EX7L_SALRD
ID EX7L_SALRD Reviewed; 398 AA.
AC Q2S4K5;
DT 23-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 24-JAN-2006, sequence version 1.
DT 25-MAY-2022, entry version 91.
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=SRU_0738;
OS Salinibacter ruber (strain DSM 13855 / M31).
OC Bacteria; Bacteroidetes; Bacteroidetes Order II. Incertae sedis;
OC Rhodothermaceae; Salinibacter.
OX NCBI_TaxID=309807;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 13855 / CECT 5946 / M31;
RX PubMed=16330755; DOI=10.1073/pnas.0509073102;
RA Mongodin E.F., Nelson K.E., Daugherty S., DeBoy R.T., Wister J., Khouri H.,
RA Weidman J., Walsh D.A., Papke R.T., Sanchez Perez G., Sharma A.K.,
RA Nesbo C.L., MacLeod D., Bapteste E., Doolittle W.F., Charlebois R.L.,
RA Legault B., Rodriguez-Valera F.;
RT "The genome of Salinibacter ruber: convergence and gene exchange among
RT hyperhalophilic bacteria and archaea.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:18147-18152(2005).
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; CP000159; ABC44451.1; -; Genomic_DNA.
DR RefSeq; YP_444876.1; NC_007677.1.
DR AlphaFoldDB; Q2S4K5; -.
DR STRING; 309807.SRU_0738; -.
DR EnsemblBacteria; ABC44451; ABC44451; SRU_0738.
DR KEGG; sru:SRU_0738; -.
DR PATRIC; fig|309807.25.peg.758; -.
DR eggNOG; COG1570; Bacteria.
DR HOGENOM; CLU_023625_2_0_10; -.
DR OMA; WPAVRFE; -.
DR Proteomes; UP000008674; 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; 2.
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..398
FT /note="Exodeoxyribonuclease 7 large subunit"
FT /id="PRO_0000273681"
SQ SEQUENCE 398 AA; 43905 MW; 35644E4736BC64B3 CRC64;
MLSVAELTRG LSDLVEDRYD DVWVEGELSD FTRAASGHCY FSLKDEDAQI RCVMWKHLTQ
YVYFEPEEGM QVRVNGHASV YERRGDLQIQ AQAMRQAGKG AQQKAFEELK QTLQAEGLFA
PERKQALPAF PDTIGVVTSG QGAAIHDIQS GLARRFPPAE VVLCPVKVQG LDAPRAVADA
VAAFNDLPAD DAQRPDLLIV GRGGGSTEDL WAFNEEVVAR ALDASNLPVV SAVGHESDVT
IADLVADERA ATPSAAAERV VPDRRDVADR VRALHDRLRS RVTGRLQDAR QRVDALVASR
AFHAPARRLE QHRQHLDALV DRLGRGGARA VDRARTRLAH LRDRLHALDP EQPLRRGYVH
LTQDGTSVQS AESLQDGDRV RLHFQDGRRD AEVLPDDG
