ID A0A1G6TD96_9PROT Unreviewed; 485 AA.
AC A0A1G6TD96;
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=SAMN04487779_100619 {ECO:0000313|EMBL:SDD26407.1};
OS Belnapia rosea.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC Acetobacteraceae; Belnapia.
OX NCBI_TaxID=938405 {ECO:0000313|EMBL:SDD26407.1, ECO:0000313|Proteomes:UP000198925};
RN [1] {ECO:0000313|EMBL:SDD26407.1, ECO:0000313|Proteomes:UP000198925}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CPCC 100156 {ECO:0000313|EMBL:SDD26407.1,
RC ECO:0000313|Proteomes:UP000198925};
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; FMZX01000006; SDD26407.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G6TD96; -.
DR STRING; 938405.SAMN02927895_03049; -.
DR Proteomes; UP000198925; 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:UP000198925}.
FT DOMAIN 14..105
FT /note="OB-fold nucleic acid binding"
FT /evidence="ECO:0000259|Pfam:PF13742"
FT DOMAIN 129..462
FT /note="Exonuclease VII large subunit C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02601"
FT REGION 459..485
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 469..485
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 485 AA; 52888 MW; 3C2B2CD117EA907F CRC64;
MDTPAPRANI PEFAVSEIAG AIKRTLEESF GRVRVRGEIT ELKRYPSGHI YLSLKDEAAK
LESVIWKTSV GRLAVKPENG IEVIATGRIG TYADRSKYQL VIDRLEFAGE GALLARIEML
RKRLLEEGLF DAGRKRRLPM LPATIGVVTS ERGAVIQDIR TTIARRFPRR ILLWPVAVQG
QGAAEQIAAA IRGFGRLQGA MRPDVIIVAR GGGSLEDLMA FNEEIVVRAA AESPIPLISA
VGHETDTTLI DFASDRRAPT PTAAAEMAIP ARTDLLADLA QTEARLLQLG RALIERARRR
LMVAERGLPD LPNILGAMRQ RLEDRGERLT LALPGLVQRK RGELGRLAPR LPHPREGIAA
RRAMLALLQA RGRAAWQRIE ARGHAAPPLA RFSTGPVESL LREKRLRLEG LVARLDSVSF
QAVLSRGFAL VRDAEGAPIT SAASVPPGGR LVLTFADGEA QATADGTKPA PKRRPRDEPT
QETLL
//
