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Database: UniProt
Entry: A0A194VAA0_9PEZI
LinkDB: A0A194VAA0_9PEZI
Original site: A0A194VAA0_9PEZI 
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
//
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