ID A0A0E0DXR8_9ORYZ Unreviewed; 948 AA.
AC A0A0E0DXR8;
DT 27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT 27-MAY-2015, sequence version 1.
DT 24-JAN-2024, entry version 31.
DE RecName: Full=Fanconi-associated nuclease {ECO:0000256|RuleBase:RU365033};
DE EC=3.1.4.1 {ECO:0000256|RuleBase:RU365033};
OS Oryza meridionalis.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Oryza.
OX NCBI_TaxID=40149 {ECO:0000313|EnsemblPlants:OMERI06G05820.2};
RN [1] {ECO:0000313|EnsemblPlants:OMERI06G05820.2}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=OR44 {ECO:0000313|EnsemblPlants:OMERI06G05820.2};
RA Wing R.A., Panaud O., Henry R.;
RL Submitted (DEC-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EnsemblPlants:OMERI06G05820.2}
RP IDENTIFICATION.
RG EnsemblPlants;
RL Submitted (APR-2015) 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 AlphaFoldDB; A0A0E0DXR8; -.
DR EnsemblPlants; OMERI06G05820.2; OMERI06G05820.2; OMERI06G05820.
DR Gramene; OMERI06G05820.2; OMERI06G05820.2; OMERI06G05820.
DR Proteomes; UP000008021; Chromosome 6.
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:0036297; P:interstrand cross-link repair; IEA:InterPro.
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; 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; 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:UP000008021};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU01256}.
FT DOMAIN 65..94
FT /note="UBZ4-type"
FT /evidence="ECO:0000259|PROSITE:PS51908"
FT REGION 35..57
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 948 AA; 105645 MW; 6125FD57450FC269 CRC64;
MLTGRESLVR LIGRRRRSPL PAALALALAV PPSRSLQDDA ADAEREAAAG GSSSGGGDVA
VAAGWVACPV CGESIRGTDY CVNTHLDICL TRGTKRKLTQ STLLDFSFSK KDTADPALNS
LNDSNEAEHM EQTDRNVSSD GAFLSLNNDK VNSKGSANAS SPGCLHGSPD ISETCDTCLP
PDALLAYMEN TANNGVVKKF LSHMPSTDAT SSTIGLLSVT DSSNSVVVDT VIVGRRFHEN
IELQEGASIT LLRDPQNAKD PDAIKVLYAG YECEQMLGYL PRELAKVLAP LLDRHYIECE
GCVVGVPEQQ LDHVPIQLKC QKYTDENESY DDLKHPQFLW ENFIGAVGNG NLLQPSSTRY
QTNFSLMITD VMANHSHLFS DKEKSFLGYI DMISCMDDLS NYDLKEVIDV LSVPEMKEIL
KELQKNNVSC TRRHELLSTL LSLYHNGTCT ILPKRILRTC IRISDVADEL LWRVQMLFFL
NGDQDLSSFL LVDLGLVRFP VYACTISHRV FQERNDLLQY EEAIQVAQVM DQSLDNSNME
MVTRCIELSE KRLSTAPKEE NATRAEPPPS FFSRFSASLV YSKILTLGAS VYERDRRYTD
AIRVLKRLLS TVASDRKRGY WALRLSVDLE HMNRSNESLS IAEAGVIDPW VRAGSKIALQ
RRVVRLSKPP RRWKVPSYAN AVTKNIKEVN IEGRPLNCET GAKNVFYGYD GELCGVEQLA
LQYYADEGGG WRGTHSEGGI WMTIFGLLMW DAIFSDVPDV FQTKFQTAPL DLETDEFYRS
RKDLIESQLK KIQDGIAEEI LISSWELHQG TSCRGVNWDR HSLTDLRAAV VCTGGHRLAS
LLRHLALDYR SWSSGMPDLL LWRFLDERGG GEAKLVEVKG PRDQLSEQQR AWILVLMDFG
FDVEVCKIAE NEKDGLFQSP GHLTMIGASI PTAQNSYVWA KPTMSIGQ
//
