ID A0A143DEV9_9PROT Unreviewed; 520 AA.
AC A0A143DEV9;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 27-MAR-2024, entry version 36.
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=AY555_05100 {ECO:0000313|EMBL:AMW34658.1};
OS Haematospirillum jordaniae.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC Novispirillaceae; Haematospirillum.
OX NCBI_TaxID=1549855 {ECO:0000313|EMBL:AMW34658.1, ECO:0000313|Proteomes:UP000076066};
RN [1] {ECO:0000313|EMBL:AMW34658.1, ECO:0000313|Proteomes:UP000076066}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=H5569 {ECO:0000313|EMBL:AMW34658.1,
RC ECO:0000313|Proteomes:UP000076066};
RA Nicholson A.C., Humrighouse B.W., Loparov V., McQuiston J.R.;
RT "Complete Genome of H5569, the type strain of the newly described species
RT Haematospirillium jordaniae.";
RL Submitted (FEB-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; CP014525; AMW34658.1; -; Genomic_DNA.
DR RefSeq; WP_066134267.1; NZ_JAAVTE010000002.1.
DR AlphaFoldDB; A0A143DEV9; -.
DR STRING; 1549855.AY555_05100; -.
DR GeneID; 53316528; -.
DR KEGG; hjo:AY555_05100; -.
DR OrthoDB; 9802795at2; -.
DR Proteomes; UP000076066; Chromosome.
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; 2.
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:UP000076066}.
FT DOMAIN 20..111
FT /note="OB-fold nucleic acid binding"
FT /evidence="ECO:0000259|Pfam:PF13742"
FT DOMAIN 135..415
FT /note="Exonuclease VII large subunit C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02601"
FT DOMAIN 329..493
FT /note="Exonuclease VII large subunit C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02601"
FT REGION 497..520
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 504..520
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 520 AA; 56059 MW; 05A59B2048A2EA0C CRC64;
MTATETTGQA DPVHNLPERT VSEVSTDLKR MVEDRFARVR VRGEISQPKL AGSGHCYLRL
KDDNAVLDGV IWKGTYPKLG TKPQDGLEVI VTGRLTTWPG RSSYQIVIES LELAGEGALL
KLLEERRRRL AAEGLFDPAT KKALPFLPRV IGVVTSPTGA VIRDILHRLS DRFPVHVLVW
PVLVQGEGAA AQIAAAVRGF NALGSDSPIV RPDLVIVARG GGSLEDLMAF NEEEVVRAVA
ASDIPVISAV GHETDTTLCD FAADRRAPTP TGAAEIAVPV RLDLCVQVAD VARRLTAATR
RSFAEQGTRL QGLARGLPPL DRLVQGHVQR LEDRAERLGT AVGSFLERNR SSFLALAAAL
RHPRDRVAMA FARLDTAGSA LSGAFRLSLG GASTRLGSSA VRLAAVSPVR GLAQGRDRVT
GLEQRLVAAM HRLQQDEGQR LLNAAERLEA ASWQRALQRG YAVVRDSNGL LVDRRASVRV
GDVLSIQLAD GDLPVVARGP GGRVSRRTRQ DSDPRQDSLF
//
