ID A0A3G2PX38_9VIBR Unreviewed; 260 AA. AC A0A3G2PX38; DT 13-FEB-2019, integrated into UniProtKB/TrEMBL. DT 13-FEB-2019, sequence version 1. DT 29-SEP-2021, entry version 10. DE RecName: Full=Flap endonuclease Xni {ECO:0000256|HAMAP-Rule:MF_01192}; DE Short=FEN {ECO:0000256|HAMAP-Rule:MF_01192}; DE EC=3.1.-.- {ECO:0000256|HAMAP-Rule:MF_01192}; GN Name=xni {ECO:0000256|HAMAP-Rule:MF_01192, GN ECO:0000313|EMBL:QGH48059.1}; GN Synonyms=ygdG {ECO:0000256|HAMAP-Rule:MF_01192}; GN ORFNames=APZ19_13590 {ECO:0000313|EMBL:QGH48059.1}; OS Vibrio owensii. OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae; OC Vibrio. OX NCBI_TaxID=696485 {ECO:0000313|EMBL:QGH48059.1, ECO:0000313|Proteomes:UP000390336}; RN [1] {ECO:0000313|EMBL:QGH48059.1, ECO:0000313|Proteomes:UP000390336} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=SH14 {ECO:0000313|EMBL:QGH48059.1, RC ECO:0000313|Proteomes:UP000390336}; RX PubMed=26634753; RA Liu L., Xiao J., Xia X., Pan Y., Yan S., Wang Y.; RT "Draft Genome Sequence of Vibrio owensii Strain SH-14, Which Causes Shrimp RT Acute Hepatopancreatic Necrosis Disease."; RL Genome Announc. 3:e01395-15(2015). CC -!- FUNCTION: Has flap endonuclease activity. During DNA replication, flap CC endonucleases cleave the 5'-overhanging flap structure that is CC generated by displacement synthesis when DNA polymerase encounters the CC 5'-end of a downstream Okazaki fragment. {ECO:0000256|HAMAP- CC Rule:MF_01192}. CC -!- COFACTOR: CC Name=K(+); Xref=ChEBI:CHEBI:29103; CC Evidence={ECO:0000256|HAMAP-Rule:MF_01192}; CC Note=Binds 1 K(+) per subunit. The potassium ion strongly increases the CC affinity for DNA. {ECO:0000256|HAMAP-Rule:MF_01192}; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000256|HAMAP-Rule:MF_01192}; CC Note=Binds 2 Mg(2+) per subunit. Only one magnesium ion has a direct CC interaction with the protein, the other interactions are indirect. CC {ECO:0000256|HAMAP-Rule:MF_01192}; CC -!- SIMILARITY: Belongs to the Xni family. {ECO:0000256|HAMAP- CC Rule:MF_01192}. CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_01192}. 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; CP045859; QGH48059.1; -; Genomic_DNA. DR RefSeq; WP_054824363.1; NZ_CP045859.1. DR EnsemblBacteria; AYO15440; AYO15440; D0812_13935. DR Proteomes; UP000390336; Chromosome 1. DR GO; GO:0017108; F:5'-flap endonuclease activity; IEA:UniProtKB-UniRule. DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-UniRule. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule. DR GO; GO:0030955; F:potassium ion binding; IEA:UniProtKB-UniRule. DR GO; GO:0033567; P:DNA replication, Okazaki fragment processing; IEA:UniProtKB-UniRule. DR CDD; cd09898; H3TH_53EXO; 1. DR HAMAP; MF_01192; Xni; 1. DR InterPro; IPR020046; 5-3_exonucl_a-hlix_arch_N. DR InterPro; IPR002421; 5-3_exonuclease. DR InterPro; IPR036279; 5-3_exonuclease_C_sf. DR InterPro; IPR020045; DNA_polI_H3TH. DR InterPro; IPR038969; FEN. DR InterPro; IPR008918; HhH2. DR InterPro; IPR029060; PIN-like_dom_sf. DR InterPro; IPR022895; Xni. DR PANTHER; PTHR42646; PTHR42646; 1. DR Pfam; PF01367; 5_3_exonuc; 1. DR Pfam; PF02739; 5_3_exonuc_N; 1. DR SMART; SM00475; 53EXOc; 1. DR SMART; SM00279; HhH2; 1. DR SUPFAM; SSF47807; SSF47807; 1. DR SUPFAM; SSF88723; SSF88723; 1. PE 3: Inferred from homology; KW DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000256|HAMAP- KW Rule:MF_01192}; KW Endonuclease {ECO:0000256|ARBA:ARBA00022759, ECO:0000256|HAMAP- KW Rule:MF_01192}; Hydrolase {ECO:0000256|HAMAP-Rule:MF_01192}; KW Magnesium {ECO:0000256|HAMAP-Rule:MF_01192}; KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_01192}; KW Nuclease {ECO:0000256|HAMAP-Rule:MF_01192}; KW Potassium {ECO:0000256|ARBA:ARBA00022958, ECO:0000256|HAMAP-Rule:MF_01192}. FT DOMAIN 3..254 FT /note="53EXOc" FT /evidence="ECO:0000259|SMART:SM00475" FT REGION 189..194 FT /note="Interaction with DNA" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01192" FT METAL 109 FT /note="Magnesium" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01192" FT METAL 176 FT /note="Potassium; via carbonyl oxygen" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01192" FT METAL 185 FT /note="Potassium; via carbonyl oxygen" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01192" FT METAL 187 FT /note="Potassium; via carbonyl oxygen" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01192" FT METAL 190 FT /note="Potassium; via carbonyl oxygen" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01192" SQ SEQUENCE 260 AA; 29317 MW; 732C39EAE95ACCAE CRC64; MSIHLVIIDA LNLIRRVHSA QPDPTDIART ITTTCRTLTR ILSEAQPTHI IAVFDHHEQD RGWRAEILPD YKQNRKPMPE PLMQGLDAIQ QAWWEQGIDS LLSEGDEADD LVATLATKVA SHGEKVTIVS TDKGYCQLLS PTLQIRDYFQ HRWLDEPFIE KEFGVKPSQL ADYWGLTGIS SSQVPGIPGV GPKAAKEILT QFEDIEAAYA SEELVPKYRK KFDEHIESAR LCKKVAALKC DIELGFNLQD IRFTGPNKTQ //