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Database: UniProt
Entry: D7G0C5_ECTSI
LinkDB: D7G0C5_ECTSI
Original site: D7G0C5_ECTSI 
ID   D7G0C5_ECTSI            Unreviewed;      1005 AA.
AC   D7G0C5;
DT   10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT   10-AUG-2010, sequence version 1.
DT   28-JUN-2023, entry version 40.
DE   RecName: Full=Fanconi-associated nuclease {ECO:0000256|RuleBase:RU365033};
DE            EC=3.1.4.1 {ECO:0000256|RuleBase:RU365033};
GN   ORFNames=Esi_0040_0052 {ECO:0000313|EMBL:CBJ26652.1};
OS   Ectocarpus siliculosus (Brown alga) (Conferva siliculosa).
OC   Eukaryota; Sar; Stramenopiles; Ochrophyta; PX clade; Phaeophyceae;
OC   Ectocarpales; Ectocarpaceae; Ectocarpus.
OX   NCBI_TaxID=2880 {ECO:0000313|EMBL:CBJ26652.1, ECO:0000313|Proteomes:UP000002630};
RN   [1] {ECO:0000313|EMBL:CBJ26652.1, ECO:0000313|Proteomes:UP000002630}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Ec32 / CCAP1310/4 {ECO:0000313|Proteomes:UP000002630};
RX   PubMed=20520714; DOI=10.1038/nature09016;
RA   Cock J.M., Sterck L., Rouze P., Scornet D., Allen A.E., Amoutzias G.,
RA   Anthouard V., Artiguenave F., Aury J.M., Badger J.H., Beszteri B.,
RA   Billiau K., Bonnet E., Bothwell J.H., Bowler C., Boyen C., Brownlee C.,
RA   Carrano C.J., Charrier B., Cho G.Y., Coelho S.M., Collen J., Corre E.,
RA   Da Silva C., Delage L., Delaroque N., Dittami S.M., Doulbeau S., Elias M.,
RA   Farnham G., Gachon C.M., Gschloessl B., Heesch S., Jabbari K., Jubin C.,
RA   Kawai H., Kimura K., Kloareg B., Kupper F.C., Lang D., Le Bail A.,
RA   Leblanc C., Lerouge P., Lohr M., Lopez P.J., Martens C., Maumus F.,
RA   Michel G., Miranda-Saavedra D., Morales J., Moreau H., Motomura T.,
RA   Nagasato C., Napoli C.A., Nelson D.R., Nyvall-Collen P., Peters A.F.,
RA   Pommier C., Potin P., Poulain J., Quesneville H., Read B., Rensing S.A.,
RA   Ritter A., Rousvoal S., Samanta M., Samson G., Schroeder D.C., Segurens B.,
RA   Strittmatter M., Tonon T., Tregear J.W., Valentin K., von Dassow P.,
RA   Yamagishi T., Van de Peer Y., Wincker P.;
RT   "The Ectocarpus genome and the independent evolution of multicellularity in
RT   brown algae.";
RL   Nature 465:617-621(2010).
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; FN648597; CBJ26652.1; -; Genomic_DNA.
DR   AlphaFoldDB; D7G0C5; -.
DR   STRING; 2880.D7G0C5; -.
DR   EnsemblProtists; CBJ26652; CBJ26652; Esi_0040_0052.
DR   eggNOG; KOG2143; Eukaryota.
DR   InParanoid; D7G0C5; -.
DR   OrthoDB; 38749at2759; -.
DR   Proteomes; UP000002630; Chromosome LG15.
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:UP000002630}.
FT   DOMAIN          840..992
FT                   /note="VRR-NUC"
FT                   /evidence="ECO:0000259|SMART:SM00990"
FT   REGION          1..38
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          78..127
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          223..282
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          714..740
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        78..104
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        223..276
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1005 AA;  110350 MW;  BF2D5247AEB8452E CRC64;
     MELGGSIATP LPPPTVADGW GGKPALQHYP HPSDAAATAG VGVQRCEWGQ TTQQVRRERQ
     QQPQEFPPAV LALQLQEWGE TQQQQPRQEA SPTLRRQQWG RGASAATHSL GGGCLRDDQE
     AGHDQPPFVM MGMLDDSRAL LLPTTRERRE VMGSLSSASV PVTWTDSTGQ SRTAILTRTK
     AKPKPCNPLP MLANLLAWMR ELPPGALPEN RLRIRLETLL ALQSPSKSVS RQSSTIGKNT
     NSNSGHTNRD RGDTTTSTAT ATNNNNSNTT SNHDGRASGG GDGDGDLSLG AAWLLAHLMF
     GMDGGGKATG PFEREILNGK VSLSGAEANA MPLLLCPLIG WSPRPREVIQ AMSEGAGILC
     AYSVELAAFE TQTGICGKAA DELVHAGFAR KVEFGEMLAL DQKMEDACEL VLKIFLCNWD
     VDREVRAQVA LGLTKTGPVA SGLCPPDIPS LFSGRQKWRS STTAVRGGDE RSSCRGRMGG
     LVGDLCVRLH SWCHQVMRAG RDLRVLLLLQ VLKGETAGDL TSQREWTGPM AQAFGLLGGA
     EVSYHKRHRD SIGGTASAGW VASLSKEERL LEVACLRLKQ AMKWVLVVVR GLAEESQKKG
     EHDEAVLIFR LLVRRDQGLA GPMYRDTAPD LVWAADWVTC DQRGFAYTRL AINLKTHLKR
     PREEQLDVVK AACDDDCVRG GDRVDLWERY QGLHKKCGDR QTASLRGRQR SPLWDPKVED
     IHPPVETQKQ GSQGTLGEKG GRKLYYYNDA APGERRWSEA RSHNVEEVVI RERYSAGGWL
     GLHGESKLIM FILMLLLWEE VFDSGVEAAV PHCIMISPLD TSDKFFTTRR EGLPDRLATI
     GQYADRQLFS DVGQRYDRLR GVRSGWCDWN VFPKQQIMEI CVAFGGKRLS DLLKTLTNNL
     ADMDKGFPDV VLRRPKGADF GAGGSSSGGG RDERDWKART HFGLGWQGHG HGWEVEVVEV
     KSKGDTISKE QKAWLAELED IGVPAMVSRV VAENEAVPKK RSRSR
//
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