ID A0A194VAA0_9PEZI Unreviewed; 851 AA.
AC A0A194VAA0;
DT 05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2016, sequence version 1.
DT 24-JAN-2024, entry version 20.
DE RecName: Full=Fanconi-associated nuclease {ECO:0000256|RuleBase:RU365033};
DE EC=3.1.4.1 {ECO:0000256|RuleBase:RU365033};
GN ORFNames=VP1G_08076 {ECO:0000313|EMBL:KUI60895.1};
OS Valsa mali var. pyri (nom. inval.).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Diaporthales; Valsaceae; Valsa.
OX NCBI_TaxID=694573 {ECO:0000313|EMBL:KUI60895.1, ECO:0000313|Proteomes:UP000078576};
RN [1] {ECO:0000313|Proteomes:UP000078576}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SXYL134 {ECO:0000313|Proteomes:UP000078576};
RA Yin Z., Liu H., Gao X., Li Z., Song N., Ke X., Dai Q., Wu Y., Sun Y.,
RA Xu J.-R., Kang Z.K., Wang L., Huang L.;
RT "Genome Sequence of Valsa Canker Pathogens Uncovers a Specific Adaption of
RT Colonization on Woody Bark.";
RL Submitted (DEC-2014) 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}.
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DR EMBL; KN714761; KUI60895.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A194VAA0; -.
DR STRING; 694573.A0A194VAA0; -.
DR OrthoDB; 38749at2759; -.
DR Proteomes; UP000078576; 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: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 InterPro; IPR033315; Fan1-like.
DR InterPro; IPR049132; FAN1-like_euk.
DR InterPro; IPR049126; FAN1-like_TPR.
DR InterPro; IPR049125; FAN1-like_WH.
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|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:UP000078576}.
FT DOMAIN 722..844
FT /note="VRR-NUC"
FT /evidence="ECO:0000259|SMART:SM00990"
FT REGION 1..109
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 321..354
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 18..44
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 61..83
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 321..344
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 851 AA; 97282 MW; 06A0B00C5C87AED6 CRC64;
MDAFVRRTAS SSKPREPLAD ISNKHEMGTA RPSKRRRVDG SGDEDSNYDG DGMSPEISSN
DLEKPTKHPV KVASRRRREV VPDSEDDDQD EHVSSVHHHD TAIESACPPV QADQDAIDEY
EVMRASHLSA DSKTNLSSSD SDNRTWVRGR SSIYVDAFNL ALDTVLEDEA HLFDENEMAI
FEQWRSLDYE AQYLYVRLFL RKAAAWHRRD RLGYHSDISD PDAAIESLQR SRELPKNETA
QKPNGEGDVA GVALQDWSLG DTFTFADSSE EYITSVDEAA SLLSLDELKM LAKEAKVQGK
NKGDILKKLL RMSSQQSGLL SVGLRRESTT GSVDSQGQDQ GSETPDPDTK QDSNRNQHFL
TKILTITGSC VRISPPIFKL FERVHLVFYR STEWTEKSLT TIILAKISKR NFPRYIVDRT
SNIFPHRQSL LEFEQAMRLE FEVDQILEFN GPPGEESYRR VLEVFDGLSA RWRSLLEEER
HKEEKVYEFG EGGYLRRFNA AHAYTRIAHK AAYVYGRLHD YLAEHNLLTE LLNQQLFQMA
RRGSWYQRKA LLEEHYMWEV KPDPNFSDPE QQKKHWRRIA ATTCESALKD RDCHLIYHYD
LQKRLTKLEK RLRIPKRLQH DFGHLRLHKP EEHTVMGTQL VRNDPTAGKR GGISTKTVWG
WKGYHSEGGI LRTLFAYLFY DVLFLYIPNV FQTAYQTCPL DLHTDAFYPT RASEINHRLA
DISNGEAPRI ICEVDAAHRE RRTCVVGLNW DYELEDLVEL AGCFPGEALA AVCKVMAQEY
RQRGGGVPDL VLWRTRPEGE GEGEGECMFG EVKSANDRLS DTQRLWIHVL TGAGVRVALV
NAVAGEVREV D
//