EXO5_BOVIN
ID EXO5_BOVIN Reviewed; 370 AA.
AC A2VDX7; F1MR90;
DT 23-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT 06-MAR-2013, sequence version 2.
DT 03-AUG-2022, entry version 74.
DE RecName: Full=Exonuclease V;
DE Short=Exo V;
DE EC=3.1.-.-;
DE AltName: Full=Defects in morphology protein 1 homolog;
GN Name=EXO5; Synonyms=DEM1;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Hereford;
RX PubMed=19393038; DOI=10.1186/gb-2009-10-4-r42;
RA Zimin A.V., Delcher A.L., Florea L., Kelley D.R., Schatz M.C., Puiu D.,
RA Hanrahan F., Pertea G., Van Tassell C.P., Sonstegard T.S., Marcais G.,
RA Roberts M., Subramanian P., Yorke J.A., Salzberg S.L.;
RT "A whole-genome assembly of the domestic cow, Bos taurus.";
RL Genome Biol. 10:R42.01-R42.10(2009).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Fetal lung;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (FEB-2007) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Single-stranded DNA (ssDNA) bidirectional exonuclease
CC involved in DNA repair. Probably involved in DNA repair following
CC ultraviolet (UV) irradiation and interstrand cross-links (ICLs) damage.
CC Has both 5'-3' and 3'-5' exonuclease activities with a strong
CC preference for 5'-ends. Acts as a sliding exonuclease that loads at
CC ssDNA ends and then slides along the ssDNA prior to cutting; however
CC the sliding and the 3'-5' exonuclease activities are abolished upon
CC binding to the replication protein A (RPA) complex that enforces 5'-
CC directionality activity (By similarity). {ECO:0000250}.
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000250|UniProtKB:Q9H790};
CC Note=Binds 1 [4Fe-4S] cluster. {ECO:0000250|UniProtKB:Q9H790};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:P38289};
CC -!- SUBUNIT: Monomer; monomeric form has weak exonuclease activity.
CC Homodimer; homodimeric form is unsure but has much higher exonuclease
CC activity, suggesting that it could homodimerize upon DNA-binding.
CC Interacts with the replication protein A (RPA) complex (By similarity).
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Cytoplasm, cytosol
CC {ECO:0000250}. Note=Localizes to repair foci in response to DNA damage.
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the EXO5 family. {ECO:0000305}.
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DR EMBL; DAAA02009128; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC133457; AAI33458.1; -; mRNA.
DR RefSeq; NP_001075077.1; NM_001081608.2.
DR RefSeq; XP_005204866.1; XM_005204809.3.
DR RefSeq; XP_005204867.1; XM_005204810.3.
DR AlphaFoldDB; A2VDX7; -.
DR SMR; A2VDX7; -.
DR STRING; 9913.ENSBTAP00000000690; -.
DR PaxDb; A2VDX7; -.
DR PRIDE; A2VDX7; -.
DR Ensembl; ENSBTAT00000000690; ENSBTAP00000000690; ENSBTAG00000000532.
DR GeneID; 538883; -.
DR KEGG; bta:538883; -.
DR CTD; 64789; -.
DR VEuPathDB; HostDB:ENSBTAG00000000532; -.
DR VGNC; VGNC:59180; EXO5.
DR eggNOG; KOG4760; Eukaryota.
DR GeneTree; ENSGT00390000015205; -.
DR HOGENOM; CLU_013225_0_2_1; -.
DR InParanoid; A2VDX7; -.
DR OMA; STQNWCE; -.
DR OrthoDB; 1601909at2759; -.
DR TreeFam; TF332529; -.
DR Proteomes; UP000009136; Chromosome 3.
DR Bgee; ENSBTAG00000000532; Expressed in oocyte and 107 other tissues.
DR GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; ISS:UniProtKB.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0045145; F:single-stranded DNA 5'-3' exodeoxyribonuclease activity; ISS:UniProtKB.
DR GO; GO:0036297; P:interstrand cross-link repair; ISS:UniProtKB.
DR Gene3D; 3.90.320.10; -; 1.
DR InterPro; IPR019190; EXOV.
DR InterPro; IPR011604; PDDEXK-like_dom_sf.
DR PANTHER; PTHR14464; PTHR14464; 1.
DR Pfam; PF09810; Exo5; 3.
PE 2: Evidence at transcript level;
KW 4Fe-4S; Cytoplasm; DNA damage; DNA repair; DNA-binding; Exonuclease;
KW Hydrolase; Iron; Iron-sulfur; Magnesium; Metal-binding; Nuclease; Nucleus;
KW Reference proteome.
FT CHAIN 1..370
FT /note="Exonuclease V"
FT /id="PRO_0000307319"
FT REGION 1..52
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 89
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250"
FT BINDING 340
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250"
FT BINDING 343
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250"
FT BINDING 349
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250"
FT CONFLICT 242
FT /note="D -> Y (in Ref. 2; AAI33458)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 370 AA; 41511 MW; FA12C11C97F4D5C7 CRC64;
MAETEEEETV SEEASGFSDL SDSELLDLED TQESSASASK PGPSYELPGK DDKLIRSPKW
KRRLDVSSPM ERFHLKYLYV TDLSTQNWCE QQMVYGKEFS GFLTPEKSAI LDTGASIHLA
RELEVHDLVS IPITSKEDAW AVKFLNILSM IPTLQSEGRI REFPVFAEVE GVLLVGVIDE
LHYTASGELE LTELKTRGNP VLPSDAQKKK DYFQVSLYKY IFDAMVQGKV TAASLIHHTK
LDPEKPLGPS VLRHAQQGGY SVKSLGDLIE LVFLSLTLSD LPLIDSLKIE YVHQGTATVL
GTEMVAFAEK EVRSKVQHYM TYWMGHREPQ GVDVEEAWKC RMCNYADICE WKKSGGLISA
TLEPQVKKAK
