EX7L_COREF
ID EX7L_COREF Reviewed; 413 AA.
AC Q8FQP1;
DT 06-JUN-2003, integrated into UniProtKB/Swiss-Prot.
DT 16-JUN-2003, sequence version 2.
DT 25-MAY-2022, entry version 101.
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=CE1078;
OS Corynebacterium efficiens (strain DSM 44549 / YS-314 / AJ 12310 / JCM 11189
OS / NBRC 100395).
OC Bacteria; Actinobacteria; Corynebacteriales; Corynebacteriaceae;
OC Corynebacterium.
OX NCBI_TaxID=196164;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 44549 / YS-314 / AJ 12310 / JCM 11189 / NBRC 100395;
RX PubMed=12840036; DOI=10.1101/gr.1285603;
RA Nishio Y., Nakamura Y., Kawarabayasi Y., Usuda Y., Kimura E., Sugimoto S.,
RA Matsui K., Yamagishi A., Kikuchi H., Ikeo K., Gojobori T.;
RT "Comparative complete genome sequence analysis of the amino acid
RT replacements responsible for the thermostability of Corynebacterium
RT efficiens.";
RL Genome Res. 13:1572-1579(2003).
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 -!- SEQUENCE CAUTION:
CC Sequence=BAC17888.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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; BA000035; BAC17888.1; ALT_INIT; Genomic_DNA.
DR RefSeq; WP_035109867.1; NZ_GG700688.1.
DR AlphaFoldDB; Q8FQP1; -.
DR STRING; 196164.23492916; -.
DR EnsemblBacteria; BAC17888; BAC17888; BAC17888.
DR KEGG; cef:CE1078; -.
DR eggNOG; COG1570; Bacteria.
DR HOGENOM; CLU_023625_2_1_11; -.
DR OrthoDB; 1371775at2; -.
DR Proteomes; UP000001409; 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..413
FT /note="Exodeoxyribonuclease 7 large subunit"
FT /id="PRO_0000197842"
SQ SEQUENCE 413 AA; 45172 MW; D3BABD9687C6EE5D CRC64;
MPSAKSTPDT PWPVRDVNNQ VKNWIERLGH LWVEGQLAQI NVKPNWKLSY LTLRDVEQEV
SVQLTCPTEI IRNRPTPLKD GDRVIVYGKP AFYAGRGSFS LWVTDIRPVG IGQLLARIEE
LRRQLAAEGL FDPARKKRLP FLPKCVGLIT GRGSAAERDV LSVARDRWPE VQFKVINTAV
QGASAVPEII AALGELDQDP GVDVIIIARG GGSVEDLLPF SEEALQRAVA AAQTPVVSAI
GHEPDTPILD NVADLRAATP TDAAKRVVPD VNEERLLIRQ LRDRGAAALR GWVAREQQAL
ASIRTRPVLA DPMTPIVRRR EEVERAVSLL RRDVNHMLRT EQSLVASLRA QVSALGPSAT
LARGYSVVQV VPRDGTPPQV VTTIEQTPPG SQLRIRVADG AITAAAMNTQ KSD
