ID A0A096M710_POEFO Unreviewed; 945 AA.
AC A0A096M710;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 24-JAN-2024, entry version 42.
DE RecName: Full=Fanconi-associated nuclease {ECO:0000256|RuleBase:RU365033};
DE EC=3.1.4.1 {ECO:0000256|RuleBase:RU365033};
OS Poecilia formosa (Amazon molly) (Limia formosa).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Cyprinodontiformes; Poeciliidae; Poeciliinae;
OC Poecilia.
OX NCBI_TaxID=48698 {ECO:0000313|Ensembl:ENSPFOP00000027201.1, ECO:0000313|Proteomes:UP000028760};
RN [1] {ECO:0000313|Proteomes:UP000028760}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=female {ECO:0000313|Proteomes:UP000028760};
RA Schartl M., Warren W.;
RL Submitted (OCT-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSPFOP00000027201.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) 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 EMBL; AYCK01018417; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; A0A096M710; -.
DR Ensembl; ENSPFOT00000025868.1; ENSPFOP00000027201.1; ENSPFOG00000004750.2.
DR GeneTree; ENSGT00390000018637; -.
DR OMA; ECRVESM; -.
DR Proteomes; UP000028760; Unassembled WGS sequence.
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 CDD; cd22326; FAN1-like; 1.
DR Gene3D; 3.40.1350.10; -; 1.
DR InterPro; IPR033315; Fan1-like.
DR InterPro; IPR049132; FAN1-like_euk.
DR InterPro; IPR049126; FAN1-like_TPR.
DR InterPro; IPR049125; FAN1-like_WH.
DR InterPro; IPR049138; Fan1_SAP_met.
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; PF21315; FAN1_HTH; 1.
DR Pfam; PF21169; Fan1_SAP; 1.
DR Pfam; PF21170; FAN1_TPR; 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:UP000028760}.
FT DOMAIN 817..932
FT /note="VRR-NUC"
FT /evidence="ECO:0000259|SMART:SM00990"
FT REGION 1..45
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 78..183
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 197..283
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 27..45
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 78..102
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 117..146
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 161..183
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 197..218
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 219..233
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 253..271
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 945 AA; 105699 MW; C355538E0F2CFB99 CRC64;
SMTERTSKDK PRRSLSLKKK KGDAKAGTSS TTKTPITNFF SSQPPPNLAC PLCGQLVPRF
KINDHIDLQC QNFDRGDSTA ASGGRNDYSG VQLSPGGNLS KSPETDQKED TKTKTSPYFK
KNNPQQTPRD INNKTVVRTI DLGSLSSKLS RKYHKKPAEV SNTSDPMSSA ESTSSSQKEN
VQTLEDNNDC ISAVTEAPSP VEKQSNQSMV SSKQSPSPAK QTKRKKKATF SVKGSLIRKK
AKYEGSGGEA SSCLDPEDTN TEGQGSDKPF NSELSEKSDA DVKVETSDAQ SLPYYLRNFR
TVLHAVLENE DDRKLFNQED MSAVHGFQSL SVMAQKLYVR LFQRKLKWLQ VNKLDYGEIC
SDLGSVAQEL AQIGFLQTEK DLEDLMEALD LLPAPELKAL AKTFHLGSSG TQKQQLVDGL
LRLSRQKSFF SPASSQSKVG TVILKRAKQL AGSCVRLSRG PRAVFSRILL LFSLTDTMDE
EEMAAGGQNQ LFTILLVNSG RLAFPDYAVQ REAKVFRDRE DLIRYEASMR ALIEVTVAMQ
GGQWDQALQL YTSAKKTWIE LSSNHDLSHQ EELPVFLRSF TTGWAYTRIL SRGVEILQRL
RRYEDAVEEL QALLKQSVYC PDSRGRWWDR LALNFHQHLK KPDQAICAMR DGLSDPLVRT
GHKLSLHQRA LRMKDSPSCK KYRLQLRELP AVQIQDVKHV TIRGQLFPHE GGMGKSRFLL
PETEEGDGSA HSTVICSVEE LSLAHYRQLG FDQGIHGEGS TFSTLFGLLM WDIIFMEGIP
DVFRNPYQTC PLDLYTDCFY ENRREAITSR VQLLCEASVE TLSAMLEDVW TSQEGKVCSL
VSWERMQCMV SLQSLIACLG GAFLGGVTDR MAKDYRHCRG GLPDLVVWNT SNNTYKLVEV
KGPNDRLSQK QQIWLDELQK LGADVEVCHV TATGARGARL EEISK
//
