
QIQAYLKTVA FRRDIDEVQK AAAVGGVGGV QTSRIASEAN REYIFSSSFT GDKQELTSTS
LEKNKDTQQK VQGVHPSQNL TDSIVAGNDS NTSSGLVHNE PGEPADESIQ TYLDERGRFR
VSRLRAMGMR MTCDIQRNLD LLKEIEQERA YVNKAANIGT VENAENNGPY ESSGIQLVGK
SQEMNVDLVG QNMQNEQTML DRDTLIEISF EYDCKNKFAN DEDDIFSSLV GGNPVAIFGA
DDTAATEQPS HSDSDCDWEE GILEGKSNAY PEHDVVELKS SVADDHKNNE REVEWEEGDC
DGANSTLLSG KLASQGWLEE ESDLQEAIRR SLESIGDMKL KCMPAVDEHS NTYENKLDCG
LEHGDDLYYS DPVDLNDNVG FLNNKNREDS TEKNELHEIE DGDKKHDFVS GNNEQTFHFH
GSQSKSSVTF NSNNTEILID TPCRMDSHSC FVDSISDTNV MTKDLVPMVA EQLLDKHDDG
KVSFYCDNTS KVDPVGATEE GKKNYIQESE PLSNSTDTTK PAILVESSLK GSTEDLDIEP
KLPSEDSNRN FYEERNSSLG NDVVNTPGHF PAHAAEVSLE EEMQILGQEY INLENEQRKL
ERNAESVNSE LFTECQELLQ MFGLPYIIAP MEAEAQCAYL ELEKLVDGVV TDDSDVLLFG
ARSVYKNIFD DRKYVETYFM EDIEKELGLT REKLIRMALL LGSDYTEGVS GIGIVNAIEV
VNAFPEEDGL LKFRQWVESP DPTILGRLDA NSGSNSRKKG SKIEEKMNSS SCNVKESAVM
QNICHAQEQN ELSDYIQEIK QTFFNKHRNV SKNWHIPSSF PSDTVISAYY SPHVDKSTEP
FTWGKPDHLV LRKLCWEKFG WTGQKADELI LPVLKEYNKR ETQLRLEAFY NFNERFAKIR
SKRIKKAVKG ITGKQPSDLI DDSAEEFSKS RKTGREPEDI TLETSRGIEG NLEGRRKSKI
KQSRKNDTVA KEQSKKKKVN DDPSSAPGTS EIENLQPSLQ IEEEQHDGKA LIRNRSGRGR
GRIMGIKRGR DNKGLSFQSC ETEASSGSSD IDDHGPRVHV DRVPKDVRRS MRSRKPVNYS
FKEPEDEDSD DSFDRRNQTG PIEENLSHIL GACEDGATDF SMAKECSAMN FPPEENLPTD
SLESGGWFCT DAGETCHPGT GNQDSSDDYL KMGGGFCLDD GDTGVKQDTS DNVDTATVDY
NADFPHGSDY LDETNRDKSS SDILFSGAEK PENGIQGGGP FNIEPNDLAS ASSYDHSDIA
VLKQENTRNN SGASTGAFSA MPFLKRRRKN
//
