ID A0A2H3TG29_FUSOX Unreviewed; 854 AA.
AC A0A2H3TG29;
DT 31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT 31-JAN-2018, sequence version 1.
DT 24-JAN-2024, entry version 19.
DE RecName: Full=Fanconi-associated nuclease {ECO:0000256|RuleBase:RU365033};
DE EC=3.1.4.1 {ECO:0000256|RuleBase:RU365033};
GN ORFNames=FRV6_07797 {ECO:0000313|EMBL:SCO83670.1};
OS Fusarium oxysporum (Fusarium vascular wilt).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC Fusarium oxysporum species complex.
OX NCBI_TaxID=5507 {ECO:0000313|EMBL:SCO83670.1, ECO:0000313|Proteomes:UP000219369};
RN [1] {ECO:0000313|Proteomes:UP000219369}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=V64-1 {ECO:0000313|Proteomes:UP000219369};
RA Guldener U.;
RL Submitted (SEP-2016) 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}.
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DR EMBL; FMJY01000004; SCO83670.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2H3TG29; -.
DR VEuPathDB; FungiDB:FOC1_g10014013; -.
DR VEuPathDB; FungiDB:FOC4_g10011303; -.
DR VEuPathDB; FungiDB:FOIG_03044; -.
DR VEuPathDB; FungiDB:FOMG_05337; -.
DR VEuPathDB; FungiDB:FOXG_01762; -.
DR VEuPathDB; FungiDB:FOZG_05503; -.
DR VEuPathDB; FungiDB:HZS61_009680; -.
DR OrthoDB; 38749at2759; -.
DR Proteomes; UP000219369; 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}.
FT DOMAIN 719..847
FT /note="VRR-NUC"
FT /evidence="ECO:0000259|SMART:SM00990"
FT REGION 1..119
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 292..328
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 19..38
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 51..75
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 303..328
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 854 AA; 98088 MW; 7BD2365444E1BDD0 CRC64;
MDAFVTRLSK PPSQLREQVR GDSPEKERPS KRAKRQGSPD SEGGLCPDHP QDISPREDFP
DNEAAKTKYQ TEEHPRITGI ESALPPAAEG QEAVEQYETM KSSQGSAHDE DDTTETTQPL
WVKGRSSIYV DAFNLALDTV LEEESHLFDG KETEVFKQWR ELNYEAQYLY VRLFLRKTAS
WHRHSRLGYH NDISDLEAAI TTLQSSRVLP ASTATPIQSP VHDLELEESR LDETFSFADR
SEDHFDSVEE AASLLSLDEL KELAKEAKVQ GRNKSELIRS LVKMSKQQSG LMSVGLSRHN
SRGSVSEDQE NLDAKAKGKD TAKLRREDSN REQHFLTKIL AILGPCIRLS PPAFKLFERV
HLVFYRSTEW TEKSLTTIIL AKIARRHFPE YIVCRTSTIF MSRLHLLEYE TAIRMEAEVD
AWEFSSPPGD EGLRLMVNIF EKVYPRWKIL VEEEQHKEHT VYEMGEGAYL RRFTPGHSYT
RIVHKAAPVF GKLKQHLREH ELLTELLDQR LFHPARRGSW YQRKALLEEH YMPALDPNPK
FTDPEQQKKH WKKIAVATCE AGLQDPDCHL IFHYDLQKRL VKLEKKLRIP RRLQHDFGHV
DLQKPIEHTI KGIQLKKDII AKGGRQVSTK TIWLDELDTQ EECSVEAMCL SQYRSEGWKG
YHAEGGIIRT LFAYLFYDIL FIYIPNVFQT AYQTCPLDLH TDAFYPSRAS EINHRLVEIA
NGEAPRLIRK VWESEHERRT SVVGLNWDFE IDDLVELAGC FEGSALAAVC KVMAQEYRQR
GGGIPDLILW RTNNLPEDSN KVPGRPKGEV MFSEVKSAND RLSDTQRLWI HVLTGAGVKV
ALCNAIAKEV REVD
//
