ID A4G9G4_HERAR Unreviewed; 147 AA.
AC A4G9G4;
DT 17-APR-2007, integrated into UniProtKB/TrEMBL.
DT 17-APR-2007, sequence version 1.
DT 27-MAR-2024, entry version 78.
DE SubName: Full=Thermonuclease {ECO:0000313|EMBL:CAL63151.1};
DE EC=3.1.31.1 {ECO:0000313|EMBL:CAL63151.1};
GN OrderedLocusNames=HEAR3042 {ECO:0000313|EMBL:CAL63151.1};
OS Herminiimonas arsenicoxydans.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Oxalobacteraceae; Herminiimonas.
OX NCBI_TaxID=204773 {ECO:0000313|EMBL:CAL63151.1, ECO:0000313|Proteomes:UP000006697};
RN [1] {ECO:0000313|EMBL:CAL63151.1, ECO:0000313|Proteomes:UP000006697}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ULPAs1 {ECO:0000313|Proteomes:UP000006697};
RX PubMed=17432936; DOI=10.1371/journal.pgen.0030053;
RA Muller D., Medigue C., Koechler S., Barbe V., Barakat M., Talla E.,
RA Bonnefoy V., Krin E., Arsene-Ploetze F., Carapito C., Chandler M.,
RA Cournoyer B., Cruveiller S., Dossat C., Duval S., Heymann M., Leize E.,
RA Lieutaud A., Lievremont D., Makita Y., Mangenot S., Nitschke W., Ortet P.,
RA Perdrial N., Schoepp B., Siguier N., Simeonova D.D., Rouy Z., Segurens B.,
RA Turlin E., Vallenet D., Van Dorsselaer A., Weiss S., Weissenbach J.,
RA Lett M.C., Danchin A., Bertin P.N.;
RT "A tale of two oxidation states: bacterial colonization of arsenic-rich
RT environments.";
RL PLoS Genet. 3:518-530(2007).
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DR EMBL; CU207211; CAL63151.1; -; Genomic_DNA.
DR AlphaFoldDB; A4G9G4; -.
DR STRING; 204773.HEAR3042; -.
DR KEGG; har:HEAR3042; -.
DR eggNOG; COG1525; Bacteria.
DR HOGENOM; CLU_046484_7_0_4; -.
DR OrthoDB; 9805504at2; -.
DR Proteomes; UP000006697; Chromosome.
DR GO; GO:0016894; F:endonuclease activity, active with either ribo- or deoxyribonucleic acids and producing 3'-phosphomonoesters; IEA:UniProtKB-EC.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR Gene3D; 2.40.50.90; -; 1.
DR InterPro; IPR035437; SNase_OB-fold_sf.
DR InterPro; IPR016071; Staphylococal_nuclease_OB-fold.
DR InterPro; IPR002071; Thermonucl_AS.
DR PANTHER; PTHR12302; EBNA2 BINDING PROTEIN P100; 1.
DR PANTHER; PTHR12302:SF3; ENDONUCLEASE LCL3-RELATED; 1.
DR Pfam; PF00565; SNase; 1.
DR SMART; SM00318; SNc; 1.
DR SUPFAM; SSF50199; Staphylococcal nuclease; 1.
DR PROSITE; PS01123; TNASE_1; 1.
DR PROSITE; PS50830; TNASE_3; 1.
PE 4: Predicted;
KW Hydrolase {ECO:0000313|EMBL:CAL63151.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000006697};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..18
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 19..147
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002669166"
FT DOMAIN 21..135
FT /note="TNase-like"
FT /evidence="ECO:0000259|PROSITE:PS50830"
SQ SEQUENCE 147 AA; 16223 MW; 15CFA358EC9C9D92 CRC64;
MRLALLALTS LLTLPAHAHQ VIGIADGDTL TLLVDKKPVK IRLANIDAPE KKQPFGQKSK
QSLSSLCWGK NAEYVTQAID RYKRTVAVVY CDGAQVNAAQ VKLGMAWVYP KYNKDAALPA
MEQAARLTGL GLWADVAPVP PWEWRRK
//
