ID G1T395_RABIT Unreviewed; 1633 AA.
AC G1T395;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 11-DEC-2019, sequence version 2.
DT 27-MAR-2024, entry version 71.
DE RecName: Full=DNA repair protein complementing XP-G cells {ECO:0008006|Google:ProtNLM};
OS Oryctolagus cuniculus (Rabbit).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX NCBI_TaxID=9986 {ECO:0000313|Ensembl:ENSOCUP00000010688.3, ECO:0000313|Proteomes:UP000001811};
RN [1] {ECO:0000313|Ensembl:ENSOCUP00000010688.3, ECO:0000313|Proteomes:UP000001811}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Thorbecke inbred {ECO:0000313|Ensembl:ENSOCUP00000010688.3,
RC ECO:0000313|Proteomes:UP000001811};
RX PubMed=21993624; DOI=10.1038/nature10530;
RA Lindblad-Toh K., Garber M., Zuk O., Lin M.F., Parker B.J., Washietl S.,
RA Kheradpour P., Ernst J., Jordan G., Mauceli E., Ward L.D., Lowe C.B.,
RA Holloway A.K., Clamp M., Gnerre S., Alfoldi J., Beal K., Chang J.,
RA Clawson H., Cuff J., Di Palma F., Fitzgerald S., Flicek P., Guttman M.,
RA Hubisz M.J., Jaffe D.B., Jungreis I., Kent W.J., Kostka D., Lara M.,
RA Martins A.L., Massingham T., Moltke I., Raney B.J., Rasmussen M.D.,
RA Robinson J., Stark A., Vilella A.J., Wen J., Xie X., Zody M.C., Baldwin J.,
RA Bloom T., Chin C.W., Heiman D., Nicol R., Nusbaum C., Young S.,
RA Wilkinson J., Worley K.C., Kovar C.L., Muzny D.M., Gibbs R.A., Cree A.,
RA Dihn H.H., Fowler G., Jhangiani S., Joshi V., Lee S., Lewis L.R.,
RA Nazareth L.V., Okwuonu G., Santibanez J., Warren W.C., Mardis E.R.,
RA Weinstock G.M., Wilson R.K., Delehaunty K., Dooling D., Fronik C.,
RA Fulton L., Fulton B., Graves T., Minx P., Sodergren E., Birney E.,
RA Margulies E.H., Herrero J., Green E.D., Haussler D., Siepel A., Goldman N.,
RA Pollard K.S., Pedersen J.S., Lander E.S., Kellis M.;
RT "A high-resolution map of human evolutionary constraint using 29 mammals.";
RL Nature 478:476-482(2011).
RN [2] {ECO:0000313|Ensembl:ENSOCUP00000010688.3}
RP IDENTIFICATION.
RC STRAIN=Thorbecke {ECO:0000313|Ensembl:ENSOCUP00000010688.3};
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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; AAGW02021415; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AAGW02021416; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR SMR; G1T395; -.
DR STRING; 9986.ENSOCUP00000010688; -.
DR PaxDb; 9986-ENSOCUP00000010688; -.
DR Ensembl; ENSOCUT00000012416.3; ENSOCUP00000010688.3; ENSOCUG00000012414.3.
DR eggNOG; KOG2520; Eukaryota.
DR GeneTree; ENSGT00510000048601; -.
DR HOGENOM; CLU_003018_2_1_1; -.
DR InParanoid; G1T395; -.
DR TreeFam; TF101235; -.
DR Proteomes; UP000001811; Chromosome 8.
DR Bgee; ENSOCUG00000012414; Expressed in upper lobe of left lung and 15 other cell types or tissues.
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; cd09904; H3TH_XPG; 1.
DR CDD; cd09868; PIN_XPG_RAD2; 2.
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 NCBIfam; TIGR00600; rad2; 1.
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.
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 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:UP000001811}.
