FAN1_ORYSJ
ID FAN1_ORYSJ Reviewed; 964 AA.
AC Q5SNL7; A0A0N7KLL9; B9FRR6;
DT 05-OCT-2010, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 102.
DE RecName: Full=Fanconi-associated nuclease 1 homolog {ECO:0000305};
DE EC=3.1.4.1 {ECO:0000250|UniProtKB:Q9Y2M0};
GN OrderedLocusNames=Os06g0171800, LOC_Os06g07490;
GN ORFNames=OsJ_20287, P0675A05.29;
OS Oryza sativa subsp. japonica (Rice).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Oryza; Oryza sativa.
OX NCBI_TaxID=39947;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=16100779; DOI=10.1038/nature03895;
RG International rice genome sequencing project (IRGSP);
RT "The map-based sequence of the rice genome.";
RL Nature 436:793-800(2005).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=cv. Nipponbare;
RX PubMed=18089549; DOI=10.1093/nar/gkm978;
RG The rice annotation project (RAP);
RT "The rice annotation project database (RAP-DB): 2008 update.";
RL Nucleic Acids Res. 36:D1028-D1033(2008).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=cv. Nipponbare;
RX PubMed=24280374; DOI=10.1186/1939-8433-6-4;
RA Kawahara Y., de la Bastide M., Hamilton J.P., Kanamori H., McCombie W.R.,
RA Ouyang S., Schwartz D.C., Tanaka T., Wu J., Zhou S., Childs K.L.,
RA Davidson R.M., Lin H., Quesada-Ocampo L., Vaillancourt B., Sakai H.,
RA Lee S.S., Kim J., Numa H., Itoh T., Buell C.R., Matsumoto T.;
RT "Improvement of the Oryza sativa Nipponbare reference genome using next
RT generation sequence and optical map data.";
RL Rice 6:4-4(2013).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=15685292; DOI=10.1371/journal.pbio.0030038;
RA Yu J., Wang J., Lin W., Li S., Li H., Zhou J., Ni P., Dong W., Hu S.,
RA Zeng C., Zhang J., Zhang Y., Li R., Xu Z., Li S., Li X., Zheng H., Cong L.,
RA Lin L., Yin J., Geng J., Li G., Shi J., Liu J., Lv H., Li J., Wang J.,
RA Deng Y., Ran L., Shi X., Wang X., Wu Q., Li C., Ren X., Wang J., Wang X.,
RA Li D., Liu D., Zhang X., Ji Z., Zhao W., Sun Y., Zhang Z., Bao J., Han Y.,
RA Dong L., Ji J., Chen P., Wu S., Liu J., Xiao Y., Bu D., Tan J., Yang L.,
RA Ye C., Zhang J., Xu J., Zhou Y., Yu Y., Zhang B., Zhuang S., Wei H.,
RA Liu B., Lei M., Yu H., Li Y., Xu H., Wei S., He X., Fang L., Zhang Z.,
RA Zhang Y., Huang X., Su Z., Tong W., Li J., Tong Z., Li S., Ye J., Wang L.,
RA Fang L., Lei T., Chen C.-S., Chen H.-C., Xu Z., Li H., Huang H., Zhang F.,
RA Xu H., Li N., Zhao C., Li S., Dong L., Huang Y., Li L., Xi Y., Qi Q.,
RA Li W., Zhang B., Hu W., Zhang Y., Tian X., Jiao Y., Liang X., Jin J.,
RA Gao L., Zheng W., Hao B., Liu S.-M., Wang W., Yuan L., Cao M.,
RA McDermott J., Samudrala R., Wang J., Wong G.K.-S., Yang H.;
RT "The genomes of Oryza sativa: a history of duplications.";
RL PLoS Biol. 3:266-281(2005).
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:0000250|UniProtKB:Q9Y2M0}.
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:0000250|UniProtKB:Q9Y2M0};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000250|UniProtKB:Q9I2N0};
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:Q9I2N0};
CC Note=Binds 2 magnesium or manganese ions per subunit.
CC {ECO:0000250|UniProtKB:Q9I2N0};
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q5SNL7-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q5SNL7-2; Sequence=VSP_039787, VSP_039788;
CC -!- SIMILARITY: Belongs to the FAN1 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=EEE65177.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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; AP002071; BAD72189.1; -; Genomic_DNA.
DR EMBL; AP008212; BAF18851.1; -; Genomic_DNA.
DR EMBL; AP014962; BAS96385.1; -; Genomic_DNA.
DR EMBL; CM000143; EEE65177.1; ALT_SEQ; Genomic_DNA.
DR RefSeq; XP_015643669.1; XM_015788183.1. [Q5SNL7-1]
DR AlphaFoldDB; Q5SNL7; -.
