ID   EX7L_ANAMF              Reviewed;         397 AA.
AC   B9KHB8;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   24-MAR-2009, sequence version 1.
DT   25-MAY-2022, entry version 61.
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=AMF_1006;
OS   Anaplasma marginale (strain Florida).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC   Anaplasmataceae; Anaplasma.
OX   NCBI_TaxID=320483;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Florida;
RX   PubMed=19134224; DOI=10.1186/1471-2164-10-16;
RA   Dark M.J., Herndon D.R., Kappmeyer L.S., Gonzales M.P., Nordeen E.,
RA   Palmer G.H., Knowles D.P. Jr., Brayton K.A.;
RT   "Conservation in the face of diversity: multistrain analysis of an
RT   intracellular bacterium.";
RL   BMC Genomics 10:16-16(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}.
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DR   EMBL; CP001079; ACM49822.1; -; Genomic_DNA.
DR   AlphaFoldDB; B9KHB8; -.
DR   STRING; 320483.AMF_1006; -.
DR   EnsemblBacteria; ACM49822; ACM49822; AMF_1006.
DR   KEGG; amf:AMF_1006; -.
DR   eggNOG; COG1570; Bacteria.
DR   HOGENOM; CLU_023625_2_0_5; -.
DR   OMA; DFTIIDY; -.
DR   Proteomes; UP000007307; 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; 2.
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..397
FT                   /note="Exodeoxyribonuclease 7 large subunit"
FT                   /id="PRO_1000200656"
SQ   SEQUENCE   397 AA;  44109 MW;  8D1E13A4E52AC2C1 CRC64;
     MSLRSCSTEM IPEFTVTEIT DLVRQVMHDT FYCIKIRGEI SGLSRPSSGH VYLSLKDDNS
     VISAVCWHGT RLDVQFENGL EVICTGHIST YQSRYQLVIE GMVLAGQGKL AAMLEERRKK
     LEKEGLFDQA RKKPLPLLPL KIGVITSPTG AVIRDILNRV KHRFPSHIIV WPVQVQGSQA
     SAMVVQAILG FNNLEEPPDV IIVARGGGSI EDLWPFNDEE LARTAAASKI PIVSAIGHET
     DFTIIDYAAD VRAPTPTAAV EIVLPERQQL VSDIAHKLSK IRSAVRNVLG AKEHRLLQLY
     GVLTETKHKI SEVGRSALAH QEKIEFLFKV ALLKKQQYLD NLIGRIDRYN KEHIISVGYA
     VIYDNTGQHV SSANAVAPDD TIVIEWKDGK RRAAILT