ID A0A1H2UCC2_9BACL Unreviewed; 456 AA.
AC A0A1H2UCC2;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 19.
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=SAMN05444487_10465 {ECO:0000313|EMBL:SDW53842.1};
OS Marininema mesophilum.
OC Bacteria; Bacillota; Bacilli; Bacillales; Thermoactinomycetaceae;
OC Marininema.
OX NCBI_TaxID=1048340 {ECO:0000313|EMBL:SDW53842.1, ECO:0000313|Proteomes:UP000198534};
RN [1] {ECO:0000313|EMBL:SDW53842.1, ECO:0000313|Proteomes:UP000198534}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 45610 {ECO:0000313|EMBL:SDW53842.1,
RC ECO:0000313|Proteomes:UP000198534};
RA de Groot N.N.;
RL Submitted (OCT-2016) 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}.
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DR EMBL; FNNQ01000004; SDW53842.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H2UCC2; -.
DR STRING; 1048340.SAMN05444487_10465; -.
DR OrthoDB; 9802795at2; -.
DR Proteomes; UP000198534; 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:UP000198534}.
FT DOMAIN 10..105
FT /note="OB-fold nucleic acid binding"
FT /evidence="ECO:0000259|Pfam:PF13742"
FT DOMAIN 128..443
FT /note="Exonuclease VII large subunit C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02601"
SQ SEQUENCE 456 AA; 52540 MW; 51EB6567322425CD CRC64;
MLGREREESF TITDLVRYLT LVIEQDGVLS QISVQGEISN FKRHARGHLY FTLKDEQSQI
RAVMFAGNTR RLRFKPKDGD DVLIRGRVGV YERDGQVQLY VTSMQPRGVG DLYAAFQELK
EKLEKEGLFS PLFKQPLPFF PHRVGVITSA HGAAVRDIIT TIQRRNSAVN ILLLPVPVQG
PESPAAVAEA IRQMNDCDVD VMIVGRGGGS LEELWAFNEE VVVRSIYESK IPVVSAVGHE
TDTSLTDFVS DVRAATPTAA AELVTPRLDE QMYRFTTLES RLIRAQRRQL DAMQERLTHA
MSRPPFRRPR TRLDQEQQRL DYLTTDLVRT VRYPILRQHH RLEHLHTRLL AQRPHARLAE
MSDRWIRLTK ACKGEMSRRI HEGREQWLRR LERLDAISPL KVMSRGYSLV YRRNETELVR
SVKQIEPGDL IKVRLADGKL KAQVWGWEEN PDGRIR
//
