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Database: UniProt
Entry: K1LMX2_9LACT
LinkDB: K1LMX2_9LACT
Original site: K1LMX2_9LACT 
ID   K1LMX2_9LACT            Unreviewed;       450 AA.
AC   K1LMX2;
DT   28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT   28-NOV-2012, sequence version 1.
DT   24-JAN-2024, entry version 48.
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=HMPREF9706_01680 {ECO:0000313|EMBL:EKB53422.1};
OS   Facklamia hominis CCUG 36813.
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Aerococcaceae; Facklamia.
OX   NCBI_TaxID=883111 {ECO:0000313|EMBL:EKB53422.1, ECO:0000313|Proteomes:UP000004465};
RN   [1] {ECO:0000313|EMBL:EKB53422.1, ECO:0000313|Proteomes:UP000004465}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CCUG 36813 {ECO:0000313|EMBL:EKB53422.1,
RC   ECO:0000313|Proteomes:UP000004465};
RG   The Broad Institute Genome Sequencing Platform;
RA   Earl A., Ward D., Feldgarden M., Gevers D., Huys G., Walker B., Young S.K.,
RA   Zeng Q., Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Alvarado L.,
RA   Arachchi H.M., Berlin A.M., Chapman S.B., Goldberg J., Griggs A., Gujja S.,
RA   Hansen M., Howarth C., Imamovic A., Larimer J., McCowen C., Montmayeur A.,
RA   Murphy C., Neiman D., Pearson M., Priest M., Roberts A., Saif S., Shea T.,
RA   Sisk P., Sykes S., Wortman J., Nusbaum C., Birren B.;
RT   "The Genome Sequence of Facklamia hominis CCUG 36813.";
RL   Submitted (JUL-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:EKB53422.1}.
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DR   EMBL; AGZD01000013; EKB53422.1; -; Genomic_DNA.
DR   RefSeq; WP_006908988.1; NZ_JH932292.1.
DR   AlphaFoldDB; K1LMX2; -.
DR   STRING; 883111.HMPREF9706_01680; -.
DR   PATRIC; fig|883111.3.peg.1699; -.
DR   HOGENOM; CLU_023625_3_1_9; -.
DR   OrthoDB; 9802795at2; -.
DR   Proteomes; UP000004465; 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:UP000004465}.
FT   DOMAIN          7..102
FT                   /note="OB-fold nucleic acid binding"
FT                   /evidence="ECO:0000259|Pfam:PF13742"
FT   DOMAIN          129..437
FT                   /note="Exonuclease VII large subunit C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02601"
SQ   SEQUENCE   450 AA;  51201 MW;  5E2F38D5FC4476C1 CRC64;
     MANENVLTVS ALSQYINQKF ERDPHLQKIR VVGEVSNYRY RANSHQYFAL KEDKYVINAI
     VFKQKFAQIK FQLEEGMRVI VSARVGVYPG AGRYQLYVDA IEPDGIGSLY LALEQLKEKM
     RKAGYFDRPK KAIPAFPKKI AVITSPSGAV IRDIMTTVKR RFPLAQIIVF PARVQGQEAI
     KDLMEAFDQV KAHQNEIDVV ILARGGGSIE DLWCFNDEEL AHRILDCSLP VISSIGHETD
     TTIADLVADL RAATPTAAAE LAVPVLTDLY TKVDQARQRL LYAFSQTLKA KRDYLQRLSS
     SYTLSQPQRI YQAYDQTLDY LKAKLASQAN AYFKEKHYLQ AGMTARLIQM QPSHRIELAK
     EQLSSYKWQL NKAINSVQGD KEKLLQNLMG LLDAYSPLKI MDRGYAIVSR DDQIINDARL
     LKMEDPLKIR MRHGVVYSRV ESVDSKIEEE
//
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