FT DOMAIN 457..552
FT /note="XPG N-terminal"
FT /evidence="ECO:0000259|SMART:SM00485"
FT DOMAIN 1227..1296
FT /note="XPG-I"
FT /evidence="ECO:0000259|SMART:SM00484"
FT REGION 1..31
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 154..181
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 439..462
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 756..840
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 859..888
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 915..934
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 940..1021
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1067..1176
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1500..1532
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1545..1633
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 11..28
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 161..175
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 759..773
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 817..831
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 995..1013
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1112..1126
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1134..1176
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1500..1528
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1556..1581
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1615..1633
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1633 AA; 182907 MW; 30B2D8D8D42B76A1 CRC64;
MPNVVETERS NDPGNGEHRS ERKSPEENLQ GAVKSFCTSA SGAPLGPKGD GHYPWSCPVT
HTREKIYAIC SDYAFLNQAT SIYKTPNSTR SSCLPDSTSL SAGNNSSRYI GIPTSTSEII
YNEENSLENL SNSLGKLPLA WEIDKSEFDG VTTNLKHKSG NAKKQISKKK TSDKKGRHQR
ECLPHSPLED VKQRKVLDLR RWYCISRPQY KTSCGISSLI SCWNFLYSTM GAGNLPPITQ
EEALHILGFQ PPFEDIRFGP FTGNTTLMRW FRQINDHFHV KGCSYVLYKP HGKNKTAGET
ASGALSKLMH GLKDESLAYI YHCQNHYFCP IGFEATPVKP SKAFSRGPLS SQEVEYWILI
GESSRKHPAI HCKKWADIVT DLNTQNPEYL DIRHLERGLQ YRKTKKVGGN LHCIIAFQRL
NWQRFGLWSF PFGNLRQESQ PPTHAQGIAK SESEDNISKK QHGRLGRSFS ASFHQDSTWK
KMSNISIWLN QALKGVRDRH GNSIENAHLL TLFHRLCKLL FFRIRPIFVF DGDAPLLKKQ
TLAKRRQRKD LASTDSRKTT EKLLKTFLKR QALKTAFKSK RNEALPSLTQ VQREDDIYVL
PPLKEEEKHS SEEEDEKEWQ ERMSQKQALQ EEFFHNPHAI DIESEDFSSL PPEVKHEILT
DMKEFTKRRR TLFEAMPEES NDFSQYQLKG LLKKNYLNQH IENVQKEMNQ QHSGQIQKQY
EEEGGFLREV ESRRVVSEDT SHYILIKGIQ AKKVAEVDSE SLPSSSKVHS VSLDMKSSPC
EKLKPEKEPD ATPPSPRTLL ALQAAMLGSS SDEELESGSL SQHRERKVSA AGDDGSISPR
TLSAIQRALD EDEDVKMCAG DSVQGAGPGV TKLPVKSSKE EKDEGLEVRD KKGVLSTAVQ
PSASVTFVEE CVASTESERE LPGSAPKEQK SFVPVVNEAF QTSDGSAVKD RRDPLPSENT
VVLPSDAPGL PTLVAPASTG SVSRNGTPAK ELELQKDLSP SERKFDSSIL SSDEETKCEQ
NPVSEVIGAV SSPEVSDLIS VPSEVIGHSK DAESLNAEEN DNFLKILQQQ ETVGSPGPGS
ISFPKSVEPG AIDSDESESD GSFIEVQGGI SEDEVQTESN EASRPPSEQG DMVPMGAKDE
EATGDTESLP RDHSESKDLD IEPHEEHEKD TEDSFNEWQD IDLEELETLE NDLLAQQNSL
KAQKQQQERV AATVTGQMFL ESQELLRLFG IPYVEAPMEA EAQCAILDLT DQTSGTITDD
SDIWLFGARH VYKNFFNKNK FVEYYQYVDF HNQLGLDRNK LINLAYLLGS DYTEGIPTVG
CVTAMEILNE FPGHGLEPLV KFSEWWQEAQ KNQKIRPNPH DTKVKKKLRK LQLAPGFPNP
AVAEAYLKPV VDDSKGAFLW GKPDPDKIRE FCQRYFGWNR SKTDESLLPV LKQLNVQQTQ
LRIDSFFRLA QQEKQEAKRI KSQRLNRAVT CMLRKEREEV ASELEAVSVA MEKEFEMLDK
AEGASQKRST ARKLEEPSSL KRKRLSASAH ESQAGGFLGD AYLSESSDTC SGEDAERLSP
VSTQRKTAKE STCSPSAWQS SARDARARDG GATTCSSSDG DGEEAGTVLV TARPVFGKKR
RRLRSARGRK RKT
//
