ID A0A1A8XY44_9PROT Unreviewed; 469 AA.
AC A0A1A8XY44;
DT 05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2016, sequence version 1.
DT 24-JAN-2024, entry version 24.
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:SBT09890.1};
GN ORFNames=ACCAA_790054 {ECO:0000313|EMBL:SBT09890.1};
OS Candidatus Accumulibacter aalborgensis.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Candidatus Accumulibacter.
OX NCBI_TaxID=1860102 {ECO:0000313|EMBL:SBT09890.1, ECO:0000313|Proteomes:UP000199169};
RN [1] {ECO:0000313|EMBL:SBT09890.1, ECO:0000313|Proteomes:UP000199169}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=3 {ECO:0000313|EMBL:SBT09890.1};
RA Kjaerup R.B., Dalgaard T.S., Juul-Madsen H.R.;
RL Submitted (JUN-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; FLQX01000159; SBT09890.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1A8XY44; -.
DR STRING; 1860102.ACCAA_790054; -.
DR Proteomes; UP000199169; 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:UP000199169}.
FT DOMAIN 19..109
FT /note="OB-fold nucleic acid binding"
FT /evidence="ECO:0000259|Pfam:PF13742"
FT DOMAIN 134..444
FT /note="Exonuclease VII large subunit C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02601"
SQ SEQUENCE 469 AA; 50866 MW; BC5775B07563A0B0 CRC64;
MSDTPRAGTG LPTLVPVIAV SMLNRLARER LEAAFPLCWV AGEVSNLSYA ASGHVYFSLK
DAAAQVRCVM FRSRTQLLGW RLENGQHIEA RVLVTLYEAR GDFQLNVEAA RRAGVGNLYE
KFIRLKEGLE REGLFASTAK RPLPLFPRRV GIVTSLQAAA LRDVLSTLGR RAAQVSIVVY
PTLVQGEGAA AQIADTIRVA GERMECEVLI VCRGGGSMED LWAFNEEVVA RAIRACPLPV
ISGIGHETDF TIADFAADQR APTPTAAAEL AAPEQAVLLA RLAARQLALQ RSMEQYLNQR
GQQIDWLTRR LQHPAQYLAA HRDGLRRLQH QLAAGVLQTS SLARHALASL GHRLLLVRPD
AARHAGRIEV LAQRLRGGWQ HTVQGQSADL TRLAASLAHL NPHAVLTRGY CIVTSDQGQI
VRESKALAAS QTITAFFQSG HVEATVLAVF DDHGAALASP AIASTARPD
//
