ID A0A836GWN8_LEIEN Unreviewed; 1720 AA. AC A0A836GWN8; DT 29-SEP-2021, integrated into UniProtKB/TrEMBL. DT 29-SEP-2021, sequence version 1. DT 22-FEB-2023, entry version 6. DE RecName: Full=Fanconi-associated nuclease {ECO:0000256|RuleBase:RU365033}; DE EC=3.1.4.1 {ECO:0000256|RuleBase:RU365033}; GN ORFNames=CUR178_00275 {ECO:0000313|EMBL:KAG5465568.1}; OS Leishmania enriettii. OC Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina; OC Trypanosomatida; Trypanosomatidae; Leishmaniinae; Leishmania. OX NCBI_TaxID=5663 {ECO:0000313|EMBL:KAG5465568.1, ECO:0000313|Proteomes:UP000674179}; RN [1] {ECO:0000313|EMBL:KAG5465568.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=CUR178 {ECO:0000313|EMBL:KAG5465568.1}; RA Almutairi H., Gatherer D.; RT "Leishmania (Mundinia) enrietti genome sequencing and assembly."; RL Submitted (FEB-2021) 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|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. CC {ECO:0000256|RuleBase:RU365033}. 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:KAG5465568.1}. 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; JAFHKP010000036; KAG5465568.1; -; Genomic_DNA. DR Proteomes; UP000674179; Unassembled WGS sequence. DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0004518; F:nuclease activity; IEA:UniProtKB-KW. DR GO; GO:0036297; P:interstrand cross-link repair; IEA:InterPro. DR InterPro; IPR033315; Fan1-like. DR InterPro; IPR014883; VRR_NUC. DR PANTHER; PTHR15749; FANCONI-ASSOCIATED NUCLEASE 1; 1. DR PANTHER; PTHR15749:SF4; FANCONI-ASSOCIATED NUCLEASE 1; 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|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 1589..1706 FT /note="VRR-NUC" FT /evidence="ECO:0000259|SMART:SM00990" FT REGION 101..200 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 578..632 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 762..804 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 1242..1276 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 1449..1497 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 142..170 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 175..189 FT /note="Acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 578..595 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 602..621 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 783..804 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1257..1276 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1464..1478 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" SQ SEQUENCE 1720 AA; 185213 MW; B085AD70C01E19EE CRC64; MSADADGAPA DPFLNPRRSR GVSHVSVVND GRMVMEDVDA DRTTSSSPAA AALSSICVCP SVAVEMRASS GLQNAAARLG SNAAACGDAA VIVPHARKRE RPAVASAHAG STAWTTAAPP QERRRRANGA AVSCSRHLGG AARTFEGRRQ RGNTERSDED ALKEATGGED GGGDEAGNAS DDDGEEDAEE RALAAAASSL TTGPEAFTAA SAASATPHPW LVTDAFHVCL WFVLRYAGDA LSAEDLWACR AVLSLTAVGA TDEGRGGACA LSKDAFSGAK GAETTTGLAS AEQAQGVCME RDIWAWSGSE ESELLLRLLL RSPHSFTARH LELRYGDWLH VQLALDALTR KRFLWWTTAG TSLNSAAGDA EAVRLRGAEE DVTTDWKKAP LIPVDELTCA EMAPSPFVEH YDGARVARLL LSSCDEVKSQ HRHAATVGES APTLSCAETV IRVAQAVRAT ELRTFLTALR HCSKARAALN ESTPKEECTT SATVSTLCPS PSVFCKSDVA GASAEATPRP VQLPKSGGRA KIVGCARLGQ TSHNGLYDAI PGRKRDMICY LVERRYSVWA PARTVGGARA ASSTTHSTAA GTVVPSYGTP RTAPRDLSSA PSASTCGPRS GVRCPSSVAS AGGRSESRRC FLTVTEEADV VAQCWDRIIG SVYVPHAGLK QNLVRVAELF HVLTSNSGAG LLSERSAKAL AATMTVATPP NLLMVRSQLL LLLQTLRAAR CEARPGPKAF LESVPHALLP RWLSPRLAEK VTTRAVPRAS RPPDRGIPSD GRAGSKTESQ GYHPSVSAES SDGDSTLMDE IVRSARSFQV SDVAEDVAAT QACAITLHVR LFANPATLQE YRRALSTQRE LYYATDGAGT AAQCHRGKSG IFLSRMYETV MAAVRAGVAR VKRHPVYGCS AASASFVSDE MTHFGSIGPP AHPVVSEAPP SPKESTPSAA VSLEALVYQK GCYAEHLLIF TPLYRWFACL EALFPLLQSA RRYADANACL RCLLYEPIFV LHHIPVGGTH CNISPMTYGF RYRAHKRGKW LTRLVQNLSH QKRYAEAFAV LTKAQAGYRE LASYAMKGAR SQSPAASVGA ACRSNDKRLP CDAMANSTAA ALCEVLAGNR SPAIESVLPQ EVQRRGRMLR VFWPATASVS SATSGDNTLL TAAEKPSPGS LALLHAAWEY VRDRYCRRQD RLALEKSLSM MHRKVHRWTP PAPNLDLETC CLSDVAVRRV RGVRDELDRM LWREPTGQAR KRSGAASGAT AKSTTSSGAR SSQRSPALPV EQFVLQHYLS RWNGASTTAA AASPAADPQH RRPTETFAID YTEPETERSD NVDGATMTSV WCGAHCEGHW IACLARAFLW DCYWAFPSAS PPLDTFSGSA HAQESNRPTG EVLWLSPFQD GPLDLTTPIQ FLWRRRALIE ARLAKLERCT REELVAYVAV HIKMERRKSD EGASLGMAKE RGRGAESGTP RSEEHALQCE EVDEDCDGDE ERACRRRSRG EAGCGSYRHR YSSETDEALR VEREEDSVLL LSPVAETSLS FAKSETSSLL LGQAEQERKA DAEEVKPMTE SADASLSLCA PTISIPEAWK VSVGPLPLLD ILRAIPLKPL WRLLRCLYLS PVTEGVPLEF SGFPDLVFWR AGGGSGGACS NAAVQASVED SAVMLRPSFR LMEVKSPTDS LSTKQIAVND LLHRCGFDVC VVRVDEVHHD GQRVSTKRIR //