EX7L_RUMCH
ID EX7L_RUMCH Reviewed; 404 AA.
AC B8I3A9;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 03-MAR-2009, sequence version 1.
DT 03-AUG-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}; OrderedLocusNames=Ccel_1904;
OS Ruminiclostridium cellulolyticum (strain ATCC 35319 / DSM 5812 / JCM 6584 /
OS H10) (Clostridium cellulolyticum).
OC Bacteria; Firmicutes; Clostridia; Eubacteriales; Oscillospiraceae;
OC Ruminiclostridium.
OX NCBI_TaxID=394503;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35319 / DSM 5812 / JCM 6584 / H10;
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Chertkov O., Saunders E., Brettin T.,
RA Detter J.C., Han C., Larimer F., Land M., Hauser L., Kyrpides N.,
RA Ivanova N., Zhou J., Richardson P.;
RT "Complete sequence of Clostridium cellulolyticum H10.";
RL Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases.
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; CP001348; ACL76252.1; -; Genomic_DNA.
DR RefSeq; WP_015925357.1; NC_011898.1.
DR AlphaFoldDB; B8I3A9; -.
DR STRING; 394503.Ccel_1904; -.
DR PRIDE; B8I3A9; -.
DR EnsemblBacteria; ACL76252; ACL76252; Ccel_1904.
DR KEGG; cce:Ccel_1904; -.
DR eggNOG; COG1570; Bacteria.
DR HOGENOM; CLU_023625_3_1_9; -.
DR OMA; WPAVRFE; -.
DR OrthoDB; 1371775at2; -.
DR Proteomes; UP000001349; 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 InterPro; IPR016102; Succinyl-CoA_synth-like.
DR PANTHER; PTHR30008; PTHR30008; 2.
DR Pfam; PF02601; Exonuc_VII_L; 2.
DR Pfam; PF13742; tRNA_anti_2; 1.
DR SUPFAM; SSF52210; SSF52210; 1.
DR TIGRFAMs; TIGR00237; xseA; 1.
PE 3: Inferred from homology;
KW Cytoplasm; Exonuclease; Hydrolase; Nuclease; Reference proteome.
FT CHAIN 1..404
FT /note="Exodeoxyribonuclease 7 large subunit"
FT /id="PRO_1000200666"
SQ SEQUENCE 404 AA; 45244 MW; B78F64A325010DDE CRC64;
MNRVYSVSDI NNYIKQLVSN DIILSDVSIR GEISNFKHHY TGHMYFTIKD KNSLLKCVMF
RSQAVSLRFS PENGMKVIVS GYISVFERDG QYQLYASSMQ PDGVGALHIA FEQLKEKLQR
EGLFDPENKK KIPVLPGSIG VVTSSTGAVI RDIINVTYRR NSKMKLVLYP VAVQGQQAAG
QIAEAIKCLN EQNKVDVIIV ARGGGSLEEL WAFNEEIVAR SIYASNIPVI SAVGHETDFT
ICDFVSDMRA PTPSAAAELA VPDMEVLLYK LESYNMRMKS SLAKKVTTLK NQLQKLNARP
FFAQPYDRVN QQRQTLDNLT KSMVRENQTI IKDKKSQFGM LAGKLDALSP LKILERGYSL
VKNPQGYVVN NVKQINIGDK LEILMNDGLA ECDVISVREG KIYE
