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UVH3_ARATH
ID   UVH3_ARATH              Reviewed;        1479 AA.
AC   Q9ATY5; Q9LRT2;
DT   21-DEC-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   03-AUG-2022, entry version 139.
DE   RecName: Full=DNA repair protein UVH3;
DE            EC=3.1.-.-;
DE   AltName: Full=ERCC5 homolog;
DE   AltName: Full=RAD2 homolog;
DE            Short=AtRAD2;
DE            Short=AtUVH3;
DE            Short=AtXPG;
DE   AltName: Full=UV hypersensitive protein 3;
DE   AltName: Full=XPG homolog;
GN   Name=UVH3; Synonyms=RAD2, XPG; OrderedLocusNames=At3g28030;
GN   ORFNames=MMG15.7;
OS   Arabidopsis thaliana (Mouse-ear cress).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX   NCBI_TaxID=3702;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND TISSUE SPECIFICITY.
RC   STRAIN=cv. Columbia;
RX   PubMed=11439121; DOI=10.1046/j.1365-313x.2001.01031.x;
RA   Liu Z., Hall J.D., Mount D.W.;
RT   "Arabidopsis UVH3 gene is a homolog of the Saccharomyces cerevisiae RAD2
RT   and human XPG DNA repair genes.";
RL   Plant J. 26:329-338(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=10907853; DOI=10.1093/dnares/7.3.217;
RA   Kaneko T., Katoh T., Sato S., Nakamura Y., Asamizu E., Tabata S.;
RT   "Structural analysis of Arabidopsis thaliana chromosome 3. II. Sequence
RT   features of the 4,251,695 bp regions covered by 90 P1, TAC and BAC
RT   clones.";
RL   DNA Res. 7:217-221(2000).
RN   [3]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Columbia;
RX   PubMed=27862469; DOI=10.1111/tpj.13415;
RA   Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA   Town C.D.;
RT   "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT   genome.";
RL   Plant J. 89:789-804(2017).
CC   -!- FUNCTION: Putative single-stranded DNA endonuclease involved in
CC       nucleotide excision repair (NER) of UV- and oxidative damaged DNA. May
CC       make the 3'-incision step in NER. Seems to play a role in senescence
CC       program. {ECO:0000269|PubMed:11439121}.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC       Note=Binds 2 magnesium ions per subunit. They probably participate in
CC       the reaction catalyzed by the enzyme. May bind an additional third
CC       magnesium ion after substrate binding. {ECO:0000250};
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC   -!- TISSUE SPECIFICITY: Expressed in all tissues at low levels.
CC       {ECO:0000269|PubMed:11439121}.
CC   -!- SIMILARITY: Belongs to the XPG/RAD2 endonuclease family. XPG subfamily.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAB01125.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; AF312711; AAK37472.1; -; mRNA.
DR   EMBL; AB028616; BAB01125.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; CP002686; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   AlphaFoldDB; Q9ATY5; -.
DR   SMR; Q9ATY5; -.
DR   BioGRID; 7757; 2.
DR   IntAct; Q9ATY5; 1.
DR   STRING; 3702.AT3G28030.1; -.
DR   PaxDb; Q9ATY5; -.
DR   PRIDE; Q9ATY5; -.
DR   ProteomicsDB; 243242; -.
DR   Araport; AT3G28030; -.
DR   TAIR; locus:2091343; AT3G28030.
DR   eggNOG; KOG2520; Eukaryota.
DR   HOGENOM; CLU_003018_1_0_1; -.
DR   InParanoid; Q9ATY5; -.
DR   PhylomeDB; Q9ATY5; -.
DR   PRO; PR:Q9ATY5; -.
DR   Proteomes; UP000006548; Chromosome 3.
DR   ExpressionAtlas; Q9ATY5; baseline and differential.
DR   Genevisible; Q9ATY5; AT.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0017108; F:5'-flap endonuclease activity; IBA:GO_Central.
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:0010213; P:non-photoreactive DNA repair; IMP:TAIR.
DR   GO; GO:0006289; P:nucleotide-excision repair; IEA:InterPro.
DR   GO; GO:0009408; P:response to heat; IMP:TAIR.
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; IPR001044; XPG/Rad2_eukaryotes.
DR   InterPro; IPR019974; XPG_CS.
DR   InterPro; IPR006085; XPG_DNA_repair_N.
DR   Pfam; PF14377; UBM; 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; SSF47807; 1.
DR   SUPFAM; SSF88723; SSF88723; 1.
DR   PROSITE; PS00841; XPG_1; 1.
