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Database: UniProt
Entry: A0A0D2PX24_GOSRA
LinkDB: A0A0D2PX24_GOSRA
Original site: A0A0D2PX24_GOSRA 
ID   A0A0D2PX24_GOSRA        Unreviewed;      1700 AA.
AC   A0A0D2PX24;
DT   29-APR-2015, integrated into UniProtKB/TrEMBL.
DT   29-APR-2015, sequence version 1.
DT   27-MAR-2024, entry version 34.
DE   RecName: Full=DNA repair protein UVH3 {ECO:0008006|Google:ProtNLM};
GN   ORFNames=B456_001G260400 {ECO:0000313|EMBL:KJB11469.1};
OS   Gossypium raimondii (New World cotton).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Malvales; Malvaceae; Malvoideae; Gossypium.
OX   NCBI_TaxID=29730 {ECO:0000313|EMBL:KJB11469.1, ECO:0000313|Proteomes:UP000032304};
RN   [1] {ECO:0000313|EMBL:KJB11469.1, ECO:0000313|Proteomes:UP000032304}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=23257886; DOI=10.1038/nature11798;
RA   Paterson A.H., Wendel J.F., Gundlach H., Guo H., Jenkins J., Jin D.,
RA   Llewellyn D., Showmaker K.C., Shu S., Udall J., Yoo M.J., Byers R.,
RA   Chen W., Doron-Faigenboim A., Duke M.V., Gong L., Grimwood J., Grover C.,
RA   Grupp K., Hu G., Lee T.H., Li J., Lin L., Liu T., Marler B.S., Page J.T.,
RA   Roberts A.W., Romanel E., Sanders W.S., Szadkowski E., Tan X., Tang H.,
RA   Xu C., Wang J., Wang Z., Zhang D., Zhang L., Ashrafi H., Bedon F.,
RA   Bowers J.E., Brubaker C.L., Chee P.W., Das S., Gingle A.R., Haigler C.H.,
RA   Harker D., Hoffmann L.V., Hovav R., Jones D.C., Lemke C., Mansoor S.,
RA   ur Rahman M., Rainville L.N., Rambani A., Reddy U.K., Rong J.K.,
RA   Saranga Y., Scheffler B.E., Scheffler J.A., Stelly D.M., Triplett B.A.,
RA   Van Deynze A., Vaslin M.F., Waghmare V.N., Walford S.A., Wright R.J.,
RA   Zaki E.A., Zhang T., Dennis E.S., Mayer K.F., Peterson D.G., Rokhsar D.S.,
RA   Wang X., Schmutz J.;
RT   "Repeated polyploidization of Gossypium genomes and the evolution of
RT   spinnable cotton fibres.";
RL   Nature 492:423-427(2012).
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; CM001740; KJB11469.1; -; Genomic_DNA.
DR   STRING; 29730.A0A0D2PX24; -.
DR   EnsemblPlants; KJB11469; KJB11469; B456_001G260400.
DR   Gramene; KJB11469; KJB11469; B456_001G260400.
DR   eggNOG; KOG2520; Eukaryota.
DR   OMA; PNSMDFS; -.
DR   Proteomes; UP000032304; Chromosome 1.
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:0016740; F:transferase activity; IEA:UniProtKB-KW.
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; 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; 2.
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   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   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.
