EX7L_CHLTR
ID EX7L_CHLTR Reviewed; 516 AA.
AC O84333;
DT 01-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 25-MAY-2022, entry version 112.
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=CT_329;
OS Chlamydia trachomatis (strain D/UW-3/Cx).
OC Bacteria; Chlamydiae; Chlamydiales; Chlamydiaceae;
OC Chlamydia/Chlamydophila group; Chlamydia.
OX NCBI_TaxID=272561;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=D/UW-3/Cx;
RX PubMed=9784136; DOI=10.1126/science.282.5389.754;
RA Stephens R.S., Kalman S., Lammel C.J., Fan J., Marathe R., Aravind L.,
RA Mitchell W.P., Olinger L., Tatusov R.L., Zhao Q., Koonin E.V., Davis R.W.;
RT "Genome sequence of an obligate intracellular pathogen of humans: Chlamydia
RT trachomatis.";
RL Science 282:754-759(1998).
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; AE001273; AAC67922.1; -; Genomic_DNA.
DR PIR; F71529; F71529.
DR RefSeq; NP_219836.1; NC_000117.1.
DR RefSeq; WP_010725160.1; NC_000117.1.
DR AlphaFoldDB; O84333; -.
DR SMR; O84333; -.
DR STRING; 813.O172_01790; -.
DR EnsemblBacteria; AAC67922; AAC67922; CT_329.
DR GeneID; 884790; -.
DR KEGG; ctr:CT_329; -.
DR PATRIC; fig|272561.5.peg.354; -.
DR HOGENOM; CLU_023625_3_1_0; -.
DR InParanoid; O84333; -.
DR OMA; KIACTIW; -.
DR Proteomes; UP000000431; 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; Reference proteome.
FT CHAIN 1..516
FT /note="Exodeoxyribonuclease 7 large subunit"
FT /id="PRO_0000197838"
SQ SEQUENCE 516 AA; 58621 MW; ECEC3F0FB66A5C0E CRC64;
MSITSPPIEV SVLTDSIKNL LEKNFLRVVV KGELSNVSLQ TSGHLYFAIK DSKAVLNGAF
FHFRSKYFDR KPKDGDYVIL HGKLTVYAPR GQYQIVAYAL TFSGEGNLLQ QFEERKQRLA
AEGYFDPKRK KPLPSGARVI GVITSPTGAV IQDILRVLSR RCHQFQVILY PVTVQGATAA
QEISQAIQFF NQNSMGVHAL IIARGGGSIE DLWAFNEEEL VKSIVASSIP IISAVGHETD
FTLCDFASDV RAPTPSAAAE IVCKSSDQYR QELQNLRRYV LSHARQFIAA KKNLLTHWQR
HLASVDFYHT AQQTLDYTRA ALERGIETKL EYYKQRFAQY RRWLKSDVLI RIEKHLADLN
QSLMLSIKNK IYTKKTSLNQ LYTSCLKNEL LNLQHHTQHS RNILSQLSRR LHIAIASSQQ
THQECLVRLQ NELSFTIHHL LTKAKERCQA IQEQASSLNP KNVLKRGFAQ LFDFNKHFVI
ISAESLKQSD LVRVCLQDGE AVVSVKEVWL NNDKKG
