EX7L_CHLFF
ID EX7L_CHLFF Reviewed; 555 AA.
AC Q253S0;
DT 11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT 18-APR-2006, sequence version 1.
DT 25-MAY-2022, entry version 90.
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=CF0696;
OS Chlamydia felis (strain Fe/C-56) (Chlamydophila felis).
OC Bacteria; Chlamydiae; Chlamydiales; Chlamydiaceae;
OC Chlamydia/Chlamydophila group; Chlamydia.
OX NCBI_TaxID=264202;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Fe/C-56;
RX PubMed=16766509; DOI=10.1093/dnares/dsi027;
RA Azuma Y., Hirakawa H., Yamashita A., Cai Y., Rahman M.A., Suzuki H.,
RA Mitaku S., Toh H., Goto S., Murakami T., Sugi K., Hayashi H., Fukushi H.,
RA Hattori M., Kuhara S., Shirai M.;
RT "Genome sequence of the cat pathogen, Chlamydophila felis.";
RL DNA Res. 13:15-23(2006).
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; AP006861; BAE81468.1; -; Genomic_DNA.
DR RefSeq; WP_011458246.1; NC_007899.1.
DR AlphaFoldDB; Q253S0; -.
DR STRING; 264202.CF0696; -.
DR PRIDE; Q253S0; -.
DR KEGG; cfe:CF0696; -.
DR eggNOG; COG1570; Bacteria.
DR HOGENOM; CLU_023625_5_0_0; -.
DR OMA; KIACTIW; -.
DR OrthoDB; 1371775at2; -.
DR Proteomes; UP000001260; 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; 2.
DR Pfam; PF02601; Exonuc_VII_L; 2.
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..555
FT /note="Exodeoxyribonuclease 7 large subunit"
FT /id="PRO_0000303781"
SQ SEQUENCE 555 AA; 64000 MW; 473411EF9959B4AC CRC64;
MTTSSPPQAV TTLTESIKNL LESNFCHVVV KGELSNVSLQ PSGHLYFGIK DSRSFLNGAF
FHFKSKYFDR RPKDGDSVII HGKLTVYAPR GQYQIVAHAL VYAGEGDLLQ KFEETKKRLA
AEGYFALEKK QTLPNIPQSI GVITSPTGAV IQDILRVLSR RCYQYKILIY PVTVQGATAA
KEISRAIEEM NKENLADVLI LARGGGSIED LWAFNEEIVV KAIDASSIPI ISAIGHETDY
TLCDFAADVR APTPSAAAEI VCQSSEQQIQ VFKSYLRYLN AHSQQLLSGK IKQIQQWKRY
LDHVDFFRSA HQSLDYLCLS VERSIQTKLS QYKQRYMQYA RWLQSDVLQR MTYRLHDLWK
MIVQAFHNRL TAAKHLCMQK KKNLTFHNTQ QFIQKLDLWK QQLHRALTQR LGYCSQSLTH
QQTLLKHFTI KLNQQFTKGK HTLNLLQKRL TRTFANTVDE HRENYVRSRE NLIFSLHHLV
ERNREKYYTL SKQLTLLNPK NVFKRGYAML FDFNENFAII SAKSLHKHSC VRVRLQDGEA
TLTVTDIQNF ETQES
