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Database: UniProt
Entry: W7U0K5_9STRA
LinkDB: W7U0K5_9STRA
Original site: W7U0K5_9STRA 
ID   W7U0K5_9STRA            Unreviewed;      1009 AA.
AC   W7U0K5;
DT   16-APR-2014, integrated into UniProtKB/TrEMBL.
DT   16-APR-2014, sequence version 1.
DT   22-FEB-2023, entry version 27.
DE   RecName: Full=Fanconi-associated nuclease {ECO:0000256|RuleBase:RU365033};
DE            EC=3.1.4.1 {ECO:0000256|RuleBase:RU365033};
GN   ORFNames=Naga_100121g2 {ECO:0000313|EMBL:EWM26169.1};
OS   Nannochloropsis gaditana.
OC   Eukaryota; Sar; Stramenopiles; Ochrophyta; Eustigmatophyceae;
OC   Eustigmatales; Monodopsidaceae; Nannochloropsis.
OX   NCBI_TaxID=72520 {ECO:0000313|EMBL:EWM26169.1, ECO:0000313|Proteomes:UP000019335};
RN   [1] {ECO:0000313|EMBL:EWM26169.1, ECO:0000313|Proteomes:UP000019335}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=B-31 {ECO:0000313|EMBL:EWM26169.1,
RC   ECO:0000313|Proteomes:UP000019335};
RX   PubMed=23966634; DOI=10.1093/mp/sst120;
RA   Corteggiani Carpinelli E., Telatin A., Vitulo N., Forcato C., D'Angelo M.,
RA   Schiavon R., Vezzi A., Giacometti G.M., Morosinotto T., Valle G.;
RT   "Chromosome Scale Genome Assembly and Transcriptome Profiling of
RT   Nannochloropsis gaditana in Nitrogen Depletion.";
RL   Mol. Plant 7:323-335(2014).
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   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EWM26169.1}.
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DR   EMBL; AZIL01000701; EWM26169.1; -; Genomic_DNA.
DR   AlphaFoldDB; W7U0K5; -.
DR   EnsemblProtists; EWM26169; EWM26169; Naga_100121g2.
DR   OrthoDB; 38749at2759; -.
DR   Proteomes; UP000019335; Chromosome 9.
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   Gene3D; 3.40.1350.10; -; 1.
DR   InterPro; IPR033315; Fan1-like.
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; 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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000019335}.
FT   DOMAIN          874..994
FT                   /note="VRR-NUC"
FT                   /evidence="ECO:0000259|SMART:SM00990"
FT   REGION          450..505
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          811..834
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        481..495
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        811..825
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1009 AA;  110840 MW;  05DB1A3C6B5453FA CRC64;
     MPCDGRSKTE KREQEEDDEV EIIEVLTVRS KRVKSSTLYG YGFGSSTLNS LHPTKTLPSL
     PPLPPVPAWG RLIDEQSTAK VALQRFLGFS PPLLRHAYTA CYRGVFNDRF NAVPGMGIAS
     IFGRYGSGVR SILNVSGCST FSSRSVEHAE GLVRDQGRSD GQAILNPEVI QDVEGEEDDD
     VSSLPNGNAQ GAKFWNKSHR NFNFILNWAL ECSEVLKSCR QDVQDLQKLR VGLSPEAATL
     LWQCFHSPRA ICRVHVQREG KKTIVKGKSS DRNDNGALQE LVKQQVVRDV TGDQGALLMH
     LYDVFAALRA DELARMTLCL FGSAAAATSA VSSSLPCSWR GRRNASREAS LKSLSTFLER
     CQKEGSPERV RRKLGHDLVK WLAKETQAPL QVKGEQQQQQ SFRLVCLAPR LAKLLQRLFA
     LFFMTNGYDA EDAVVLWWND LETLRFASRG DVDGAGQGRS GEGLLPFASR GPSTSTKSSA
     DDENQEAEAT IQKAERPPRS ELPVAWPGLG SPEIPCAYRQ FADTTLSLSD AFEAAVASGD
     SATAYACLHT VSDLFLPRPM LPAHASGSVV SDPACTSLAA LEVTQVKTGT HRFQLDVPAE
     YRGLEELPGI LFKVLARVIG RGIGLLERDR KHAQAVHYLK IILDGSEPLP WSLRGHFHSR
     LVLDLVHCNR PGEALAACEH ALADPRVDGE DRLFLQAKCL SLAVAPRRWK KPTFPALQTA
     PVLELKMAEV QGWRQKGKSL EDSVLACLLQ REGDGMAGRE GCFPGVREED PQQAGHWRGA
     HWENGLMLSL FGILCWDVLW SAQPAHSEKE SILATSSQGA NGGRPDCRTR SSRGTRSTQS
     CRYQHAPCDL QHNRGFLKSC PGRVSALEQV LARIQRGESG ALLAENHARY HGTLCLGIDW
     TTFSLPVLQT VAEALGSSAL MLLCETLIRD YSLLSHGFPD LLLWRDAGPH GGMPAMVRLV
     EVKGPGDSLS WAQKYWIDKL LGVGVRVEVA RVVEGNERGL RPGAQRRKA
//
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