ID F7VAU9_9PROT Unreviewed; 427 AA.
AC F7VAU9;
DT 21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT 21-SEP-2011, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE RecName: Full=Type-4 uracil-DNA glycosylase {ECO:0000256|ARBA:ARBA00019403};
GN ORFNames=ATPR_0498 {ECO:0000313|EMBL:GAA07494.1};
OS Acetobacter tropicalis NBRC 101654.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC Acetobacteraceae; Acetobacter.
OX NCBI_TaxID=749388 {ECO:0000313|EMBL:GAA07494.1, ECO:0000313|Proteomes:UP000004319};
RN [1] {ECO:0000313|EMBL:GAA07494.1, ECO:0000313|Proteomes:UP000004319}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NBRC 101654 {ECO:0000313|EMBL:GAA07494.1,
RC ECO:0000313|Proteomes:UP000004319};
RX PubMed=21554859; DOI=10.1016/j.bbrc.2011.04.126;
RA Matsutani M., Hirakawa H., Nishikura M., Soemphol W., Ali I.A.I.,
RA Yakushi T., Matsushita K.;
RT "Increased number of Arginine-based salt bridges contributes to the
RT thermotolerance of thermotolerant acetic acid bacteria, Acetobacter
RT tropicalis SKU1100.";
RL Biochem. Biophys. Res. Commun. 409:120-124(2011).
CC -!- SIMILARITY: Belongs to the uracil-DNA glycosylase (UDG) superfamily.
CC Type 4 (UDGa) family. {ECO:0000256|ARBA:ARBA00006521}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:GAA07494.1}.
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DR EMBL; BABS01000009; GAA07494.1; -; Genomic_DNA.
DR RefSeq; WP_006557509.1; NZ_BABS01000009.1.
DR AlphaFoldDB; F7VAU9; -.
DR Proteomes; UP000004319; Unassembled WGS sequence.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004844; F:uracil DNA N-glycosylase activity; IEA:UniProtKB-EC.
DR GO; GO:0006281; P:DNA repair; IEA:UniProt.
DR CDD; cd10030; UDG-F4_TTUDGA_SPO1dp_like; 1.
DR Gene3D; 3.40.470.10; Uracil-DNA glycosylase-like domain; 1.
DR InterPro; IPR005273; Ura-DNA_glyco_family4.
DR InterPro; IPR005122; Uracil-DNA_glycosylase-like.
DR InterPro; IPR036895; Uracil-DNA_glycosylase-like_sf.
DR NCBIfam; TIGR00758; UDG_fam4; 1.
DR NCBIfam; TIGR03914; UDG_fam_dom; 1.
DR PANTHER; PTHR33693; TYPE-5 URACIL-DNA GLYCOSYLASE; 1.
DR PANTHER; PTHR33693:SF3; TYPE-5 URACIL-DNA GLYCOSYLASE; 1.
DR Pfam; PF03167; UDG; 1.
DR SMART; SM00986; UDG; 1.
DR SMART; SM00987; UreE_C; 1.
DR SUPFAM; SSF52141; Uracil-DNA glycosylase-like; 1.
PE 3: Inferred from homology;
KW 4Fe-4S {ECO:0000256|ARBA:ARBA00022485};
KW Iron {ECO:0000256|ARBA:ARBA00023004};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723}.
FT DOMAIN 252..412
FT /note="Uracil-DNA glycosylase-like"
FT /evidence="ECO:0000259|SMART:SM00986"
SQ SEQUENCE 427 AA; 48677 MW; 7FEEFC4D538D9DFC CRC64;
MTEILLAHQV DLPTWRRAAR HHVFAGTPPE ELTWRVQPSA LLSQSRPDVQ AAFSVSEEEK
QEPLRLSRRL VEQLVLAIQA HDPERFTLLY RLVFRVMHEG LDLRTHANDP DVRRLEALAE
AVVAETHRFR ADFAAYFRHG GRGEWVSHLS NYIVEANASY CLARVAEPWS VQTGYRRMQW
DGRALSFGPG SEERLPLLWQ RDGEGVWLGY PKTVLPPAEE DIAQATTLDQ LGSEAMDCRA
CALWQPATRT VFGEGPITAR VMLVGEQPGD QEDLAGHPFV GPAGQVLDRA LQEAGIERPD
VYVTNAVKHF RFLWRGTRRL HQKPEQSSVD ACRLWLNAER RLIQPVLVVM MGVTAAQSLL
KRPVTISRER SRIFPLEGGS HGLVTVHPSY LLRLPNEADK QREYQRFLED LQQVKRFMEE
GRQQPVF
//
