ID A0A0V0VDJ7_9BILA Unreviewed; 392 AA.
AC A0A0V0VDJ7;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 24-JAN-2024, entry version 19.
DE RecName: Full=Fanconi-associated nuclease {ECO:0000256|RuleBase:RU365033};
DE EC=3.1.4.1 {ECO:0000256|RuleBase:RU365033};
DE Flags: Fragment;
GN ORFNames=T09_8395 {ECO:0000313|EMBL:KRX61628.1};
OS Trichinella sp. T9.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=181606 {ECO:0000313|EMBL:KRX61628.1, ECO:0000313|Proteomes:UP000054681};
RN [1] {ECO:0000313|EMBL:KRX61628.1, ECO:0000313|Proteomes:UP000054681}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS409 {ECO:0000313|EMBL:KRX61628.1};
RA Korhonen P.K., Edoardo P., Giuseppe L.R., Gasser R.B.;
RT "Evolution of Trichinella species and genotypes.";
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
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|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.
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:KRX61628.1}.
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DR EMBL; JYDN01000046; KRX61628.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0V0VDJ7; -.
DR Proteomes; UP000054681; 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:0004528; F:phosphodiesterase I activity; IEA:UniProtKB-EC.
DR GO; GO:0036297; P:interstrand cross-link repair; IEA:InterPro.
DR InterPro; IPR033315; Fan1-like.
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.
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|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:UP000054681}.
FT DOMAIN 293..371
FT /note="VRR-NUC"
FT /evidence="ECO:0000259|Pfam:PF08774"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KRX61628.1"
SQ SEQUENCE 392 AA; 45820 MW; BEEFC0EC4766AD64 CRC64;
LENEMWNCWN SKKYTVCLHV GSRIRHLLDE ELRLLSEKPC SVRLVHYQNF TTVVSLLRAS
TVLAQAFEKL KMYDKANAEF EYLISINCQF VPAHRRSFWY ERAILNYGRH LKLPKKAYEL
ALDVIQDDTF DYYFRQRIYD RVLQMNLVGE DCEKQLATNI QAALDETIEI DVEIPEKVIS
APLLSKSMGT SVKTVFVVPQ EHQFSCPGVE AVALNYYYQK ENFSKGLHSE GSIWLALFGL
LCWNEIYDST VEDVWISRYQ TYPLDLYAGE MFWINRQKTF EKKFETLQCL SVQDIQSMLR
ASWREHEGIN SIVKWDAFES SEMFEEMLSC MDGHMLVKLF GRLASNFKRH SSGFPDLVVW
NVQSRDIKVF FLLIRILFSV IHYVGGGSQR TG
//
