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Database: UniProt
Entry: A4ADE7_9GAMM
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Original site: A4ADE7_9GAMM 
ID   A4ADE7_9GAMM            Unreviewed;       451 AA.
AC   A4ADE7;
DT   03-APR-2007, integrated into UniProtKB/TrEMBL.
DT   03-APR-2007, sequence version 1.
DT   24-JAN-2024, entry version 80.
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=KT71_18117 {ECO:0000313|EMBL:EAQ95945.1};
OS   Congregibacter litoralis KT71.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Cellvibrionales; Halieaceae;
OC   Congregibacter.
OX   NCBI_TaxID=314285 {ECO:0000313|EMBL:EAQ95945.1, ECO:0000313|Proteomes:UP000019205};
RN   [1] {ECO:0000313|EMBL:EAQ95945.1, ECO:0000313|Proteomes:UP000019205}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KT71 {ECO:0000313|EMBL:EAQ95945.1,
RC   ECO:0000313|Proteomes:UP000019205};
RX   PubMed=17299055; DOI=10.1073/pnas.0608046104;
RA   Fuchs B.M., Spring S., Teeling H., Quast C., Wulf J., Schattenhofer M.,
RA   Yan S., Ferriera S., Johnson J., Glockner F.O., Amann R.;
RT   "Characterization of a marine gammaproteobacterium capable of aerobic
RT   anoxygenic photosynthesis.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:2891-2896(2007).
RN   [2] {ECO:0000313|EMBL:EAQ95945.1, ECO:0000313|Proteomes:UP000019205}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KT71 {ECO:0000313|EMBL:EAQ95945.1,
RC   ECO:0000313|Proteomes:UP000019205};
RX   PubMed=19287491; DOI=10.1371/journal.pone.0004866;
RA   Spring S., Lunsdorf H., Fuchs B.M., Tindall B.J.;
RT   "The photosynthetic apparatus and its regulation in the aerobic
RT   gammaproteobacterium Congregibacter litoralis gen. nov., sp. nov.";
RL   PLoS ONE 4:E4866-E4866(2009).
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}.
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:EAQ95945.1}.
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DR   EMBL; AAOA02000001; EAQ95945.1; -; Genomic_DNA.
DR   RefSeq; WP_008296065.1; NZ_CM002299.1.
DR   AlphaFoldDB; A4ADE7; -.
DR   STRING; 314285.KT71_18117; -.
DR   eggNOG; COG1570; Bacteria.
DR   HOGENOM; CLU_023625_3_1_6; -.
DR   OrthoDB; 9802795at2; -.
DR   Proteomes; UP000019205; 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; 1.
DR   Pfam; PF13742; tRNA_anti_2; 1.
PE   3: Inferred from homology;
KW   Coiled coil {ECO:0000256|SAM:Coils};
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:UP000019205}.
FT   DOMAIN          14..101
FT                   /note="OB-fold nucleic acid binding"
FT                   /evidence="ECO:0000259|Pfam:PF13742"
FT   DOMAIN          127..445
FT                   /note="Exonuclease VII large subunit C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02601"
FT   COILED          267..379
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   451 AA;  50571 MW;  92F359CFDB4282B5 CRC64;
     MPSTTVAADV LSPSQLNRQA RSLLESHFSY VWIEGELSNF ARPSSGHWYF TLKDDKAQVR
     CAMFKTYNQR LRFSPNNGDQ VRVRARVSLY EGRGEFQLIG EFLEPAGAGA LQARFEALRD
     QLRAEGLFDA ANKQPLPRSV NHLAVITSPT GAALQDILQV LARRNPSIRV TILPVAVQGT
     DAPGEIRQAL QEANEYARSR YDCDFDAVII ARGGGSLEDL WAFNDEALAR EIVASKLPVV
     SGVGHEVDVT IADFAADVRA PTPSAAAELL SEDRVELIAR LAEAQKRLHR AMVHRLERER
     MNLDRMRARL KHPGDRLREQ AQRLDELENR LNRAIKQRLA QLQHAQQARR ERLLSHSPLR
     RLTISREKVA RQKAALEAAM AQKLAWHRQG LERREQVLKS LNPLAILERG YAIISDAQGG
     VVRASDAVSP EQVLEARLAR GRLKLRVESS E
//
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