ID K3XV50_SETIT Unreviewed; 918 AA.
AC K3XV50;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 24-JAN-2024, entry version 55.
DE RecName: Full=Fanconi-associated nuclease {ECO:0000256|RuleBase:RU365033};
DE EC=3.1.4.1 {ECO:0000256|RuleBase:RU365033};
OS Setaria italica (Foxtail millet) (Panicum italicum).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC Panicoideae; Panicodae; Paniceae; Cenchrinae; Setaria.
OX NCBI_TaxID=4555 {ECO:0000313|EnsemblPlants:KQL09563, ECO:0000313|Proteomes:UP000004995};
RN [1] {ECO:0000313|EnsemblPlants:KQL09563, ECO:0000313|Proteomes:UP000004995}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Yugu1 {ECO:0000313|EnsemblPlants:KQL09563,
RC ECO:0000313|Proteomes:UP000004995};
RX PubMed=22580951; DOI=10.1038/nbt.2196;
RA Bennetzen J.L., Schmutz J., Wang H., Percifield R., Hawkins J.,
RA Pontaroli A.C., Estep M., Feng L., Vaughn J.N., Grimwood J., Jenkins J.,
RA Barry K., Lindquist E., Hellsten U., Deshpande S., Wang X., Wu X.,
RA Mitros T., Triplett J., Yang X., Ye C.Y., Mauro-Herrera M., Wang L., Li P.,
RA Sharma M., Sharma R., Ronald P.C., Panaud O., Kellogg E.A., Brutnell T.P.,
RA Doust A.N., Tuskan G.A., Rokhsar D., Devos K.M.;
RT "Reference genome sequence of the model plant Setaria.";
RL Nat. Biotechnol. 30:555-561(2012).
RN [2] {ECO:0000313|EnsemblPlants:KQL09563}
RP IDENTIFICATION.
RC STRAIN=Yugu1 {ECO:0000313|EnsemblPlants:KQL09563};
RG EnsemblPlants;
RL Submitted (AUG-2018) to UniProtKB.
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; AGNK02002233; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; K3XV50; -.
DR STRING; 4555.K3XV50; -.
DR EnsemblPlants; KQL09563; KQL09563; SETIT_005807mg.
DR Gramene; KQL09563; KQL09563; SETIT_005807mg.
DR eggNOG; KOG2143; Eukaryota.
DR HOGENOM; CLU_005116_2_0_1; -.
DR InParanoid; K3XV50; -.
DR OMA; ITDVMAN; -.
DR Proteomes; UP000004995; Chromosome IV.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0008409; F:5'-3' exonuclease activity; IBA:GO_Central.
DR GO; GO:0017108; F:5'-flap endonuclease activity; IBA:GO_Central.
DR GO; GO:0070336; F:flap-structured DNA binding; IBA:GO_Central.
DR GO; GO:0016818; F:hydrolase activity, acting on acid anhydrides, in phosphorus-containing anhydrides; IEA:InterPro.
DR GO; GO:0004528; F:phosphodiesterase I activity; IEA:UniProtKB-EC.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0007129; P:homologous chromosome pairing at meiosis; IEA:EnsemblPlants.
DR GO; GO:0036297; P:interstrand cross-link repair; IBA:GO_Central.
DR CDD; cd22326; FAN1-like; 1.
DR Gene3D; 3.30.70.2330; -; 1.
DR Gene3D; 3.40.1350.10; -; 1.
DR Gene3D; 3.30.160.60; Classic Zinc Finger; 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; IPR014905; HIRAN.
DR InterPro; IPR006642; Rad18_UBZ4.
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; PF08797; HIRAN; 1.
DR Pfam; PF08774; VRR_NUC; 1.
DR SMART; SM00910; HIRAN; 1.
DR SMART; SM00990; VRR_NUC; 1.
DR SMART; SM00734; ZnF_Rad18; 1.
DR PROSITE; PS51908; ZF_UBZ4; 1.
PE 3: Inferred from homology;
KW DNA damage {ECO:0000256|ARBA:ARBA00022763, ECO:0000256|PROSITE-
KW ProRule:PRU01256};
KW DNA repair {ECO:0000256|ARBA:ARBA00023204, ECO:0000256|PROSITE-
KW ProRule:PRU01256};
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:UP000004995};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU01256}.
FT DOMAIN 72..101
FT /note="UBZ4-type"
FT /evidence="ECO:0000259|PROSITE:PS51908"
FT REGION 35..63
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 918 AA; 103042 MW; A14726BAC4559695 CRC64;
MLTGRESLVR LIGRRRRSPL PASLAAVLSP SCPLPSASPA QADDGGGPGE AAGVEAGSSY
GGSGGVGVRA EWVSCPVCGE SIRGSDYCVN THLDICLTRG TKRKLTQSTL LNFRFSKKVS
AEPTSNNLTN EVETESVKQI DEDLSRNQEF ISLDSDTESS KAGATISSSG CLNGSFRTSK
TISTYAPSNT ILPDVKDEHC SSSMLPTVAT SCSDDACADL DSSTTITVDT VIVGRRFHEN
IELREDAGIT FLRDPQNAKD SDAIKVLYAA SECEMLGYLP RELAKVLAPL MDMHYVECEG
CVVGLPEQQL GNVPIQITIQ KCKIDNQIND DPEYWQSLWE KFISTVKSGN FQRPSSARYQ
RNFNLMIADV MANHAHVFSD IERSFLASFK SLSDDGQRLF VRIYTRKGPW FRKSTISYRE
ISDLEHAVME LKLAGYINML SCTVDPSEYD MKEILDVLSV PEIKEILKEL PKENTSCIRR
HELACTLLSL YHNGTCASLP KRILKWTGTC IRISKMADEL LWRIQAIRVA QLMDESLDNN
NMDLVTRCID LSENRLCTMP KQENATSPEH SPSFFSHFSA SWVYSKILTL GVSVYERDRR
YEDAIRILKI LLSKVACDRR RGYWTLRLSV DLDHMGRPNE SLSVAEGGAI DPWVRAGSKF
ALQRRVLRLS KPPRRWKVPS YADYVKRNIK EMNIEGRPLN CETGAKNLFY GYDGELCGVE
QLALQYYADE GGGWRGTHSE GGIWMTIFGL LMWDVMFSDI QDVFQSKFQT APLDLETDYF
YKSRKDLAES QLKKIQEGMA EEMLISSWEL HQGTSCRGVN WDRHSLTDLR AVVACIGGHR
LALLLRHLAV DYRSWSSGMP DLLLWRFLDE RGGGEAKLVE VKGPRDQLSE QQRAWILVLM
DFGFDVEVCK VSPVTKRR
//
