EX7L_RICAH
ID EX7L_RICAH Reviewed; 444 AA.
AC A8GPH1;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 13-NOV-2007, sequence version 1.
DT 25-MAY-2022, entry version 76.
DE RecName: Full=Exodeoxyribonuclease 7 large subunit {ECO:0000255|HAMAP-Rule:MF_00378};
DE EC=3.1.11.6 {ECO:0000255|HAMAP-Rule:MF_00378};
DE AltName: Full=Exodeoxyribonuclease VII large subunit {ECO:0000255|HAMAP-Rule:MF_00378};
DE Short=Exonuclease VII large subunit {ECO:0000255|HAMAP-Rule:MF_00378};
GN Name=xseA {ECO:0000255|HAMAP-Rule:MF_00378}; OrderedLocusNames=A1C_05220;
OS Rickettsia akari (strain Hartford).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC Rickettsiaceae; Rickettsieae; Rickettsia; spotted fever group.
OX NCBI_TaxID=293614;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Hartford;
RA Madan A., Fahey J., Helton E., Ketteman M., Madan A., Rodrigues S.,
RA Sanchez A., Whiting M., Dasch G., Eremeeva M.;
RT "Complete genome sequence of Rickettsia akari.";
RL Submitted (SEP-2007) 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:0000255|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:0000255|HAMAP-Rule:MF_00378};
CC -!- SUBUNIT: Heterooligomer composed of large and small subunits.
CC {ECO:0000255|HAMAP-Rule:MF_00378}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00378}.
CC -!- SIMILARITY: Belongs to the XseA family. {ECO:0000255|HAMAP-
CC Rule:MF_00378}.
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DR EMBL; CP000847; ABV75296.1; -; Genomic_DNA.
DR RefSeq; WP_012149926.1; NC_009881.1.
DR AlphaFoldDB; A8GPH1; -.
DR SMR; A8GPH1; -.
DR STRING; 293614.A1C_05220; -.
DR EnsemblBacteria; ABV75296; ABV75296; A1C_05220.
DR KEGG; rak:A1C_05220; -.
DR eggNOG; COG1570; Bacteria.
DR HOGENOM; CLU_023625_2_0_5; -.
DR OMA; WPAVRFE; -.
DR Proteomes; UP000006830; 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 PANTHER; PTHR30008; PTHR30008; 1.
DR Pfam; PF02601; Exonuc_VII_L; 1.
DR Pfam; PF13742; tRNA_anti_2; 1.
DR TIGRFAMs; TIGR00237; xseA; 1.
PE 3: Inferred from homology;
KW Cytoplasm; Exonuclease; Hydrolase; Nuclease.
FT CHAIN 1..444
FT /note="Exodeoxyribonuclease 7 large subunit"
FT /id="PRO_1000048780"
SQ SEQUENCE 444 AA; 49786 MW; A68B9C33D8C81B44 CRC64;
MLENFIANQA TKEFSVSEIS NKIKELLENN FGYIKVKGEI SGLKIASSGH AYFNLKENTA
ILACTCWRPI LAKIKFPLND GIEVVISGKL SSYAGNSRYQ LSVDNLQPAG LGAMLQILND
RKARLEKEGL FNKIRIPIPF LPDKIGVITS ITGAVIKDII HRIRERFPTR IIIWPVSVQG
ENSSNEIAEA IEGFNNLAEV NKPSVIIVAR GGGSIEDLWS FNDEILVRAA YNSKIPIISA
VGHEVDYTLI DLAADKRAPT PTAAAEFAVP VRSILNNTLH SYEKILLNNT SRLIKYHEHN
IINYDKIHRY LSHYMDNRQQ LLDETGFNLL DALLCFIELQ ETKIKSFSKE RVNPAKILNY
KTLELTHQTA YLSKSANNTL KNFEYKLELN STLLASLDYN NVLKRGFAIV KGETGNFLSS
KIAAANEKIF NIKFSDGEIK VVRN
