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Database: UniProt
Entry: A0A1L3ZZQ7_9SPHN
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Original site: A0A1L3ZZQ7_9SPHN 
ID   A0A1L3ZZQ7_9SPHN        Unreviewed;       463 AA.
AC   A0A1L3ZZQ7;
DT   15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT   15-MAR-2017, sequence version 1.
DT   13-SEP-2023, entry version 25.
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=BSL82_12255 {ECO:0000313|EMBL:API61121.1};
OS   Tardibacter chloracetimidivorans.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC   Sphingomonadaceae; Tardibacter.
OX   NCBI_TaxID=1921510 {ECO:0000313|EMBL:API61121.1, ECO:0000313|Proteomes:UP000182063};
RN   [1] {ECO:0000313|Proteomes:UP000182063}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JJ-A5 {ECO:0000313|Proteomes:UP000182063};
RA   Lee H., Ka J.-O.;
RT   "Complete Genome Sequence of alachlor-degrading Sphingomonas sp. strain JJ-
RT   A5.";
RL   Submitted (NOV-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; CP018221; API61121.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1L3ZZQ7; -.
DR   STRING; 1921510.BSL82_12255; -.
DR   KEGG; sphj:BSL82_12255; -.
DR   Proteomes; UP000182063; 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   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:UP000182063}.
FT   DOMAIN          27..119
FT                   /note="OB-fold nucleic acid binding"
FT                   /evidence="ECO:0000259|Pfam:PF13742"
FT   DOMAIN          143..435
FT                   /note="Exonuclease VII large subunit C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02601"
FT   REGION          435..463
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   463 AA;  49765 MW;  58CC3686F54D5D2B CRC64;
     MPNDPTLNEE NARLVAEEGA SGNSPALSVS ELSNALKRTV EDRFGHVRVR GEISGWKRAA
     SGHGYLCLKD DNAVLDGVMW KGVLQSLRFA PEDGLEVIAT GKLTTYPGRS KYQIVIERLE
     IAGAGALMAL LEQRRRKLLA EGLFDPARKR PLPFLPEVIG VVTSPTGAVI RDILHRLEDR
     FPRRVIVWPV LVQGETAAAQ VAAAVRGFNA ISGVDRPDLL IVARGGGSIE DLWAFNEEIV
     VRAVAESGIP TISAVGHETD TTLCDFAADV RAPTPTAAAE MAVPVRADLI TAVRQLSLRA
     ERCAQRVLES RRERVEGLGR RLPTPRALLG LARQRADDIG ERLPRALAVR AQRASASLDA
     VGARLRPQLL DRRLKEAGSQ LERLWRVAES LNPKGVLRRG YALVTDTSGH VVTSAAGARA
     ARRVSLQFAD GGVDATIGSD ESAPRAPSPK KAAAASSSQP KLL
//
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