EX7L_CAUVN
ID EX7L_CAUVN Reviewed; 505 AA.
AC B8GYM1;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 03-MAR-2009, sequence version 1.
DT 03-AUG-2022, entry version 77.
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=CCNA_02329;
OS Caulobacter vibrioides (strain NA1000 / CB15N) (Caulobacter crescentus).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Caulobacterales;
OC Caulobacteraceae; Caulobacter.
OX NCBI_TaxID=565050;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NA1000 / CB15N;
RX PubMed=20472802; DOI=10.1128/jb.00255-10;
RA Marks M.E., Castro-Rojas C.M., Teiling C., Du L., Kapatral V.,
RA Walunas T.L., Crosson S.;
RT "The genetic basis of laboratory adaptation in Caulobacter crescentus.";
RL J. Bacteriol. 192:3678-3688(2010).
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; CP001340; ACL95794.1; -; Genomic_DNA.
DR RefSeq; WP_010920107.1; NC_011916.1.
DR RefSeq; YP_002517702.1; NC_011916.1.
DR AlphaFoldDB; B8GYM1; -.
DR PRIDE; B8GYM1; -.
DR EnsemblBacteria; ACL95794; ACL95794; CCNA_02329.
DR GeneID; 7332283; -.
DR KEGG; ccs:CCNA_02329; -.
DR PATRIC; fig|565050.3.peg.2281; -.
DR HOGENOM; CLU_023625_3_1_5; -.
DR OMA; LVWPVKV; -.
DR OrthoDB; 1371775at2; -.
DR PhylomeDB; B8GYM1; -.
DR Proteomes; UP000001364; 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; Reference proteome.
FT CHAIN 1..505
FT /note="Exodeoxyribonuclease 7 large subunit"
FT /id="PRO_1000200664"
FT REGION 466..505
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 481..497
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 505 AA; 54443 MW; C14873CAE227CC02 CRC64;
MSDLPPTDSN APPYSVSELA FALKRTLEDR YGFVRLRGEL SKVTHHSNGH VYLTIKDDKS
AIDGVVWKGN VRGLGVRPEH GLEVIVTGKI TTYPAGSRYQ IVIDSMEAAG VGALLAQLER
LKAKLAAEGL FAPERKRPLP SMPAVVGVIT SPTGAVIRDI LHRIRDRWPC QVLVWPCVVQ
GDAAAGQVSA AIRGFNAIQP GGPVPRPDVL IVARGGGSVE DLWAFNDEGL ARTVAEGTIP
LISAVGHETD TTLIDFVSDR RAPTPTAAAE MATPVLAELR ALISDLDRRL NRCGARTIEE
RRTRLVSAAR GLPRPNDLLA LAQQRFDIAS GRLDAALDRN TTVHAQSLLK VTARLTPEAL
GRQRAVKAER LADLSRRLDL AARRAPDRVA QHARLPALWD RLNAAGQRRL QRDADRLENL
EKLRQSLNPE RPLELGFALV RKGDGTLARS AADLVSGERV NLKFKSGDRD AVIDGEGGPA
PAPTAPAPKP RPKPAAPPAG QGDLF
