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Database: UniProt
Entry: K0Z9H9_9ACTN
LinkDB: K0Z9H9_9ACTN
Original site: K0Z9H9_9ACTN 
ID   K0Z9H9_9ACTN            Unreviewed;       434 AA.
AC   K0Z9H9;
DT   28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT   28-NOV-2012, sequence version 1.
DT   24-JAN-2024, entry version 52.
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   ORFNames=HMPREF9451_00729 {ECO:0000313|EMBL:EJZ84020.1};
OS   Slackia piriformis YIT 12062.
OC   Bacteria; Actinomycetota; Coriobacteriia; Eggerthellales; Eggerthellaceae;
OC   Slackia.
OX   NCBI_TaxID=742818 {ECO:0000313|EMBL:EJZ84020.1, ECO:0000313|Proteomes:UP000006069};
RN   [1] {ECO:0000313|EMBL:EJZ84020.1, ECO:0000313|Proteomes:UP000006069}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=YIT 12062 {ECO:0000313|EMBL:EJZ84020.1,
RC   ECO:0000313|Proteomes:UP000006069};
RG   The Broad Institute Genome Sequencing Platform;
RA   Earl A., Ward D., Feldgarden M., Gevers D., Morotomi M., Walker B.,
RA   Young S.K., Zeng Q., Gargeya S., Fitzgerald M., Haas B., Abouelleil A.,
RA   Alvarado L., Arachchi H.M., Berlin A.M., Chapman S.B., Goldberg J.,
RA   Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., Larimer J.,
RA   McCowen C., Montmayeur A., Murphy C., Neiman D., Pearson M., Priest M.,
RA   Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C.,
RA   Birren B.;
RT   "The Genome Sequence of Slackia piriformis YIT 12062.";
RL   Submitted (AUG-2012) 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_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}.
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:EJZ84020.1}.
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DR   EMBL; ADMD01000006; EJZ84020.1; -; Genomic_DNA.
DR   RefSeq; WP_009138952.1; NZ_JH815198.1.
DR   AlphaFoldDB; K0Z9H9; -.
DR   PATRIC; fig|742818.3.peg.776; -.
DR   eggNOG; COG1570; Bacteria.
DR   HOGENOM; CLU_023625_2_2_11; -.
DR   InParanoid; K0Z9H9; -.
DR   OrthoDB; 9802795at2; -.
DR   Proteomes; UP000006069; 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: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; 1.
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:UP000006069}.
FT   DOMAIN          17..108
FT                   /note="OB-fold nucleic acid binding"
FT                   /evidence="ECO:0000259|Pfam:PF13742"
FT   DOMAIN          132..422
FT                   /note="Exonuclease VII large subunit C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02601"
SQ   SEQUENCE   434 AA;  46940 MW;  89BA944CB87731EA CRC64;
     MLLSQASSQG AATSRPLSVS EAMQAAKRSL ESITVKLIGE VSEVNAKAGY KAVYFTVKDA
     GASLPCMIWL NRYHQSGVQL CVGQRVELTG RFTLYAPKGR MNFDVFSISL AGEGDLRRRV
     AELAQRLERE GLMAASRKRP VGSLYEHIGL VTSPRGAAVH DVLRTIRRRF PVARISLAGV
     AVEGSQAPQG IVFGIDACVR AGCEVILVVR GGGSFEDLMP FNDERLARAI AACPVPIVTG
     IGHEPDTSIA DMVADVRSST PTAAAERVSP DSSTLLRELD ARAASMSASQ RLAIERYEAR
     LGHIASRPLF KDPHLLFSTD LLTLDLLHDR LSRALPECLA KDSLHLNDMQ RRLCDRAKTS
     FERFEHDLAL RAGRLHDLSP LAVLSRGYAI AKDEEGSVVR SIHAVHGGDR IDVAVSDGVI
     SCSVNCSSPH TQAE
//
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