DR SMR; Q5SNL7; -.
DR STRING; 4530.OS06T0171800-01; -.
DR PaxDb; Q5SNL7; -.
DR PRIDE; Q5SNL7; -.
DR EnsemblPlants; Os06t0171800-01; Os06t0171800-01; Os06g0171800. [Q5SNL7-1]
DR GeneID; 4340269; -.
DR Gramene; Os06t0171800-01; Os06t0171800-01; Os06g0171800. [Q5SNL7-1]
DR KEGG; osa:4340269; -.
DR eggNOG; KOG2143; Eukaryota.
DR HOGENOM; CLU_005116_2_0_1; -.
DR InParanoid; Q5SNL7; -.
DR OMA; ITDVMAN; -.
DR OrthoDB; 1003565at2759; -.
DR Proteomes; UP000000763; Chromosome 6.
DR Proteomes; UP000007752; Chromosome 6.
DR Proteomes; UP000059680; Chromosome 6.
DR Genevisible; Q5SNL7; OS.
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 Gene3D; 3.40.1350.10; -; 1.
DR InterPro; IPR033315; Fan1-like.
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; PTHR15749; 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 Alternative splicing; DNA damage; DNA repair; Hydrolase; Magnesium;
KW Manganese; Metal-binding; Nuclease; Reference proteome; Zinc; Zinc-finger.
FT CHAIN 1..964
FT /note="Fanconi-associated nuclease 1 homolog"
FT /id="PRO_0000398624"
FT DOMAIN 844..958
FT /note="VRR-NUC"
FT ZN_FING 63..92
FT /note="UBZ4-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01256"
FT REGION 31..56
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 66
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01256"
FT BINDING 69
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01256"
FT BINDING 83
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01256"
FT BINDING 87
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01256"
FT BINDING 786
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q9I2N0"
FT BINDING 907
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q9I2N0"
FT BINDING 907
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q9I2N0"
FT BINDING 926
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q9I2N0"
FT BINDING 927
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q9I2N0"
FT VAR_SEQ 1..386
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_039787"
FT VAR_SEQ 387..407
FT /note="SFQLLPDDGQRLFVRIYTRKG -> MMDKGSLLGSTLEKVAISASR (in
FT isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_039788"
SQ SEQUENCE 964 AA; 107918 MW; 7F10C365308ED754 CRC64;
MLTGRESLVR LIGRRRRSPL PAALALAVPP SRSLQDDAAD AEREAAAGGS SSGGGDAAGA
AGWVACPVCG ESIRGTDYCV NTHLDICLTR GTKRKLTQST LLDFSFSRKA TDDYALNNLN
TSDEAEHMEP TDGNVSSDGA FFSLNNDKVN SKGSANASSP GCLHGSPDIS ETCDTCLPPN
VLLPYTENTA NNGVVKKCLS HMPSTDATSS TIGLLSVTDS SNSVVVDTVI VGRRFHENIE
LQEGASITLL RDPQNAKDPD AIKVLYAGYE CEQMLGYLPR ELAKVLAPLL DRHYIECEGC
VVGVPEQQLD HVPIQLKCQK YTDENETYDD LKHPQFLWEN FICAVGNGNL LQPSSTRYQT
NFSSMITDVM ANHSHLFSDK EKSFLDSFQL LPDDGQRLFV RIYTRKGPWF RMSSISYREI
SDLGQAAMEL KLAGYIDMIS CMDDLSNYDL KEVIDVLSVP EMKEILKELQ KNNVSCTRRH
ELLSTLLYLY RNGTCTILPK RILKWTGTCI RTSDVADELL WRVQRLFFLN GDQDLSFFLL
VDLGLVRFPV YACTISHRVF QEISDLLQYE EAIQVAQVMD QSLDNSNMEM VTRCIELSEN
RLSTAPKEEN ATRAEPPPSF FSRFSASSVY SKILTLGVSV YERDRRYTDA IRVLKRLLST
VASDRKRGYW ALRLSVDLEH MNRSNESLSI AEAGVIDPWV RAGSKIALQR RVVRLSKPPR
RWKVPSYANA VTTNIKEVNI EGRPLNCETG AKNVFYGYDG ELCGVEQLAL QYYADEGGGW
RGTHSEGGIW MTIFGLLMWD AIFSDVPDVF QTKFQTAPLD LETDEFYRSR KDLIESQLKK
IQDGIAEEIL ISSWELHQGT SCRGVNWDRH SLTDLRAAVV CTGGHRLASL LRHLALDYRS
WSSGMPDLLL WRFLDERGGG EAKLVEVKGP RDQLSEQQRA WILVLMDFGF DVEVCKVSPV
SKRR
