FAN1_CAEBR
ID FAN1_CAEBR Reviewed; 878 AA.
AC A8WZU5;
DT 05-OCT-2010, integrated into UniProtKB/Swiss-Prot.
DT 16-DEC-2008, sequence version 2.
DT 03-AUG-2022, entry version 64.
DE RecName: Full=Fanconi-associated nuclease 1 homolog {ECO:0000305};
DE EC=3.1.4.1 {ECO:0000250|UniProtKB:Q9Y2M0};
GN Name=fan-1; ORFNames=CBG05421;
OS Caenorhabditis briggsae.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6238;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AF16;
RX PubMed=14624247; DOI=10.1371/journal.pbio.0000045;
RA Stein L.D., Bao Z., Blasiar D., Blumenthal T., Brent M.R., Chen N.,
RA Chinwalla A., Clarke L., Clee C., Coghlan A., Coulson A., D'Eustachio P.,
RA Fitch D.H.A., Fulton L.A., Fulton R.E., Griffiths-Jones S., Harris T.W.,
RA Hillier L.W., Kamath R., Kuwabara P.E., Mardis E.R., Marra M.A.,
RA Miner T.L., Minx P., Mullikin J.C., Plumb R.W., Rogers J., Schein J.E.,
RA Sohrmann M., Spieth J., Stajich J.E., Wei C., Willey D., Wilson R.K.,
RA Durbin R.M., Waterston R.H.;
RT "The genome sequence of Caenorhabditis briggsae: a platform for comparative
RT genomics.";
RL PLoS Biol. 1:166-192(2003).
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 -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9Y2M0}.
CC -!- SIMILARITY: Belongs to the FAN1 family. {ECO:0000305}.
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DR EMBL; HE601369; CAP25905.2; -; Genomic_DNA.
DR AlphaFoldDB; A8WZU5; -.
DR SMR; A8WZU5; -.
DR STRING; 6238.CBG05421; -.
DR PRIDE; A8WZU5; -.
DR WormBase; CBG05421; CBP07085; WBGene00027875; Cbr-fan-1.
DR eggNOG; KOG2143; Eukaryota.
DR HOGENOM; CLU_311526_0_0_1; -.
DR InParanoid; A8WZU5; -.
DR OMA; LEEHYMW; -.
DR OrthoDB; 1003565at2759; -.
DR Proteomes; UP000008549; Chromosome IV.
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:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004528; F:phosphodiesterase I activity; IEA:UniProtKB-EC.
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; IPR006642; Rad18_UBZ4.
DR InterPro; IPR011856; tRNA_endonuc-like_dom_sf.
DR InterPro; IPR014883; VRR_NUC.
DR PANTHER; PTHR15749; PTHR15749; 1.
DR Pfam; PF08774; VRR_NUC; 1.
DR SMART; SM00990; VRR_NUC; 1.
DR PROSITE; PS51908; ZF_UBZ4; 1.
PE 3: Inferred from homology;
KW DNA damage; DNA repair; Hydrolase; Magnesium; Manganese; Metal-binding;
KW Nuclease; Nucleus; Reference proteome; Zinc; Zinc-finger.
FT CHAIN 1..878
FT /note="Fanconi-associated nuclease 1 homolog"
FT /id="PRO_0000398621"
FT DOMAIN 757..870
FT /note="VRR-NUC"
FT ZN_FING 32..59
FT /note="UBZ4-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01256"
FT REGION 88..180
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 94..108
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 125..141
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 142..160
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 161..180
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 35
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01256"
FT BINDING 38
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01256"
FT BINDING 50
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01256"
FT BINDING 54
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01256"
FT BINDING 695
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q9I2N0"
FT BINDING 823
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q9I2N0"
FT BINDING 823
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q9I2N0"
FT BINDING 838
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q9I2N0"
FT BINDING 839
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q9I2N0"
SQ SEQUENCE 878 AA; 100613 MW; D16F0F264FB4BC9C CRC64;
MKKVKKEKVI GPVVPVSYNR SILAAFEKQA KGKTCPLCNI KFSLASYRSH MNVCKVADDD
DEIKVMASYT REEAILLRAG PEIVLGEENS GQEIPVNPKK KRRTGEEQLE STPNPPVVQA
FDFDVPGPST SSENLDPPSE SSEVRSVEKE IKKSPVWENR RRSTRLAQNS QKSQSESQEA
IVKKETATVL EVLASINNFE TRIANSDRPT PYYVKCTVKI LKKIISTMKS DGDFYADNFW
LPSDIITFYR FVECLSDGAK CLLVRLFVRK PNWYHLEKLE QKYTEILNIR GAAVELMKWE
FISDDSTLKT LNEALRISDI TVLKNVAKKF KIDGNKNRQD LVQSLRKFAL SQQSIFGGTG
SVELAVLKSL KTELGTCIKI KDEMVDLFKC LFTLYCPVTT NSANVIDNPA STNVYQDLLY
MMLSVENGSV EFPAPNPCPN IASFYKNRAM LMEYVTAKAL ESSLVLQMSN GDHDIALDLA
IDAKEFLDQM PLEQKKYYES LEIHERKFTS IWVHTRCCGH ATSVLEKQKK YGMAVEWQKD
LLITNKDVQS CCLDSRGMWW DRMLLNLDSH LKVSVFPSYS QTKKRFFQEK TECAKMIQIA
LTDSSILEKE LLSIQDRALK LKEMPPDFRP PLNIGTPMKR VITARTISKS LGDGRVNRFV
FRDEEKEEDV ECSVEEAARR WYIENDEFTT GVHDEGATWH TLFGLLFYDI IFCTDAVMAS
VWHSEVQDCP SDLSNTLYLK RKEKFEERFE WLKDADQETI EDNIRRIWGM KQNETNRECS
WKHFQSGIED CVSIFQCIPR PAMLSIFRRL AENYRNSRSG FPDLTLWNPE KKTVAVIEVK
GPGDRLSTKQ RLWLSFFADN GIKAEVCHVE AQNSRLLV
