EX7L_CERSK
ID EX7L_CERSK Reviewed; 519 AA.
AC B9KM14;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 24-MAR-2009, sequence version 1.
DT 25-MAY-2022, entry version 67.
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};
GN OrderedLocusNames=RSKD131_0152;
OS Cereibacter sphaeroides (strain KD131 / KCTC 12085) (Rhodobacter
OS sphaeroides).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC Rhodobacteraceae; Cereibacter.
OX NCBI_TaxID=557760;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KD131 / KCTC 12085;
RX PubMed=19028901; DOI=10.1128/jb.01565-08;
RA Lim S.-K., Kim S.J., Cha S.H., Oh Y.-K., Rhee H.-J., Kim M.-S., Lee J.K.;
RT "Complete genome sequence of Rhodobacter sphaeroides KD131.";
RL J. Bacteriol. 191:1118-1119(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; CP001150; ACM00012.1; -; Genomic_DNA.
DR RefSeq; WP_012643513.1; NC_011963.1.
DR AlphaFoldDB; B9KM14; -.
DR SMR; B9KM14; -.
DR PRIDE; B9KM14; -.
DR EnsemblBacteria; ACM00012; ACM00012; RSKD131_0152.
DR GeneID; 67445634; -.
DR KEGG; rsk:RSKD131_0152; -.
DR HOGENOM; CLU_023625_3_1_5; -.
DR OMA; LVWPVKV; -.
DR Proteomes; UP000001597; Chromosome 1.
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.
FT CHAIN 1..519
FT /note="Exodeoxyribonuclease 7 large subunit"
FT /id="PRO_1000200677"
FT REGION 500..519
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 519 AA; 56321 MW; CB2D8677E53FA4CB CRC64;
MSDLFEDPAP SRNTPEFTVS ELSGAVKRVI EGEFGLVRVR GEIGRVSRPA SGHLYFDLKD
DRAVMAAICW KGQAGRLSVR PEEGMEVVAT GRMTTFPGQS KYQIIVEDMA PAGAGALMAM
LEKRRAALAA EGLFDAARKR PLPYLPRVIG VVTSPSGAVI RDILHRLRDR FPSHVLIWPV
AVQGEKCAPE VAAAIRGFNA LPEGGPIPRP DLLIVARGGG SLEDLWGFNE EIVVRAAAES
RIPLISAVGH ETDTTLIDHA ADRRAPTPTA AAEMAVPVRL ELLAGLDGQG ARLSRCAAET
IRRRDQRLRD LARALPRLES LVAGPSQRFD LWSGRLSGAL GQSVAARRAR LEPLGAHLRP
RLLADLVARQ KDRLGDRTRS LETCLGRRAE RARDRFEALS ARLAPAFARL IAETERATRR
DAATLGTLAA RLDAAPEARL ARLSDRLEAL DRLRQTLGYR ETLKRGYAVV RADGAVVTTK
AEAGTAAVLE IEFQDGRLSV GRGKTRKPKE EPPAQGSLL
