ID A4HPC8_LEIBR Unreviewed; 1744 AA. AC A4HPC8; DT 01-MAY-2007, integrated into UniProtKB/TrEMBL. DT 01-MAY-2007, sequence version 1. DT 11-DEC-2019, entry version 56. DE RecName: Full=Fanconi-associated nuclease {ECO:0000256|RuleBase:RU365033}; DE EC=3.1.4.1 {ECO:0000256|RuleBase:RU365033}; GN ORFNames=LBRM_35_2830 {ECO:0000313|EMBL:CAM44035.1}; OS Leishmania braziliensis. OC Eukaryota; Euglenozoa; Kinetoplastida; Trypanosomatidae; Leishmaniinae; OC Leishmania; Leishmania braziliensis species complex. OX NCBI_TaxID=5660 {ECO:0000313|Proteomes:UP000007258}; RN [1] {ECO:0000313|EMBL:CAM44035.1, ECO:0000313|Proteomes:UP000007258} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MHOM/BR/75/M2904 {ECO:0000313|EMBL:CAM44035.1, RC ECO:0000313|Proteomes:UP000007258}; RX PubMed=17572675; DOI=10.1038/ng2053; RA Peacock C.S., Seeger K., Harris D., Murphy L., Ruiz J.C., Quail M.A., RA Peters N., Adlem E., Tivey A., Aslett M., Kerhornou A., Ivens A., RA Fraser A., Rajandream M.-A., Carver T., Norbertczak H., Chillingworth T., RA Hance Z., Jagels K., Moule S., Ormond D., Rutter S., Sqaures R., RA Whitehead S., Rabbinowitsch E., Arrowsmith C., White B., Thurston S., RA Bringaud F., Baldauf S.L., Faulconbridge A., Jeffares D., Depledge D.P., RA Oyola S.O., Hilley J.D., Brito L.O., Tosi L.R.O., Barrell B., Cruz A.K., RA Mottram J.C., Smith D.F., Berriman M.; RT "Comparative genomic analysis of three Leishmania species that cause RT diverse human disease."; RL Nat. Genet. 39:839-847(2007). RN [2] {ECO:0000313|EMBL:CAM44035.1, ECO:0000313|Proteomes:UP000007258} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MHOM/BR/75/M2904 {ECO:0000313|EMBL:CAM44035.1, RC ECO:0000313|Proteomes:UP000007258}; RX PubMed=22038252; DOI=10.1101/gr.122945.111; RA Rogers M.B., Hilley J.D., Dickens N.J., Wilkes J., Bates P.A., RA Depledge D.P., Harris D., Her Y., Herzyk P., Imamura H., Otto T.D., RA Sanders M., Seeger K., Dujardin J.C., Berriman M., Smith D.F., RA Hertz-Fowler C., Mottram J.C.; RT "Chromosome and gene copy number variation allow major structural change RT between species and strains of Leishmania."; RL Genome Res. 21:2129-2142(2011). 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 --------------------------------------------------------------------------- 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; FR799010; CAM44035.1; -; Genomic_DNA. DR RefSeq; XP_001568903.1; XM_001568853.1. DR GeneDB; LbrM.35.2830:pep; -. DR GeneID; 5419878; -. DR KEGG; lbz:LBRM_35_2830; -. DR EuPathDB; TriTrypDB:LbrM.35.2830; -. DR eggNOG; ENOG410K45R; Eukaryota. DR eggNOG; ENOG4110DJV; LUCA. DR InParanoid; A4HPC8; -. DR OMA; RWFACLE; -. DR Proteomes; UP000007258; Chromosome 36. DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0004528; F:phosphodiesterase I activity; IEA:UniProtKB-EC. DR GO; GO:0036297; P:interstrand cross-link repair; IEA:InterPro. DR InterPro; IPR033315; Fan1-like. DR InterPro; IPR014883; VRR_NUC. DR