ID A0A010R986_9PEZI Unreviewed; 843 AA.
AC A0A010R986;
DT 11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT 11-JUN-2014, sequence version 1.
DT 24-JAN-2024, entry version 37.
DE RecName: Full=Fanconi-associated nuclease {ECO:0000256|RuleBase:RU365033};
DE EC=3.1.4.1 {ECO:0000256|RuleBase:RU365033};
GN ORFNames=CFIO01_03706 {ECO:0000313|EMBL:EXF74274.1};
OS Colletotrichum fioriniae PJ7.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum;
OC Colletotrichum acutatum species complex.
OX NCBI_TaxID=1445577 {ECO:0000313|EMBL:EXF74274.1, ECO:0000313|Proteomes:UP000020467};
RN [1] {ECO:0000313|EMBL:EXF74274.1, ECO:0000313|Proteomes:UP000020467}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PJ7 {ECO:0000313|EMBL:EXF74274.1,
RC ECO:0000313|Proteomes:UP000020467};
RA Baroncelli R., Thon M.R.;
RT "The genome sequence of Colletotrichum fioriniae PJ7.";
RL Submitted (FEB-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|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:EXF74274.1}.
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DR EMBL; JARH01000997; EXF74274.1; -; Genomic_DNA.
DR RefSeq; XP_007602010.1; XM_007601948.1.
DR AlphaFoldDB; A0A010R986; -.
DR STRING; 1445577.A0A010R986; -.
DR KEGG; cfj:CFIO01_03706; -.
DR eggNOG; KOG2143; Eukaryota.
DR HOGENOM; CLU_005116_1_0_1; -.
DR OrthoDB; 38749at2759; -.
DR Proteomes; UP000020467; 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:UP000020467}.
FT DOMAIN 720..836
FT /note="VRR-NUC"
FT /evidence="ECO:0000259|SMART:SM00990"
FT REGION 1..64
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 299..328
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 10..24
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 843 AA; 97007 MW; 52D2E9B153B57CD8 CRC64;
MDAFVQRIPR PRSQPSSRSP TRPSPLSERP AKKVKVEIKD SDCDDDDYEI KSEVDEADTS
GLTVNDVSDA DDEVKHHTRQ TDIESTLPPI QLDKEAIEEY ELMRSSQVSV HEDEPAVAPE
RKWVRGKSSI YVDAFNLALD TVLSDESHLF DAKECDVFEQ WKSLGYEAQY LYVRLFLRKT
SAWHRQDRLG YYSDVSDPEA AIVSLQKVRG LPEPDAPACS NPVEGIDLEE FSLDDNFTFA
DASEEHITTI EEASSLLSLD ELKDLAKEAK FQGRNKADLV KALCRTGYQQ TGLFAHGLQR
SGSGESQTAR GLMRDRHDTP PHLSRQDSNQ TQHFLEKIRI ITGPCIRLSP LTYKLFERVH
LVFYRSTEWT EKSLTAIILA SIARRNYPEY IVCRSTNIFA SRRHVLEFES AVRVEAEVDQ
VLEFNGSPGE AGLRKVVDVF DRVYPRWQTL LREEQDKERR LYEEGEGAYL RRFTPVHSYT
RIVHKAAYVF GKLKHYEREH SILTKLLEQH LFHPARRGSW YQRKALLEEH YMYALDANAV
SPDPDIQKKH WKRIAATTCE TALEDNECHL IYHYDLQKRL LKLEKQLRIP RRLQHDFGHV
RLQKPLEHTV EGIQVIKEDR QGRNGRQAST KTIWVDELEE GGECSVEEMC LSWYRSKGYK
GYHAEGGIVR TLFAYLFYDI LFLYIPNVFQ TAYQTCPLDL HTDSFYPTRL SEINHRLVEI
GNGGAEAIIR EVDARERERR TCVIGLNWDY DVEDLVELVG CFDGSALAAL CKVMAQEYRQ
RGGGLPDLIL WRTEPKKECM FAEVKSANDR LSDTQRLWIH VLTGAGVKVV LCNAVAKEVK
IVD
//