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:UP000032304};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          1..98
FT                   /note="XPG N-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00485"
FT   DOMAIN          1003..1072
FT                   /note="XPG-I"
FT                   /evidence="ECO:0000259|SMART:SM00484"
FT   REGION          129..151
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          405..433
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          439..458
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          581..798
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1130..1182
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1308..1491
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1624..1700
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        129..145
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        406..423
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        595..613
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        666..680
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        687..701
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        704..718
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        752..784
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1150..1182
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1327..1352
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1359..1373
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1416..1433
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1439..1453
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1460..1491
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1674..1688
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1700 AA;  189037 MW;  1E80A3F6ACC5336C CRC64;
     MGVHGLWELL APVGRRVSVE TLAGKKLAID ASIWMVQFMK AMRDEKGEMI RNAHLLGFFR
     RICKLLYLKT KPVFVFDGAT PILKRRTVIA RRRQRENAQA KIRKTAEKLL LNQLKQMRLK
     ELAKDLDNQR KMQKNNNKDK GKMVSSDNQS DTNFVGCNAN VELTKEGDVK LKEKLEVPSI
     AKDGGHNEDE DEDEDEVIIL PDIDGNIDPD VLAALPQSMQ RQLLKQILLN DLNQSNKERS
     GTEHDAMTST SYSQEKLDEM LAASLATQED SNLANASTSV AAIPSEDDGD EDEEMILPAM
     HGNVDPAVLA ALPPSLQLDL LGQMRERLMA ENRQKYQKVK KAPEKFSELQ IQSYLKTVAF
     RREIDEVQRA AAGRGVAGVQ TSRIASEANR EFIFSSSFTG DKQALTSARK EIDEDKQQER
     HSDHPSGFLG SVKSSCKSNV AAESVPDEST SAPDEDVGTY VDATGRIRVS RVRGMGIRMT
     RDLQRNLDLM KEIEKERTNL NKGVNVKSVP DKSKIDASKS VSNGNQFVET SHDDNGESVN
     VNESNQQSAF ETESCMEITF EDDGKTEYFD DDDIFARLAA GEPVTLPSPE EKSLRKQPSG
     SDSDFEWEEG VVEGKWDGVT PGMNAEHNLL NKESNITDDS EVEWEEEPSD APKSSSGPVE
     SGRMLSKGYW EEESDLQEAI RRSLTDVGVE KSNSFPSDVI ESKNLGENLD EDFGSLHEKG
     DTGASSFPGD AVNWQNKSCE NLDRPRKPCT VNEPSISETF NSPESPSPVH NSDKNMTILS
     KFSERSDGSH SEQSRHNETA EFVATLEKEV DFPTGKHLDV SKEVDGLSTI SDSWFKDNSH
     SFDAAHGDIP DTIQVDKKTG SEDEPSNLVS DNKSSIEAEI LDQDKKIDFE AKPSQQSVDT
     VNLSIPTVQS SANKVISDLH IEQELSGDIT YENCVNKAEQ HTDMSTIKGN DNEEIKFSKA
     SLDEELLILD QECINMVDEQ RKLERNAESV SSEMFAECQE LLQMFGLPYI IAPMEAEAQC
     AYMELTNLVD GVVTDDSDVF LFGARSVYKN IFDDRKYVET YFMQDIEKEL GLTREKLMRM
     ALLLGSDYTE GVSGIGIVNA IEVVNAFPEE DGLHKFREWI ESPDPTILGK LNVQEGSSAR
     KRGPKSTEKD VNGTKTSTRG SESNNGTSSL DQNSFQADKN MQSTDCTDDI KQIFMDKHRN
     VSKNWHIPSS FPSEAVISAY SLPQVDKSTE PFTWGRPDLF VLRKLCWEKF GWGSQKSDEL
     LLPVLRESEK RETQLRMEAF YTFNERFAKI RSKRIKKAVK GITGNQSSEL IDDGMQQVSK
     SRRKRRASPV QSGDDKSGEP SNKKEDIASR CQSKSTDKSV PKTSRKRQSS GKDVSFEMRT
     PEPQLQTLRR RETNKQSAGN GRGRGGGEGR RRKGSSGFQQ FETSSSGGDS GNVNQEVDGE
     KLDQPREVRR SMHTRNPVNY TVKDLEDEGG LSHKESSGED AMEKEAGEDV KEKIQCEARE
     PSLDNIYGDY LETGGGFCMD ERGTDLPDAN QDVDLETEPT NDYLKMGGGF YMEGDIDQPD
     TSQDVNPFSE TGSANDYLKM GGGFCMEESE TIGNPDAGNY EDPVQATESS NCFAFMDKAD
     DNIDSAEPSV NAEGSLLDKL QNGGKTPDEA NDALNLNHRN AANKDDSKES ASLPEASDVG
     TTFISGLSAM PSLKRKRRRR
//
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