EX7L_RICCN
ID EX7L_RICCN Reviewed; 444 AA.
AC Q92GU6;
DT 06-JUN-2002, integrated into UniProtKB/Swiss-Prot.
DT 02-AUG-2002, sequence version 2.
DT 25-MAY-2022, entry version 98.
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=RC1026;
OS Rickettsia conorii (strain ATCC VR-613 / Malish 7).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC Rickettsiaceae; Rickettsieae; Rickettsia; spotted fever group.
OX NCBI_TaxID=272944;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC VR-613 / Malish 7;
RX PubMed=11557893; DOI=10.1126/science.1061471;
RA Ogata H., Audic S., Renesto-Audiffren P., Fournier P.-E., Barbe V.,
RA Samson D., Roux V., Cossart P., Weissenbach J., Claverie J.-M., Raoult D.;
RT "Mechanisms of evolution in Rickettsia conorii and R. prowazekii.";
RL Science 293:2093-2098(2001).
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAL03564.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AE006914; AAL03564.1; ALT_INIT; Genomic_DNA.
DR PIR; B97828; B97828.
DR RefSeq; WP_041471739.1; NC_003103.1.
DR AlphaFoldDB; Q92GU6; -.
DR SMR; Q92GU6; -.
DR EnsemblBacteria; AAL03564; AAL03564; RC1026.
DR KEGG; rco:RC1026; -.
DR PATRIC; fig|272944.4.peg.1167; -.
DR HOGENOM; CLU_023625_2_0_5; -.
DR OMA; WPAVRFE; -.
DR Proteomes; UP000000816; 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_0000197872"
SQ SEQUENCE 444 AA; 49886 MW; CAB0B6BB443F476B CRC64;
MLDNFIAHQA TKEFSVSEIS NKIKELLENN FGYIKVKGEI SGLKIANSGH AYFNLKENTA
ILACTCWRPI LAKITFPLND GMEVVISGKL SSYAGNSRYQ LSVDNLQPTG LGAMLQILNE
RKAKLEKEGL FNKIRIPIPF LPDKIGVITS ITGAVIKDII HRIRERFPTR IIIWPVSVQG
ENSGNEIAEA IEGFNNLEEV NKPRVIIVAR GGGSIEDLWS FNDEILVRAA YNSKIPIISA
VGHEVDYTLI DLAADKRAPT PTAAAEFAVP VRSILNNTLQ SYEKILLNNT SRLIKYHEQN
IVNYNKIHRY LSHYINNRQQ LLDETGFNLL DALPCFIELQ ETKIKSFSKE RVNPAKIINY
KTLELTHQTA YLSKSANNTL KNFEYKLELN STLLASLDYH NVLKRGFAIV KGETGNFLSS
KMTAANEKIF NIKFSDGEIK VVRA
