ID A0A0S4IFU9_9PSED Unreviewed; 549 AA.
AC A0A0S4IFU9;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 24-JAN-2024, entry version 32.
DE RecName: Full=Fanconi-associated nuclease {ECO:0000256|RuleBase:RU365033};
DE EC=3.1.4.1 {ECO:0000256|RuleBase:RU365033};
GN ORFNames=PYEL_44240 {ECO:0000313|EMBL:CRN08562.1};
OS Pseudomonas sp. URMO17WK12:I11.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=1283291 {ECO:0000313|EMBL:CRN08562.1, ECO:0000313|Proteomes:UP000062067};
RN [1] {ECO:0000313|Proteomes:UP000062067}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Falquet L., Falquet L.;
RL Submitted (JUN-2015) to the EMBL/GenBank/DDBJ databases.
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; LN865164; CRN08562.1; -; Genomic_DNA.
DR RefSeq; WP_059184081.1; NZ_LN865164.1.
DR AlphaFoldDB; A0A0S4IFU9; -.
DR PATRIC; fig|1283291.5.peg.4372; -.
DR Proteomes; UP000062067; Chromosome 1.
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; IPR040603; FAN1_SAP_bact.
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; PF18081; FANC_SAP; 1.
DR Pfam; PF08774; VRR_NUC; 1.
DR SMART; SM00990; VRR_NUC; 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}.
FT DOMAIN 431..545
FT /note="VRR-NUC"
FT /evidence="ECO:0000259|SMART:SM00990"
SQ SEQUENCE 549 AA; 62772 MW; 4AE3C15FEBF15ABE CRC64;
MIAHSVEDPL YYLHNFRQVL CWVGQRYADL LDLSEQAFIA TFAELDAPAQ AIMVRMVMRK
GELFRDDRLQ YAEVGDIGQA LAPLMGLGWV CEPEHLTLEQ LFTLLRKDEL AQCFATQLSR
PRAAKHELLA ELQALELAPR SLRQWFAHSE LRIVQWCRQA VCDRIRLLFF GNLYQDWSDF
VLADLGVLRF EQVAFSADSR ALHQRSEVDL ALALHQCAER LEEGADTASV LATLQGLHSD
NAWLARRRAR LLFALGQQCE RRGEWDQAMA VYAQCAHPQA RIRQVRVLER TQSWEQAHAL
ALQLAAAPAN ALEVQALERM LPRLARKLGG PPQRRQRLKP VELIELELPR AHAELGVEEA
VRQHLAASGG EVHYVENTLF NSLFGLLCWE AVFAPVPGAF FNPFQSAPQD LHDSDFQHRR
SDVFERCLSR LDDGTHRQII RDCYATKRGL QSPFVFWGML NETLLDQALG CLPGAHLKQC
FLRLLQDIRN NRTGMPDLIQ FWPEQGSYRM VEVKGPGDRL QDNQLRWLEF CRLHGLPVAV
CHVRWSEAA
//
