ID A0A1Z5TC02_HORWE Unreviewed; 876 AA.
AC A0A1Z5TC02;
DT 27-SEP-2017, integrated into UniProtKB/TrEMBL.
DT 27-SEP-2017, sequence version 1.
DT 24-JAN-2024, entry version 23.
DE RecName: Full=Fanconi-associated nuclease {ECO:0000256|RuleBase:RU365033};
DE EC=3.1.4.1 {ECO:0000256|RuleBase:RU365033};
GN ORFNames=BTJ68_07368 {ECO:0000313|EMBL:OTA33391.1};
OS Hortaea werneckii EXF-2000.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetidae; Mycosphaerellales; Teratosphaeriaceae; Hortaea.
OX NCBI_TaxID=1157616 {ECO:0000313|EMBL:OTA33391.1, ECO:0000313|Proteomes:UP000194280};
RN [1] {ECO:0000313|EMBL:OTA33391.1, ECO:0000313|Proteomes:UP000194280}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=EXF-2000 {ECO:0000313|EMBL:OTA33391.1,
RC ECO:0000313|Proteomes:UP000194280};
RA Sinha S., Flibotte S., Neira M., Lenassi M., Gostincar C., Stajich J.E.,
RA Nislow C.E.;
RT "The recent genome duplication of the halophilic yeast Hortaea werneckii:
RT insights from long-read sequencing.";
RL Submitted (JAN-2017) 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 -!- 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:OTA33391.1}.
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DR EMBL; MUNK01000076; OTA33391.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Z5TC02; -.
DR STRING; 1157616.A0A1Z5TC02; -.
DR VEuPathDB; FungiDB:BTJ68_07368; -.
DR InParanoid; A0A1Z5TC02; -.
DR OrthoDB; 38749at2759; -.
DR Proteomes; UP000194280; 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: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 CDD; cd22326; FAN1-like; 1.
DR Gene3D; 3.40.1350.10; -; 1.
DR InterPro; IPR033315; Fan1-like.
DR InterPro; IPR049132; FAN1-like_euk.
DR InterPro; IPR049126; FAN1-like_TPR.
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; PF21170; FAN1_TPR; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000194280}.
FT DOMAIN 748..869
FT /note="VRR-NUC"
FT /evidence="ECO:0000259|SMART:SM00990"
FT REGION 32..87
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 212..231
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 288..325
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 609..643
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 35..63
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 288..307
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 622..640
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 876 AA; 99875 MW; E0D16509626D5420 CRC64;
MKLPLIHASL VITNQEHKPR ENAMLGQTKI IAHPKSTNYD EDGEQDFATP PAKRVKREVP
DSDADSDDEL LEHEEQQARR TDLESALPPI QTDREAIEAY EAARAAEQAE LGLKDRLDGQ
KWVRGKSSIY VDAFNLALET VLDQESHLFD EAEHAVFKQW QGLSYEAQYL YVRLFLRKTS
SWHRINRLGY HSDIADMPQA IADIQVVREL PDSSSKAEDY PGELEPPEGT TLQTSFTFAD
RSGECIADLE EASSLLLLDE LKALAKDAKV HGKNKKELLR AFRRTSGKQT GLGWSGLKRS
DTDESTASAG IAEEDGRETP PAKAENRDAH WVGKILAETG PCIRLSLPTL KLFERVHLVF
YRSTEWTEKS LTTIILARIA RWNFPEYIVS RSANIFASRS LLLEFEASLR TQHRIDSMLE
FNGTPTKDDL RLVLDIFEEV YPRWKALLDE EQQKEDSIYA TGEGAYLRRL SPAWVYTRIV
HKGAYILGKF KEHEREHRVL NELLEQRLFH TSRRGDWYQR KALLEEHYMH LHLPSPPDCR
TTEAKKKHWK RMALQTCERG LQDQLTHLIF HHDLQKRTLK LEKQLKIPKR QQHEFSHVLL
TKPAERTFEG VRIEKSPSRN ASRRNSEQNG NGTSTPKPAS DRRGAKTIWL DPALSTVINE
STGEETLIEG ECSVEDMCLS SYRALGYKGY HSEGGIVRTL FAYLFFDVLF IYIPNVFQTE
FQTCPLDLHT DGFYAARMSE VNARLNEISN GEAGRLIQDV WEAHHERKTC VVGLDWSFDI
NDLLEIASAF PAAALSTVMK VMAQEYGQRG GGVPDLFLWK ARDEDAKSGG EVMFAEVKSE
NDRLSDTQRM WIDVLSGAGV RVELCHALAK EVKTQD
//
