EX7L_PECCP
ID EX7L_PECCP Reviewed; 462 AA.
AC C6DBG5;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-SEP-2009, sequence version 1.
DT 25-MAY-2022, entry version 65.
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=PC1_3005;
OS Pectobacterium carotovorum subsp. carotovorum (strain PC1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Pectobacteriaceae; Pectobacterium.
OX NCBI_TaxID=561230;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PC1;
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Tice H., Bruce D.,
RA Goodwin L., Pitluck S., Munk A.C., Brettin T., Detter J.C., Han C.,
RA Tapia R., Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N.,
RA Balakrishnan V., Glasner J., Perna N.T.;
RT "Complete sequence of Pectobacterium carotovorum subsp. carotovorum PC1.";
RL Submitted (JUL-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; CP001657; ACT14028.1; -; Genomic_DNA.
DR RefSeq; WP_015841182.1; NC_012917.1.
DR AlphaFoldDB; C6DBG5; -.
DR SMR; C6DBG5; -.
DR STRING; 561230.PC1_3005; -.
DR EnsemblBacteria; ACT14028; ACT14028; PC1_3005.
DR KEGG; pct:PC1_3005; -.
DR eggNOG; COG1570; Bacteria.
DR HOGENOM; CLU_023625_3_1_6; -.
DR OMA; WPAVRFE; -.
DR OrthoDB; 1371775at2; -.
DR Proteomes; UP000002736; 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; 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..462
FT /note="Exodeoxyribonuclease 7 large subunit"
FT /id="PRO_1000205679"
SQ SEQUENCE 462 AA; 52436 MW; D5659F48D77B1C64 CRC64;
MSQFPSSAIF TVSRLNQTVR QLLEMEMGQI WLSGEISNLS QPSSGHWYFT LKDERAQVRC
AMFRTSNRRV TFRPQNGQQV LIRATITLYE PRGDYQLLAE SMQPAGDGLL QQQFEQLKQK
LAAEGLFDQQ FKQVLPSPAK QVGVITSASG AALHDILQVL QRRDPSLPVI VYPTSVQGAD
APLQIVRAIE LANQREECDV LIVGRGGGSL EDLWSFNDER VARAIFASRI PIVSAVGHET
DVTIADFVGD LRAPTPSAAA ELVSRNQLEL LRQIQSQRQR LEMAMDYYLA QRNREFTRLH
HRLQQQHPQL RLARQQAQLV KLRQRLDDAM QQQLRQTLRR SERLQQRLMQ QQPQTRIHRA
QQRLQQLSYQ MQSAVERQLN QNKQKLGIAC SRLEGVSPLA TLARGYNVTT APDGKVLKNV
TQITPGETLK TRLQDGWVES QVTTLVPNPS SVKKRRKPSS QS