PANTHER; PTHR15749; PTHR15749; 1. DR Pfam; PF08774; 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|RuleBase:RU365033}; KW Magnesium {ECO:0000256|RuleBase:RU365033}; KW Manganese {ECO:0000256|RuleBase:RU365033}; KW Metal-binding {ECO:0000256|RuleBase:RU365033}; KW Nuclease {ECO:0000256|RuleBase:RU365033}; KW Nucleus {ECO:0000256|RuleBase:RU365033}; KW Reference proteome {ECO:0000313|Proteomes:UP000007258}. FT DOMAIN 1654..1729 FT /note="VRR-NUC" FT /evidence="ECO:0000259|Pfam:PF08774" FT REGION 1..29 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 63..191 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 792..820 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 1474..1533 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 64..85 FT /note="Polar" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 107..122 FT /note="Polar" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1479..1533 FT /note="Polyampholyte" FT /evidence="ECO:0000256|SAM:MobiDB-lite" SQ SEQUENCE 1744 AA; 188848 MW; F308E27B73477654 CRC64; MSADADATPT DPFLKPRRSP KTSRSSAVND SAMLVEVVDA GQTTSSSSVA AAALFAARLR PSVTVATGAS TSPRDTLTPL ASSAATSRGG AAIMPHTRKR ERPAAESASA GSSTSTTAAP PLAQKRQEAA QRKSEPSPSS SRRTGGAART AMDHGQHSKY RSDEDALGGA TVAGGGDDAE GYGSGEDGDG DAEERALVAT ASSLMAGQGA FATTSAVSAT PHPWLVTDAF HVCLWYVLRY AGSALSAEDL WSCRALVSLT AVDATEKAHA GECGLFKGAI SGTAGAERMT AAFAAERAPG TSMQSDGWDW TGSEESELLL RLLLRKSHSF TARHLELRYG DWLHVQSALN ALTQRRFLWW ATKGTSLDSA ADGVGTVPLH GAEEEAATDL TETPLIPDDE LTTEMAPSQL VKHYDGARVA RLLLNSCDEG RTQCSHAAAI GESVPTFGSM EAVIRVAQAV RVTELRTFLT MLRHRSKARA AMDESAQEGD ECITTSSIIS TSASTLGISE NIVCKDGGAG RDVVAEQASV LRLKSCSRAA DIACARPRQM SDNSLYDVIP GRKRDMIRYL VERRYSVWAP SSTVKGSPEV SATPNTVAVD TTVPSYDAPC TAPHALCSAP LIASPALRGA VRCTSASVGA ASRPLFRRCF RTVAEEADAV AQCWDRVIGS VYVPHSGLKQ HLTWMTELFH VLSSNHGAGM MSEKGAKSVV ATMTVATPPT LLMTRPQLLL LLQTLRAARR QERPSLPESS LSTAAHLNSN VFAESVPYAL LPRWFSSPPV AKATRAVPRP CRQLDRGIPS NGGAGNTMES QPCPDVSVEP NDDESNAMDD IVYTTHWFRA FGAAGDDVAA QTFATPPRVR LFASPAILQE YRRALSIQRK LYYATDGATT AAQRHRGKSR TFVSCMYDTV MAAVRAGVAA VKQHPLHARS ASSASFVSGE MRHFVSMYPP ALPVVSDTAP SVTVSLESLV YQQGCYAEHL LTFTPLYRWF ACLELLFPLL QSGQRYSDAN ACLHHLLYEP IFVLHHLPVS GSRSPISPVT YAFCFKPHKR GKWLARMAQN LSHQKRYAEA LAVLEECQAG YHELASHAMG DARLAPAAAA VGNGVYVASA KWLPCDVMTN STAAALCDVL MGNRSPTSES ALPLKVQRRG RMLRVLWGAA AAASALPAAD NSTTSLPQAE KPSPVSLALL HAAWEYVRDR YCRRQDRLTL ERLLAVVHRK VHQWTSLAAH RDLATRSLVD VAVRHVGGVR DALNRILWRE PSVQARGLTT TSTGGVVRAA KSMTPSEVRN PQHHPALPVE LFVLQHYLNR WNGASSTTAT AAGLATVPQH RRRNDTMVTD PPKGETERSD GIGDVKVASM WCGEHCEGQW IACFAHAFLW DCYWSFPPVF SPLDGFPVNA CDHKSNRPPL QTCPTHGVLW LSAFQDGPLD LATPIQFLWR RRALIEARLA KLERCTREEL VDFVAARIKV AGNTEGARPS KARARERDTE VEAPRAEDDV VQRADEDEGY SGDEERERRR HSRDEGGRSP RRPRYTARVE ERWCVSNDED SVLIASSFSA TPLLFTEFTT PSLLLGQVGQ EASAEMERVG LMRESADASL SSCSSTLAIP EAWKVPVGSL PLLDILRAIP LEPLWRLLRC LYLSPVTEGV PLEFSGFPDL VFWRTGGCGG GNYRYAAIQP SAEESSTVLR ASFCLMEVKS PNDCLSTKQI AVNDLLRRCG FEVFVVHVDE VHDDGRRVST KCIR //