ID A0A1D6NU95_MAIZE Unreviewed; 967 AA.
AC A0A1D6NU95;
DT 30-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 30-NOV-2016, sequence version 1.
DT 24-JAN-2024, entry version 33.
DE RecName: Full=Fanconi-associated nuclease {ECO:0000256|RuleBase:RU365033};
DE EC=3.1.4.1 {ECO:0000256|RuleBase:RU365033};
GN ORFNames=ZEAMMB73_Zm00001d045179 {ECO:0000313|EMBL:AQL01722.1};
OS Zea mays (Maize).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC Panicoideae; Andropogonodae; Andropogoneae; Tripsacinae; Zea.
OX NCBI_TaxID=4577 {ECO:0000313|EMBL:AQL01722.1};
RN [1] {ECO:0000313|EMBL:AQL01722.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Seedling {ECO:0000313|EMBL:AQL01722.1};
RG Maize Genome Sequencing Project;
RA Ware D.;
RT "Update maize B73 reference genome by single molecule sequencing
RT technologies.";
RL Submitted (DEC-2015) 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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CM000785; AQL01722.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1D6NU95; -.
DR OrthoDB; 38749at2759; -.
DR ExpressionAtlas; A0A1D6NU95; baseline and differential.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
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; IEA:EnsemblPlants.
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 Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU01256}.
SQ SEQUENCE 967 AA; 108693 MW; 2B810A2F25F284B1 CRC64;
MLTGRESLVR LIGRRRRSPL PASLVAALSL PSPSPSTSLA QADDGGGSGE AAGGEAGSTS
GGSRVVGMGA EWVVCPVCGD SIRGSDYCVN THLDMCLTRG TKRKLTQSTL LNFQFSKKVS
AEPTINNLNN ESETENMKQI DEGLSSDQAF FAFDSEIGSS KAGTTISSPT CMNDSLGTSE
TITSYAPSNT VLSDAKDAVN DGAGELPTVA TSCSFDECAV MDSSTVVVVD TVIVGRRFHE
NIELREDADI TFMRDPQNAK DPDAIKVLHA GSECEEMLGY LPRDLAKVLA PLVDKHHVEC
EGSVVGLHEQ QFGNVPIQIT IQKCKSDNQR NNDPNCCQSL WENFVSIVKR ENFRRPHSAR
YQTNFNLMIA DVMVNHAHVF SDIEKSFLAS FKSLSDDGQR LFIRIYTRKG PWFRKGSISY
QEISDLEHAV MELELAGYID MLSCTIDPFE YDMKEILDVL SVPEMKEILK ELPKDNTICT
RRHELVSTLL SSYRNGTCAS LPKRILKWTG TCIRISKMAD ELLWRIQRLF FLNGDQDLSS
FLLVEFGIVK FPDYVCSISH RIFQERNDLL EYEDAIRVAQ VMDESLDNNK MDLVTRCIDL
SENRLCIMPK RENTITPERL RSFFSRFSAS WVYSKILTLG VSVYERDRRY EDAVRILKTL
LSTVACDRRR GYWALRLSID LEHMGRPNES LSTAEGGATD PWVRAGSKFA LQRRVLRLSK
PPRRWKVPSY ADYVKRNIRE VSIEGRPLNC ETGAKNVFYG YDGELCGVEQ LALQYYADEG
GGWQGTHSEG SIWMTIFGLL MWDVMFSDIQ DVFQSKFQTA PLDLGTDDFY KSRENIAESQ
LKRIRDGMAE EMLISSWELH QGTSCQGVNW ARYSLTDLRA VVACVGGHRL ASLLRHLAVD
YRSWSSGMPD LLLWRFLDER GGGEAKLVEV KGPRDQLSEQ QRAWILVLMD FGFDVEVCKV
SPVTKRR
//
