ID B2GJV2_KOCRD Unreviewed; 437 AA.
AC B2GJV2;
DT 10-JUN-2008, integrated into UniProtKB/TrEMBL.
DT 10-JUN-2008, sequence version 1.
DT 27-MAR-2024, entry version 96.
DE RecName: Full=Exodeoxyribonuclease 7 large subunit {ECO:0000256|HAMAP-Rule:MF_00378};
DE EC=3.1.11.6 {ECO:0000256|HAMAP-Rule:MF_00378};
DE AltName: Full=Exodeoxyribonuclease VII large subunit {ECO:0000256|HAMAP-Rule:MF_00378};
DE Short=Exonuclease VII large subunit {ECO:0000256|HAMAP-Rule:MF_00378};
GN Name=xseA {ECO:0000256|HAMAP-Rule:MF_00378,
GN ECO:0000313|EMBL:BAG29057.1};
GN OrderedLocusNames=KRH_07100 {ECO:0000313|EMBL:BAG29057.1};
OS Kocuria rhizophila (strain ATCC 9341 / DSM 348 / NBRC 103217 / DC2201).
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC Kocuria.
OX NCBI_TaxID=378753 {ECO:0000313|EMBL:BAG29057.1, ECO:0000313|Proteomes:UP000008838};
RN [1] {ECO:0000313|EMBL:BAG29057.1, ECO:0000313|Proteomes:UP000008838}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 9341 / DSM 348 / NBRC 103217 / DC2201
RC {ECO:0000313|Proteomes:UP000008838};
RX PubMed=18408034; DOI=10.1128/JB.01853-07;
RA Takarada H., Sekine M., Kosugi H., Matsuo Y., Fujisawa T., Omata S.,
RA Kishi E., Shimizu A., Tsukatani N., Tanikawa S., Fujita N., Harayama S.;
RT "Complete genome sequence of the soil actinomycete Kocuria rhizophila.";
RL J. Bacteriol. 190:4139-4146(2008).
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_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:0000256|HAMAP-Rule:MF_00378,
CC ECO:0000256|RuleBase:RU004355};
CC -!- SUBUNIT: Heterooligomer composed of large and small subunits.
CC {ECO:0000256|HAMAP-Rule:MF_00378}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00378,
CC ECO:0000256|RuleBase:RU004355}.
CC -!- SIMILARITY: Belongs to the XseA family. {ECO:0000256|HAMAP-
CC Rule:MF_00378, ECO:0000256|RuleBase:RU004355}.
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DR EMBL; AP009152; BAG29057.1; -; Genomic_DNA.
DR RefSeq; WP_012397782.1; NC_010617.1.
DR AlphaFoldDB; B2GJV2; -.
DR STRING; 378753.KRH_07100; -.
DR KEGG; krh:KRH_07100; -.
DR eggNOG; COG1570; Bacteria.
DR HOGENOM; CLU_023625_2_1_11; -.
DR OrthoDB; 9802795at2; -.
DR Proteomes; UP000008838; 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 NCBIfam; TIGR00237; xseA; 1.
DR PANTHER; PTHR30008; EXODEOXYRIBONUCLEASE 7 LARGE SUBUNIT; 1.
DR PANTHER; PTHR30008:SF0; EXODEOXYRIBONUCLEASE 7 LARGE SUBUNIT; 1.
DR Pfam; PF02601; Exonuc_VII_L; 2.
DR Pfam; PF13742; tRNA_anti_2; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_00378};
KW Exonuclease {ECO:0000256|ARBA:ARBA00022839, ECO:0000256|HAMAP-
KW Rule:MF_00378};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|HAMAP-Rule:MF_00378};
KW Nuclease {ECO:0000256|ARBA:ARBA00022722, ECO:0000256|HAMAP-Rule:MF_00378};
KW Reference proteome {ECO:0000313|Proteomes:UP000008838}.
FT DOMAIN 41..131
FT /note="OB-fold nucleic acid binding"
FT /evidence="ECO:0000259|Pfam:PF13742"
FT DOMAIN 155..367
FT /note="Exonuclease VII large subunit C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02601"
FT DOMAIN 344..423
FT /note="Exonuclease VII large subunit C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02601"
FT REGION 1..39
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 437 AA; 47935 MW; 388F4886FEDC9BE2 CRC64;
MDTSFPHDAA PHAHGAPGQQ EPPAELPRLA RDTSPENPWP LSKLSHALHG WVQKAPDAWV
EGQVIEVNER ARVCYVTLRD LQEEASVSVT LFKKEMARLE RPLERGSRVV VNLQADFYVK
TGRLSMLGRD IRPVGLGDLL ERLERLRRAL ADEGLFDPAR KKPLPVLPHR VGLITGRNSD
AEKDVVRNAT NRWPGVQFEI REVPVQGSGS ARAVIGALEE LDAMAEVDVI VIARGGGAFE
DLLSFSEESL LRAVFAARTP VVSAIGHEND QPLLDHVADV RASTPTDAGK RVVPDVHEER
LRLGQARAAL DRAVGSLIER EQQGLATVRS RPVLSQPDGM ILVREEDLDR WRTRAWTATN
SLTLRAQDSV AQMRARVRAL SPQQTLDRGY AVVQTTDGSV LTDASRAQVG QQLTVRLAAG
ELGVDVTGTS TRQPGEH
//
