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Database: UniProt
Entry: A0A2T3MT85_9GAMM
LinkDB: A0A2T3MT85_9GAMM
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ID   A0A2T3MT85_9GAMM        Unreviewed;       449 AA.
AC   A0A2T3MT85;
DT   18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT   18-JUL-2018, sequence version 1.
DT   24-JAN-2024, entry version 15.
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=C9I89_19270 {ECO:0000313|EMBL:PSW02114.1};
OS   Photobacterium lipolyticum.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Photobacterium.
OX   NCBI_TaxID=266810 {ECO:0000313|EMBL:PSW02114.1, ECO:0000313|Proteomes:UP000240904};
RN   [1] {ECO:0000313|EMBL:PSW02114.1, ECO:0000313|Proteomes:UP000240904}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 16190 {ECO:0000313|EMBL:PSW02114.1,
RC   ECO:0000313|Proteomes:UP000240904};
RA   Butler K.;
RT   "Whole genome sequencing of Histamine producing bacteria.";
RL   Submitted (MAR-2018) 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}.
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:PSW02114.1}.
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DR   EMBL; PYMC01000019; PSW02114.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2T3MT85; -.
DR   OrthoDB; 9802795at2; -.
DR   Proteomes; UP000240904; 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:UP000240904}.
FT   DOMAIN          15..108
FT                   /note="OB-fold nucleic acid binding"
FT                   /evidence="ECO:0000259|Pfam:PF13742"
FT   DOMAIN          131..445
FT                   /note="Exonuclease VII large subunit C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02601"
SQ   SEQUENCE   449 AA;  50366 MW;  4F142D7A0DE3473F CRC64;
     MTMFAQQTQS NDRIYTVSSL NAEVRLLLEN EMGIVWLVGE LSNLSMPVSG HWYFTLKDSR
     AQVKCAMFKG NNRRVTFKPA NGTQVLVKAR LSLYEPRGDY QLIIESMQPE GDGRLQQQFE
     QLKMALAAEG LFAQSLKKSL PEQPQRVGIV TSKTGAALHD ILNVLQRRDP NLPIVIYPTM
     VQGEGAAISI AQAIGRANTR QECDVLIVGR GGGSLEDLWA FNEEIVARTI AASQIPVVSA
     VGHEVDVTIA DFVADVRAPT PSAAAELVSR DMTHQTQKID QKRQQLQHAF RHYMTEHSAR
     LVQLHHRLER QHPQLRLNQQ QQHLDDISSR LERAINKLTT GHHQHLERIE YKLALHSPAQ
     TIKHNSTRLK QAERRLLDAM DRRLLNASHK LAMAAEKLET VSPLATLGRG YSITRDTKGN
     VIRRADQVKA GDELHTKVAE GEIRSVVTE
//
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