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Database: UniProt
Entry: A0L6H7_MAGMM
LinkDB: A0L6H7_MAGMM
Original site: A0L6H7_MAGMM 
ID   A0L6H7_MAGMM            Unreviewed;       448 AA.
AC   A0L6H7;
DT   12-DEC-2006, integrated into UniProtKB/TrEMBL.
DT   12-DEC-2006, sequence version 1.
DT   27-MAR-2024, entry version 103.
DE   RecName: Full=Exodeoxyribonuclease 7 large subunit {ECO:0000256|HAMAP-Rule:MF_00378};
DE            EC=3.1.11.6 {ECO:0000256|HAMAP-Rule:MF_00378};
DE   AltName: Full=Exodeoxyribonuclease VII large subunit {ECO:0000256|HAMAP-Rule:MF_00378};
DE            Short=Exonuclease VII large subunit {ECO:0000256|HAMAP-Rule:MF_00378};
GN   Name=xseA {ECO:0000256|HAMAP-Rule:MF_00378};
GN   OrderedLocusNames=Mmc1_1052 {ECO:0000313|EMBL:ABK43570.1};
OS   Magnetococcus marinus (strain ATCC BAA-1437 / JCM 17883 / MC-1).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Magnetococcales;
OC   Magnetococcaceae; Magnetococcus.
OX   NCBI_TaxID=156889 {ECO:0000313|EMBL:ABK43570.1, ECO:0000313|Proteomes:UP000002586};
RN   [1] {ECO:0000313|Proteomes:UP000002586}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-1437 / JCM 17883 / MC-1
RC   {ECO:0000313|Proteomes:UP000002586};
RX   PubMed=19465526; DOI=10.1128/AEM.02874-08;
RA   Schubbe S., Williams T.J., Xie G., Kiss H.E., Brettin T.S., Martinez D.,
RA   Ross C.A., Schuler D., Cox B.L., Nealson K.H., Bazylinski D.A.;
RT   "Complete genome sequence of the chemolithoautotrophic marine magnetotactic
RT   coccus strain MC-1.";
RL   Appl. Environ. Microbiol. 75:4835-4852(2009).
RN   [2] {ECO:0000313|EMBL:ABK43570.1, ECO:0000313|Proteomes:UP000002586}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-1437 / JCM 17883 / MC-1
RC   {ECO:0000313|Proteomes:UP000002586};
RX   PubMed=22581902;
RA   Bazylinski D.A., Williams T.J., Lefevre C.T., Berg R.J., Zhang C.L.,
RA   Bowser S.S., Dean A.J., Beveridge T.J.;
RT   "Magnetococcus marinus gen. nov., sp. nov., a marine, magnetotactic
RT   bacterium that represents a novel lineage (Magnetococcaceae fam. nov.;
RT   Magnetococcales ord. nov.) at the base of the Alphaproteobacteria.";
RL   Int. J. Syst. Evol. Microbiol. 0:0-0(2012).
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:0000256|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:0000256|HAMAP-Rule:MF_00378,
CC         ECO:0000256|RuleBase:RU004355};
CC   -!- SUBUNIT: Heterooligomer composed of large and small subunits.
CC       {ECO:0000256|HAMAP-Rule:MF_00378}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00378,
CC       ECO:0000256|RuleBase:RU004355}.
CC   -!- SIMILARITY: Belongs to the XseA family. {ECO:0000256|HAMAP-
CC       Rule:MF_00378, ECO:0000256|RuleBase:RU004355}.
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DR   EMBL; CP000471; ABK43570.1; -; Genomic_DNA.
DR   RefSeq; WP_011712727.1; NC_008576.1.
DR   AlphaFoldDB; A0L6H7; -.
DR   STRING; 156889.Mmc1_1052; -.
DR   KEGG; mgm:Mmc1_1052; -.
DR   eggNOG; COG1570; Bacteria.
DR   HOGENOM; CLU_023625_3_1_5; -.
DR   OrthoDB; 9802795at2; -.
DR   Proteomes; UP000002586; 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   NCBIfam; TIGR00237; xseA; 1.
DR   PANTHER; PTHR30008; EXODEOXYRIBONUCLEASE 7 LARGE SUBUNIT; 1.
DR   PANTHER; PTHR30008:SF0; EXODEOXYRIBONUCLEASE 7 LARGE SUBUNIT; 1.
DR   Pfam; PF02601; Exonuc_VII_L; 1.
DR   Pfam; PF13742; tRNA_anti_2; 1.
PE   3: Inferred from homology;
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_00378};
KW   Exonuclease {ECO:0000256|ARBA:ARBA00022839, ECO:0000256|HAMAP-
KW   Rule:MF_00378};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|HAMAP-Rule:MF_00378};
KW   Nuclease {ECO:0000256|ARBA:ARBA00022722, ECO:0000256|HAMAP-Rule:MF_00378};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002586}.
FT   DOMAIN          13..105
FT                   /note="OB-fold nucleic acid binding"
FT                   /evidence="ECO:0000259|Pfam:PF13742"
FT   DOMAIN          129..441
FT                   /note="Exonuclease VII large subunit C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02601"
SQ   SEQUENCE   448 AA;  49905 MW;  F67F7C1EF3083140 CRC64;
     MYSNDTPSWK KVLSVFELNS AIRDLLEEGF AFVRVQGEVS RISAPASGHL YFNLVDEQAQ
     IRAVVWRASK ARLSHHPREG EEVLITGRIS VFAPRGEYQI IVDALTPKGA GSEREKLLQL
     HRQLEQEGLF DPQRKRPLPY LPHVIGVATS ESGAALQDII RVLESRNPDF HLLLAPCQVQ
     GSEAPQAIVQ ALRALNADGR AQVIICGRGG GSAEDLACFN SEQVVRAIAA SAIPVVSAVG
     HEVDTTLADL AADLRAATPS QAAELIMPER LALAQETTAL ALRLQRAMHQ QLHNQQRRVQ
     QASQRLLHPS RRLDQARLRC DELQMRLQGV LERLLPQQQQ RLRRATNTLH HWATGPSLPR
     QRQQLKQQQH RAHTAMLYQL RQWQSRLHSA QLQLIALSPL QVLERGYAIV RDNQGSVLRD
     AQAAPLESTL TITLAKGTLA ARVTQRKP
//
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