EX7L_NAUPA
ID EX7L_NAUPA Reviewed; 445 AA.
AC B9L5W5;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 24-MAR-2009, sequence version 1.
DT 25-MAY-2022, entry version 88.
DE RecName: Full=Exodeoxyribonuclease 7 large subunit {ECO:0000255|HAMAP-Rule:MF_00378};
DE EC=3.1.11.6 {ECO:0000255|HAMAP-Rule:MF_00378};
DE AltName: Full=Exodeoxyribonuclease VII large subunit {ECO:0000255|HAMAP-Rule:MF_00378};
DE Short=Exonuclease VII large subunit {ECO:0000255|HAMAP-Rule:MF_00378};
GN Name=xseA {ECO:0000255|HAMAP-Rule:MF_00378}; OrderedLocusNames=NAMH_1360;
OS Nautilia profundicola (strain ATCC BAA-1463 / DSM 18972 / AmH).
OC Bacteria; Proteobacteria; Epsilonproteobacteria; Nautiliales; Nautiliaceae;
OC Nautilia.
OX NCBI_TaxID=598659;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-1463 / DSM 18972 / AmH;
RX PubMed=19197347; DOI=10.1371/journal.pgen.1000362;
RA Campbell B.J., Smith J.L., Hanson T.E., Klotz M.G., Stein L.Y., Lee C.K.,
RA Wu D., Robinson J.M., Khouri H.M., Eisen J.A., Cary S.C.;
RT "Adaptations to submarine hydrothermal environments exemplified by the
RT genome of Nautilia profundicola.";
RL PLoS Genet. 5:E1000362-E1000362(2009).
CC -!- FUNCTION: Bidirectionally degrades single-stranded DNA into large acid-
CC insoluble oligonucleotides, which are then degraded further into small
CC acid-soluble oligonucleotides. {ECO:0000255|HAMAP-Rule:MF_00378}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Exonucleolytic cleavage in either 5'- to 3'- or 3'- to 5'-
CC direction to yield nucleoside 5'-phosphates.; EC=3.1.11.6;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00378};
CC -!- SUBUNIT: Heterooligomer composed of large and small subunits.
CC {ECO:0000255|HAMAP-Rule:MF_00378}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00378}.
CC -!- SIMILARITY: Belongs to the XseA family. {ECO:0000255|HAMAP-
CC Rule:MF_00378}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP001279; ACM93262.1; -; Genomic_DNA.
DR RefSeq; WP_015902314.1; NC_012115.1.
DR AlphaFoldDB; B9L5W5; -.
DR SMR; B9L5W5; -.
DR STRING; 598659.NAMH_1360; -.
DR EnsemblBacteria; ACM93262; ACM93262; NAMH_1360.
DR KEGG; nam:NAMH_1360; -.
DR eggNOG; COG1570; Bacteria.
DR HOGENOM; CLU_023625_2_0_7; -.
DR OMA; DFTIIDY; -.
DR OrthoDB; 1371775at2; -.
DR Proteomes; UP000000448; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0009318; C:exodeoxyribonuclease VII complex; IEA:InterPro.
DR GO; GO:0008855; F:exodeoxyribonuclease VII activity; IEA:UniProtKB-UniRule.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0006308; P:DNA catabolic process; IEA:UniProtKB-UniRule.
DR CDD; cd04489; ExoVII_LU_OBF; 1.
DR HAMAP; MF_00378; Exonuc_7_L; 1.
DR InterPro; IPR003753; Exonuc_VII_L.
DR InterPro; IPR020579; Exonuc_VII_lsu_C.
DR InterPro; IPR025824; OB-fold_nuc-bd_dom.
DR PANTHER; PTHR30008; PTHR30008; 1.
DR Pfam; PF02601; Exonuc_VII_L; 1.
DR Pfam; PF13742; tRNA_anti_2; 1.
DR TIGRFAMs; TIGR00237; xseA; 1.
PE 3: Inferred from homology;
KW Cytoplasm; Exonuclease; Hydrolase; Nuclease; Reference proteome.
FT CHAIN 1..445
FT /note="Exodeoxyribonuclease 7 large subunit"
FT /id="PRO_1000200675"
SQ SEQUENCE 445 AA; 50410 MW; A1D14B60F0C66B87 CRC64;
MTPISVTQLN NQIKSIVESH FEIVLVEGEI SKVVYHSSGH LYFTLKDENS SINCAMWKSN
LTRMKFRLKE GEKVYVYGAL SVYVPRGEYK IIAQSIEPSG VGALQKAFEQ LKEELSKLGY
FDEARKKSIP RFPRRIAIVT SATGAALQDM LRVAGKRWQL TEIYLFNALV QGDGAAEDIA
MKIKLADEFV FEDGSGFDLI IIGRGGGSKE DLWPFNERVV ADAVYNASTP IISAVGHEID
YLISDFVADV RAATPSNAME IALPDKNEIL LMLDEMKNAF VYKISHLIQK KERELIHIRE
LLNASSPVKK LDMKLQECEL LLKRFNHSYI NQIQKKEKEL NELKNILFSL SPVIKINSFE
KEIELLKSTF KNKTAQIISS KEKELINLKS AYETLNPKKR EKKGFAEITK NGKRIDLKEL
KIGDIFDVSN ADVLIKSKAL EKIEN