DR   PROSITE; PS00842; XPG_2; 1.
PE   2: Evidence at transcript level;
KW   DNA damage; DNA repair; Endonuclease; Hydrolase; Magnesium; Metal-binding;
KW   Nuclease; Nucleus; Reference proteome.
FT   CHAIN           1..1479
FT                   /note="DNA repair protein UVH3"
FT                   /id="PRO_0000154034"
FT   REGION          1..98
FT                   /note="N-domain"
FT   REGION          128..150
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          239..266
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          384..425
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          548..579
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          854..877
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          934..1022
FT                   /note="I-domain"
FT   REGION          1206..1372
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1418..1479
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        393..410
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1219..1259
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1260..1279
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1325..1359
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1423..1453
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         30
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         77
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         946
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         948
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         967
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         969
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         1018
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   1479 AA;  165668 MW;  72F38D472849EE55 CRC64;
     MGVQGLWELL APVGRRVSVE TLANKRLAID ASIWMVQFIK AMRDEKGDMV QNAHLIGFFR
     RICKLLFLRT KPIFVFDGAT PALKRRTVIA RRRQRENAQT KIRKTAEKLL LNRLKDIRLK
     EQAKDIKNQR LKQDDSDRVK KRVSSDSVED NLRVPVEEDD VGASFFQEEK LDEVSQASLV
     GETGVDDVVK ESVKDDPKGK GVLLDGDDLD NLVQDSSVQG KDYQEKLDEM LAASLAAEEE
     RNFTSKASTS AAAIPSEEDE EEDSDGDEEI LLPVMDGNID PAVLASLPPS MQLDLLAQMR
     EKLMAENRQK YQKVKKAPEK FSELQIEAYL KTVAFRREIN EVQRSAGGRA VGGVQTSRIA
     SEANREFIFS SSFAGDKEVL ASAREGRNDE NQKKTSQQSL PVSVKNASPL KKSDATIELD
     RDEPKNPDEN IEVYIDERGR FRIRNRHMGI QMTRDIQRNL HLMKEKERTA SGSMAKNDET
     FSAWENFPTE DQFLEKSPVE KDVVDLEIQN DDSMLHPPSS IEISFDHDGG GKDLNDEDDM
     FLQLAAGGPV TISSTENDPK EDTSPWASDS DWEEVPVEQN TSVSKLEANL SNQHIPKDIS
     IAEGVAWEEY SCKNANNSVE NDTVTKITKG YLEEEADLQE AIKKSLLELH DKESGDVLEE
     NQSVRVNLVV DKPSEDSLCS RETVGEAEEE RFLDEITILK TSGAISEQSN TSVAGNADGQ
     KGITKQFGTH PSSGSNNVSH AVSNKLSKVK SVISPEKALN VASQNRMLST MAKQHNEEGS
     ESFGGESVKV SAMPIADEEI TGFLDEKDNA DGESSIMMDD KRDYSRRKIQ SLVTESRDPS
     RNVVRSRIGI LHDTDSQNER REENNSNEHT FNIDSSTDFE EKGVPVEFSE ANIEEEIRVL
     DQEFVSLGDE QRKLERNAES VSSEMFAECQ ELLQIFGIPY IIAPMEAEAQ CAFMEQSNLV
     DGIVTDDSDV FLFGARSVYK NIFDDRKYVE TYFMKDIEKE LGLSRDKIIR MAMLLGSDYT
     EGISGIGIVN AIEVVTAFPE EDGLQKFREW VESPDPTILG KTDAKTGSKV KKRGSASVDN
     KGIISGASTD DTEEIKQIFM DQHRKVSKNW HIPLTFPSEA VISAYLNPQV DLSTEKFSWG
     KPDLSVLRKL CWEKFNWNGK KTDELLLPVL KEYEKRETQL RIEAFYSFNE RFAKIRSKRI
     NKAVKGIGGG LSSDVADHTL QEGPRKRNKK KVAPHETEDN NTSDKDSPIA NEKVKNKRKR
     LEKPSSSRGR GRAQKRGRGR GRVQKDLLEL SDGSSDDDDD DDKVVELEAK PANLQKSTRS
     RNPVMYSAKE DDELDESRSN EGSPSENFEE VDEGRIGNDD SVDASINDCP SEDYIQTGGG
     FCADEADEIG DAHLEDKATD DYRVIGGGFC VDEDETAEEN TMDDDAEILK MESEEQRKKG
     KRRNEEDASL DENVDIHFGN SSAGGLSAMP FLKRKKRKN
 
 
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