ID A0A1H6W8K7_9BACT Unreviewed; 575 AA.
AC A0A1H6W8K7;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 21.
DE RecName: Full=Fanconi-associated nuclease {ECO:0000256|RuleBase:RU365033};
DE EC=3.1.4.1 {ECO:0000256|RuleBase:RU365033};
GN ORFNames=SAMN05216327_10621 {ECO:0000313|EMBL:SEJ09160.1};
OS Dyadobacter sp. SG02.
OC Bacteria; Bacteroidota; Cytophagia; Cytophagales; Spirosomataceae;
OC Dyadobacter.
OX NCBI_TaxID=1855291 {ECO:0000313|EMBL:SEJ09160.1, ECO:0000313|Proteomes:UP000199631};
RN [1] {ECO:0000313|EMBL:SEJ09160.1, ECO:0000313|Proteomes:UP000199631}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SG02 {ECO:0000313|EMBL:SEJ09160.1,
RC ECO:0000313|Proteomes:UP000199631};
RA de Groot N.N.;
RL Submitted (OCT-2016) 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}.
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; FNYL01000006; SEJ09160.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H6W8K7; -.
DR STRING; 1855291.SAMN05216327_10621; -.
DR OrthoDB; 9803913at2; -.
DR Proteomes; UP000199631; Unassembled WGS sequence.
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; 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.
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 455..567
FT /note="VRR-NUC"
FT /evidence="ECO:0000259|SMART:SM00990"
SQ SEQUENCE 575 AA; 67480 MW; 72C0115275DC1E97 CRC64;
MSAELTDPFA QEQVFPTDLP PKYYLEYFNY VLAFVRKRYA HILHGSELEF LDNYESLSED
AQCLFIRFSN RSKSFFRSNS LSYSEIGDMP AVLTELLERD FIETLCEAHE SRFTEVIDLF
TKPELLEFTK LLQPDIMPSK SIKKPDLVRW LLYEYDFAVL CEVIGALEPV VKVSFEAEVM
LMKFLFFGNR YADMTEFVVR DLGHVRFQSF DEQYLSIQFD TRKDADDTLM VSLMKETFDI
IKQDLPPEEI YDWFMNWQAA SGTGLSHKAL PSFNTFILKV SAWLERKKML SQALTIYQLT
SDAPARERRV RLLYNLGEID EALALCEEIA ESPQNADERF FSLDFYEKIK NKKARTVKRT
TQALKAAEAI EVPVSFRFRV EFGAITYYQE QGYNAFFSEN EPWRALFGLL FWDIIYDTNV
QTIHNPLQRI PSDFFLPDFY FKRSEQLKER LAAAHSREII DELVTQTFTD KYGITNVLVP
WYDGALDKVL TLTSLLSPEK IHKIMLEMAL NLRENTRGFP DLLVWNDDDY AFIEIKSPTD
HLSSRQLHWQ HFFAEHGVQS RIVRVNWIKE NINLM
//
