ID U4KH62_9VIBR Unreviewed; 540 AA.
AC U4KH62;
DT 11-DEC-2013, integrated into UniProtKB/TrEMBL.
DT 11-DEC-2013, sequence version 1.
DT 24-JAN-2024, entry version 41.
DE RecName: Full=Fanconi-associated nuclease {ECO:0000256|RuleBase:RU365033};
DE EC=3.1.4.1 {ECO:0000256|RuleBase:RU365033};
GN ORFNames=VIBNI_B1242 {ECO:0000313|EMBL:CCO61004.1};
OS Vibrio nigripulchritudo.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=28173 {ECO:0000313|EMBL:CCO61004.1, ECO:0000313|Proteomes:UP000016895};
RN [1] {ECO:0000313|EMBL:CCO61004.1, ECO:0000313|Proteomes:UP000016895}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SnF1 {ECO:0000313|Proteomes:UP000016895};
RX PubMed=23739050; DOI=10.1038/ismej.2013.90;
RA Goudenege D., Labreuche Y., Krin E., Ansquer D., Mangenot S., Calteau A.,
RA Medigue C., Mazel D., Polz M.F., Le Roux F.;
RT "Comparative genomics of pathogenic lineages of Vibrio nigripulchritudo
RT identifies virulence-associated traits.";
RL ISME J. 7:1985-1996(2013).
CC -!- FUNCTION: Nuclease required for the repair of DNA interstrand cross-
CC links (ICL). Acts as a 5'-3' exonuclease that anchors at a cut end of
CC DNA and cleaves DNA successively at every third nucleotide, allowing to
CC excise an ICL from one strand through flanking incisions.
CC {ECO:0000256|RuleBase:RU365033}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Hydrolytically removes 5'-nucleotides successively from the
CC 3'-hydroxy termini of 3'-hydroxy-terminated oligonucleotides.;
CC EC=3.1.4.1; Evidence={ECO:0000256|ARBA:ARBA00000983,
CC ECO:0000256|RuleBase:RU365033};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|RuleBase:RU365033};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000256|RuleBase:RU365033};
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|RuleBase:RU365033}.
CC -!- SIMILARITY: Belongs to the FAN1 family. {ECO:0000256|ARBA:ARBA00005533,
CC ECO:0000256|RuleBase:RU365033}.
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DR EMBL; FO203527; CCO61004.1; -; Genomic_DNA.
DR RefSeq; WP_022561513.1; NC_022543.1.
DR AlphaFoldDB; U4KH62; -.
DR STRING; 28173.VIBNI_B1242; -.
DR KEGG; vni:VIBNI_B1242; -.
DR PATRIC; fig|1260221.3.peg.4849; -.
DR eggNOG; COG2176; Bacteria.
DR OrthoDB; 9803913at2; -.
DR Proteomes; UP000016895; Chromosome 2.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0004528; F:phosphodiesterase I activity; IEA:UniProtKB-EC.
DR GO; GO:0036297; P:interstrand cross-link repair; IEA:InterPro.
DR Gene3D; 3.40.1350.10; -; 1.
DR InterPro; IPR033315; Fan1-like.
DR InterPro; IPR049125; FAN1-like_WH.
DR InterPro; IPR011335; Restrct_endonuc-II-like.
DR InterPro; IPR011856; tRNA_endonuc-like_dom_sf.
DR InterPro; IPR014883; VRR_NUC.
DR PANTHER; PTHR15749; FANCONI-ASSOCIATED NUCLEASE 1; 1.
DR PANTHER; PTHR15749:SF4; FANCONI-ASSOCIATED NUCLEASE 1; 1.
DR Pfam; PF21315; FAN1_HTH; 1.
DR Pfam; PF08774; VRR_NUC; 1.
DR SMART; SM00990; VRR_NUC; 1.
DR SUPFAM; SSF52980; Restriction endonuclease-like; 1.
PE 3: Inferred from homology;
KW DNA damage {ECO:0000256|RuleBase:RU365033};
KW DNA repair {ECO:0000256|RuleBase:RU365033};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU365033};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|RuleBase:RU365033};
KW Manganese {ECO:0000256|ARBA:ARBA00023211, ECO:0000256|RuleBase:RU365033};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|RuleBase:RU365033};
KW Nuclease {ECO:0000256|ARBA:ARBA00022722, ECO:0000256|RuleBase:RU365033};
KW Nucleus {ECO:0000256|RuleBase:RU365033};
KW Reference proteome {ECO:0000313|Proteomes:UP000016895}.
FT DOMAIN 426..536
FT /note="VRR-NUC"
FT /evidence="ECO:0000259|SMART:SM00990"
SQ SEQUENCE 540 AA; 63375 MW; 3E1E49F28970443F CRC64;
MPSQPPELPV DYYHTNFQLL LNNAIQTYDD LLADKEKRWI ESYNKLDKAS QCLLIRLLSR
KGEWFRSDKL VYQEIGDITA CLAQLSEHKL IFLPDKLNCR QLAHSLLTKP EIATLYPNLN
KQLPKSDLIS LLPDEEIDIA NLPFTCIQLL HAELMPIFTA LFFTNTHQDF TQFVLSDLGL
NRFESYSLSR KLRYFNHRDE LLSLLEIGDI GNQYYEYRKA PLEHIQHWLN VLPAKSGHQD
VDKKRSHLIN KLARDLERYE RFDEAISHFS ENALPPSRER RVRMWEKMGL DEQALTLTQD
MLGSPYDVDE WEVAQRIERK LVKKLGDKPS PATKPKFEEV YIELDLSEQR VEVATQIHYN
QSGWETYYLE NCFLNGLFGL VFWDSIYAPV QGAFNHAYQY RPLDLYRPEF SENRSELIGT
DIQRFLTLGY EPLIERYNEK YGIANPYVIW DVFTPEHITQ ASIALPEEQL VELFRVMLSD
MRNFRAGQPD LVAFKNGELK FIEVKGPGDK LQQNQIRWLQ KFQQLGVNAE VCYVNYSKKK
//