ID A0A250VAM2_STROL Unreviewed; 85 AA.
AC A0A250VAM2;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 24-JAN-2024, entry version 24.
DE RecName: Full=Exodeoxyribonuclease 7 small subunit {ECO:0000256|HAMAP-Rule:MF_00337};
DE EC=3.1.11.6 {ECO:0000256|HAMAP-Rule:MF_00337};
DE AltName: Full=Exodeoxyribonuclease VII small subunit {ECO:0000256|HAMAP-Rule:MF_00337};
DE Short=Exonuclease VII small subunit {ECO:0000256|HAMAP-Rule:MF_00337};
GN Name=xseB {ECO:0000256|HAMAP-Rule:MF_00337,
GN ECO:0000313|EMBL:GAX51086.1};
GN ORFNames=SO3561_02585 {ECO:0000313|EMBL:GAX51086.1};
OS Streptomyces olivochromogenes.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1963 {ECO:0000313|EMBL:GAX51086.1, ECO:0000313|Proteomes:UP000217446};
RN [1] {ECO:0000313|Proteomes:UP000217446}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NBRC 3561 {ECO:0000313|Proteomes:UP000217446};
RA Dohra H., Kodani S.;
RT "Streptomyces olivochromogenes NBRC 3561 whole genome shotgun sequence.";
RL Submitted (MAY-2017) 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:0000256|HAMAP-Rule:MF_00337}.
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:0000256|HAMAP-Rule:MF_00337};
CC -!- SUBUNIT: Heterooligomer composed of large and small subunits.
CC {ECO:0000256|HAMAP-Rule:MF_00337}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00337}.
CC -!- SIMILARITY: Belongs to the XseB family. {ECO:0000256|ARBA:ARBA00009998,
CC ECO:0000256|HAMAP-Rule:MF_00337}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:GAX51086.1}.
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DR EMBL; BDQI01000004; GAX51086.1; -; Genomic_DNA.
DR RefSeq; WP_067368332.1; NZ_KQ948455.1.
DR AlphaFoldDB; A0A250VAM2; -.
DR STRING; 1963.AQJ27_15915; -.
DR Proteomes; UP000217446; Unassembled WGS sequence.
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:0006308; P:DNA catabolic process; IEA:UniProtKB-UniRule.
DR Gene3D; 1.10.287.1040; Exonuclease VII, small subunit; 1.
DR HAMAP; MF_00337; Exonuc_7_S; 1.
DR InterPro; IPR003761; Exonuc_VII_S.
DR InterPro; IPR037004; Exonuc_VII_ssu_sf.
DR NCBIfam; TIGR01280; xseB; 1.
DR PANTHER; PTHR34137; EXODEOXYRIBONUCLEASE 7 SMALL SUBUNIT; 1.
DR PANTHER; PTHR34137:SF1; EXODEOXYRIBONUCLEASE 7 SMALL SUBUNIT; 1.
DR Pfam; PF02609; Exonuc_VII_S; 1.
DR PIRSF; PIRSF006488; Exonuc_VII_S; 1.
DR SUPFAM; SSF116842; XseB-like; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_00337};
KW Exonuclease {ECO:0000256|ARBA:ARBA00022839, ECO:0000256|HAMAP-
KW Rule:MF_00337};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|HAMAP-Rule:MF_00337};
KW Nuclease {ECO:0000256|ARBA:ARBA00022722, ECO:0000256|HAMAP-Rule:MF_00337};
KW Reference proteome {ECO:0000313|Proteomes:UP000217446}.
FT REGION 63..85
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 85 AA; 9305 MW; FE4CB89617136256 CRC64;
MTSKVDEALG YEQARDELIE VVRRLEAGGT TLEESLALWE RGEELAKVCR RWLEGARARL
DAALAEEESE SGDGDGHGDG GRDSE
//