LOCUS WP_031039417 259 aa linear BCT 13-DEC-2021
DEFINITION MULTISPECIES: exodeoxyribonuclease III [Streptomyces].
ACCESSION WP_031039417
VERSION WP_031039417.1
KEYWORDS RefSeq.
SOURCE Streptomyces
ORGANISM Streptomyces
Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
Streptomycetaceae.
REFERENCE 1 (residues 1 to 259)
AUTHORS Mathieu,A., O'Rourke,E.J. and Radicella,J.P.
TITLE Helicobacter pylori genes involved in avoidance of mutations
induced by 8-oxoguanine
JOURNAL J Bacteriol 188 (21), 7464-7469 (2006)
PUBMED 16936028
REFERENCE 2 (residues 1 to 259)
AUTHORS Georg,J., Schomacher,L., Chong,J.P., Majernik,A.I., Raabe,M.,
Urlaub,H., Muller,S., Ciirdaeva,E., Kramer,W. and Fritz,H.J.
TITLE The Methanothermobacter thermautotrophicus ExoIII homologue Mth212
is a DNA uridine endonuclease
JOURNAL Nucleic Acids Res 34 (18), 5325-5336 (2006)
PUBMED 17012282
REFERENCE 3 (residues 1 to 259)
AUTHORS Shida,T., Ogawa,T., Ogasawara,N. and Sekiguchi,J.
TITLE Characterization of Bacillus subtilis ExoA protein: a
multifunctional DNA-repair enzyme similar to the Escherichia coli
exonuclease III
JOURNAL Biosci Biotechnol Biochem 63 (9), 1528-1534 (1999)
PUBMED 10540738
COMMENT REFSEQ: This record represents a single, non-redundant, protein
sequence which may be annotated on many different RefSeq genomes
from the same, or different, species.
##Evidence-For-Name-Assignment-START##
Evidence Category :: HMM
Evidence Accession :: TIGR00633.1
Evidence Source :: JCVI
##Evidence-For-Name-Assignment-END##
COMPLETENESS: full length.
FEATURES Location/Qualifiers
source 1..259
/organism="Streptomyces"
/db_xref="taxon:1883"
Protein 1..259
/product="exodeoxyribonuclease III"
/calculated_mol_wt=28211
Region 1..257
/region_name="ExoIII-like_AP-endo"
/note="Escherichia coli exonuclease III (ExoIII) and
Neisseria meningitides NExo-like subfamily of the ExoIII
family purinic/apyrimidinic (AP) endonucleases; cd09086"
/db_xref="CDD:197320"
Site order(7,34,108,111,149,151,250)
/site_type="other"
/note="putative phosphate binding site [ion binding]"
/db_xref="CDD:197320"
Site order(7,34,108,149,151,220,249..250)
/site_type="active"
/note="putative catalytic site [active]"
/db_xref="CDD:197320"
Site order(9..10,12..14,34,60..61,108,111,113,119,149,151,203,
206..207,217,219..220,246..247,250)
/site_type="active"
/db_xref="CDD:197320"
Site order(9,34,249..250)
/site_type="metal-binding"
/note="metal binding site A [ion binding]"
/db_xref="CDD:197320"
Site order(9..10,12..14,60..61,108,111,113,119,206..207,
246..247)
/site_type="DNA binding"
/note="DNA binding site [nucleotide binding]"
/db_xref="CDD:197320"
Site order(108,111,149,151,203,217,219,250)
/site_type="other"
/note="putative AP binding site [nucleotide binding]"
/db_xref="CDD:197320"
Site order(108,149,151,250)
/site_type="other"
/note="putative metal binding site B [ion binding]"
/db_xref="CDD:197320"
ORIGIN
1 mriatwnvns itarlprlla wlestgtdvl clqeakvaee qfpfdqlrea gyeaavhatg
61 rwngvavisr vgledvvkgl pgdpgydgap epraisatcg parvwsvyvp ngrevdhphy
121 ayklqwfeal kaavagdaag srpfavlgdy nvaptdddvf dvaafeglth vtpaeraala
181 alreaglsdv vprplkydhp ftywdyrqlg fpknrgmrid lvygnesfak avtdayvdre
241 erkgkgasdh apvvvdldv
//