ID A0A026VZR7_OOCBI Unreviewed; 1009 AA.
AC A0A026VZR7;
DT 09-JUL-2014, integrated into UniProtKB/TrEMBL.
DT 09-JUL-2014, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE SubName: Full=G/T mismatch-specific thymine DNA glycosylase {ECO:0000313|EMBL:EZA48374.1};
GN ORFNames=X777_13681 {ECO:0000313|EMBL:EZA48374.1};
OS Ooceraea biroi (Clonal raider ant) (Cerapachys biroi).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Formicoidea;
OC Formicidae; Dorylinae; Ooceraea.
OX NCBI_TaxID=2015173 {ECO:0000313|EMBL:EZA48374.1, ECO:0000313|Proteomes:UP000053097};
RN [1] {ECO:0000313|EMBL:EZA48374.1, ECO:0000313|Proteomes:UP000053097}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=24508170; DOI=10.1016/j.cub.2014.01.018;
RA Oxley P.R., Ji L., Fetter-Pruneda I., McKenzie S.K., Li C., Hu H.,
RA Zhang G., Kronauer D.J.;
RT "The genome of the clonal raider ant Cerapachys biroi.";
RL Curr. Biol. 24:451-458(2014).
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; KK107638; EZA48374.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A026VZR7; -.
DR STRING; 2015173.A0A026VZR7; -.
DR OMA; RPKKIHQ; -.
DR Proteomes; UP000053097; Unassembled WGS sequence.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0000700; F:mismatch base pair DNA N-glycosylase activity; IEA:InterPro.
DR GO; GO:0006285; P:base-excision repair, AP site formation; IEA:InterPro.
DR CDD; cd10028; UDG-F2_TDG_MUG; 1.
DR Gene3D; 3.40.470.10; Uracil-DNA glycosylase-like domain; 1.
DR InterPro; IPR017956; AT_hook_DNA-bd_motif.
DR InterPro; IPR015637; MUG/TDG.
DR InterPro; IPR005122; Uracil-DNA_glycosylase-like.
DR InterPro; IPR036895; Uracil-DNA_glycosylase-like_sf.
DR PANTHER; PTHR12159; G/T AND G/U MISMATCH-SPECIFIC DNA GLYCOSYLASE; 1.
DR PANTHER; PTHR12159:SF9; G_T MISMATCH-SPECIFIC THYMINE DNA GLYCOSYLASE; 1.
DR Pfam; PF03167; UDG; 1.
DR SMART; SM00384; AT_hook; 3.
DR SMART; SM00986; UDG; 1.
DR SMART; SM00987; UreE_C; 1.
DR SUPFAM; SSF52141; Uracil-DNA glycosylase-like; 1.
PE 4: Predicted;
KW DNA damage {ECO:0000256|ARBA:ARBA00022763};
KW DNA repair {ECO:0000256|ARBA:ARBA00023204};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Reference proteome {ECO:0000313|Proteomes:UP000053097}.
FT DOMAIN 213..371
FT /note="Uracil-DNA glycosylase-like"
FT /evidence="ECO:0000259|SMART:SM00986"
FT REGION 1..68
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 90..140
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 154..201
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 400..510
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 605..726
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 807..863
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 981..1009
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..15
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 19..37
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 47..68
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 169..201
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 400..423
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 449..472
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 482..500
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 624..639
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 681..695
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 829..863
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1009 AA; 109945 MW; 8C82E12CBFE96145 CRC64;
MVKQEARDDG YETSPDLEMR STGGDSSQQY HTPLTPHTPH TPHTPHTPLT PISATAHQPQ
QPGSTASALG QVAIKCETPV DPYSFVEEEM SMSGMRTASS PGGGGGGGNP ENMTCPGGAQ
PGLGTPTSTP PGALPGPQHH QMNLVMNGAA SVNPQLAHQP KKRGRKKKSE MILTPEEAEL
AEAKKRAKTY KERKKHDRFD GMPEEEVSKR VLPDHLTNNL DIIIIGINPG LFAAYKGHHY
AGPGNHFWKC LHLSGLTPEP LTADDDYKLL RLGIGFTNMV ARATKGSADL TRKEIKEGSH
VLLEKLRKYK PKIAVFNGKL IYEVFSGKKE FGFGRQPSLV DGTNTYMWVM PSSSARCAQL
PRAADKVPYY AALKKFRDYL NGTISHLDES DIVFADSKLK KKEHEPIEDK KPVFTDDLPD
GENRITEING VKQESGLIPG KKKRGRPKKI KNPEDQPVPD PEKLDANGEV IKKRRGRPKK
IHQQQKQLER ENREREQQQQ QQHQHQMGHL NDGYGNAVTN CFSSPLMSPP KPFPHMAPYP
QPMNDAGFYG QGMNDNSPYN MSAKQSPVHL QSQHYTVPSH SPKSISLSFT HSDLSSEINT
AISSENNLEP SPLTSPSVEH PDFEPPTSMS QQNLGNDHRQ YNPAGGPDPA GHHGSPGTPS
HNSYVGGYMG YHEQAPDAHN PHPHQATSTP LSQSAEDHSH HSHPTPPHPH TPTHTAMSPH
HPHEQYGIKR NSQDVASKSL SDLESLVDQI PSIADGGSQR LQHAHPGILA EKMDAHHQSY
MSGFGGMPAG PTGMTNYSPP LPPGGGIYPG ALHHSPSDTG YGSLYVMNGR HHQDSQQQQQ
QQQQQQHQQQ QQQQQQQQHS KSYTVENLAS SNYTPSMNHG HPGNSYPNII PGPHYPVPMG
STNGYLFGGL ESSLMQRTYG ISGMSGMGGM HPSAALGHPM AANPYPYNGS YSSSFDAYPA
PPAGIHAPSA NYPGYVGTAG AAPSTTTSPP SYLAPSHHRP PVDLSYDGV
//