ID E2AKY4_CAMFO Unreviewed; 1193 AA.
AC E2AKY4;
DT 30-NOV-2010, integrated into UniProtKB/TrEMBL.
DT 30-NOV-2010, sequence version 1.
DT 27-MAR-2024, entry version 63.
DE SubName: Full=DNA-repair protein complementing XP-G cells {ECO:0000313|EMBL:EFN65901.1};
GN ORFNames=EAG_09204 {ECO:0000313|EMBL:EFN65901.1};
OS Camponotus floridanus (Florida carpenter ant).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Formicoidea;
OC Formicidae; Formicinae; Camponotus.
OX NCBI_TaxID=104421 {ECO:0000313|Proteomes:UP000000311};
RN [1] {ECO:0000313|EMBL:EFN65901.1, ECO:0000313|Proteomes:UP000000311}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C129 {ECO:0000313|Proteomes:UP000000311};
RX PubMed=20798317; DOI=10.1126/science.1192428;
RA Bonasio R., Zhang G., Ye C., Mutti N.S., Fang X., Qin N., Donahue G.,
RA Yang P., Li Q., Li C., Zhang P., Huang Z., Berger S.L., Reinberg D.,
RA Wang J., Liebig J.;
RT "Genomic comparison of the ants Camponotus floridanus and Harpegnathos
RT saltator.";
RL Science 329:1068-1071(2010).
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; GL440425; EFN65901.1; -; Genomic_DNA.
DR RefSeq; XP_011260023.1; XM_011261721.2.
DR AlphaFoldDB; E2AKY4; -.
DR STRING; 104421.E2AKY4; -.
DR EnsemblMetazoa; XM_011261721.3; XP_011260023.1; LOC105253603.
DR GeneID; 105253603; -.
DR KEGG; cfo:105253603; -.
DR InParanoid; E2AKY4; -.
DR OMA; PNSMDFS; -.
DR OrthoDB; 26655at2759; -.
DR Proteomes; UP000000311; Unassembled WGS sequence.
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 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:UP000000311}.
FT DOMAIN 1..98
FT /note="XPG N-terminal"
FT /evidence="ECO:0000259|SMART:SM00485"
FT DOMAIN 831..900
FT /note="XPG-I"
FT /evidence="ECO:0000259|SMART:SM00484"
FT REGION 582..609
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1079..1133
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1193 AA; 135862 MW; 3579687DE6FCBEB7 CRC64;
MGVHGLWKLL EASGKPVPLE SLEGKVLAID ISIWIYQVLQ GYQDRHGTPK PNAHLLGLFT
RICKLLYYKI KPVFVFDGGV PMLKKNTIAL RRKQKSIATS KAQKMKADLI NNLIKHSVVK
TALNKDSKVD QTNGAIQAML NMPTNCSKED MFILPDMPST SNMQTYISDN EDDSDTSVEL
SPRKQSKWMG NIHNVDVTSN EFKALPADVR YDILTDLKET RKQNSWGRLH EIPQESQEFS
GYQLTRLLKR RYVQESLESA EKEMGGKTLT LEELDKLLTE QGVNTKGNDA AFRIAADSTT
RLIYISDKNA LVKDSNKSET DEDDILQNIN EEVKSIAGPS NHTPIVEDIN EYELNDSDDD
IDMIHDFSFI TSDENKNALD SDRESEIDMN ESLAPLDKKS SKNATNPALA YLLEYSGLSQ
NQIMHLMKYN KDQSRKIKTA DKDVKLHEKN TNSELTEGRN PTIAKSEFSL PENYVGVSKS
IESQNMQNAC TTNENMTVEL ILSNMESDNF TKKELLKNKT EVLDVTSDVI SSDKLVEFEE
HSFSPTKSND NMTTELISSN VKSDNFKEKS LKNNVETSDV TSNVTFPIDN SRRSEERSSP
TKSNDNMNVE LISTVQTDTS DSDSDDFIEI QDVPIPYVEI SQKNITKKEN VEITFKPDEK
LEDDIFADIF EKTDKNKDLP TSLEQICCMQ QSINENDKHR IPLISENKNL KTNLLDTIPE
ELIIEKTKIK LLENTQLIEN ISNDEDKIHD FQDSNDLVQK NNTDLLTEDD TCNEYIQEKR
TVLPTNEEDL IELKGQLECE QEELTKGIGK FERQATNISD QIQTEAQELL RLFGIPYIVA
PMEAEAQCAY LEQIELTNGT ITDDSDIWLF GGQYVYKNFF NNNRRVLQFH AYDIQHHFKL
SRNQLIQLAL LVGSDYTTGV AGIGPVTALE ILAAFPAEGD NILHGLYKFC SWIKEGKPSG
KMGLRNKLRN VKLDRDFPNQ AVAQAYLFPT IDESKETFTW GKPNVVLLCD YTRQKFGWTK
GKFDDTMVPV LKRLEENKNQ KLLDMYFKKK ILPRSIEPTL SKRVQKALCR LNNVDMDEEN
VNDESQSKRS KKSNTVQKLN KEDVVEIATD ETHEESLPKD ATSSKPVKSI DKKKYTKEYI
PQREKDKECA LERKLHAIEV LRKSKQGLGK TKKGKRVIRK VKKEAELSES DSN
//
