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Database: UniProt
Entry: A0A2B8BBV3_9PROT
LinkDB: A0A2B8BBV3_9PROT
Original site: A0A2B8BBV3_9PROT 
ID   A0A2B8BBV3_9PROT        Unreviewed;       587 AA.
AC   A0A2B8BBV3;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   20-DEC-2017, sequence version 1.
DT   24-JAN-2024, entry version 22.
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=CRT60_26210 {ECO:0000313|EMBL:PGH55038.1};
OS   Azospirillum palustre.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC   Azospirillaceae; Azospirillum.
OX   NCBI_TaxID=2044885 {ECO:0000313|EMBL:PGH55038.1, ECO:0000313|Proteomes:UP000225379};
RN   [1] {ECO:0000313|Proteomes:UP000225379}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=B2 {ECO:0000313|Proteomes:UP000225379};
RA   Kravchenko I.K., Grouzdev D.S.;
RL   Submitted (OCT-2017) 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   -!- 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   -!- SIMILARITY: Belongs to the XseA family. {ECO:0000256|HAMAP-
CC       Rule:MF_00378}.
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:PGH55038.1}.
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DR   EMBL; PDKW01000043; PGH55038.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2B8BBV3; -.
DR   OrthoDB; 9802795at2; -.
DR   Proteomes; UP000225379; 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; 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}.
FT   DOMAIN          70..163
FT                   /note="OB-fold nucleic acid binding"
FT                   /evidence="ECO:0000259|Pfam:PF13742"
FT   DOMAIN          186..412
FT                   /note="Exonuclease VII large subunit C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02601"
FT   DOMAIN          387..541
FT                   /note="Exonuclease VII large subunit C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02601"
FT   REGION          45..69
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          550..587
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        45..59
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        560..576
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   587 AA;  63612 MW;  C870B4B649272B5B CRC64;
     MAQQSACSRP PDPTTRTFMG GRSFRLVAIC APCIMAAPQL KSAMTSENAP QTSTPLIAPE
     PRPGSNLPEF TVGDLARRLK RSIEEEFGFV RVRGEISQPK KHSSGHCYMR LKDDTAVIEA
     VCWRGTMAKL AVRPEEGLEV IVTGRMTTYP GRSQYQLIVE SMELAGEGAL LKMLEERKRR
     LAAEGLFDPA RKKRIPFLPD VIGVVTSPTG AVIRDILHRL NDRFPRHVLL WPVAVQGERA
     AAEVTAAIEG FNRIQPGGRV PRPDLIIVAR GGGSLEDLMA FNEENVVRAA AASAIPLISA
     VGHETDTTLI DFASDLRAPT PTAAAEMAVP VRGELLAQIL DDERRLLACA SRAVEDRRNR
     VEGLARGLGD PRALLEGHAQ RLDDRAERLN LAAMALLERR RTRVGELAAK LRHPREKLAQ
     AEQKLASESR ALDSGLRHAV TTAGGRFDRV AGRLSLTPAR VKLADGERRI ADLTPRLDRS
     HAKGVADKAA SLASLGQLLE SYSYKGVLAR GFALVEDRDG RPVTRADQAT PGLAVNIVFA
     NDAKVAATVD GGAPKVEIKP EAQADPKPEK KAAPRKPRPV PVQGSLF
//
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