EX7L_MYCMS
ID EX7L_MYCMS Reviewed; 469 AA.
AC Q6MUD1;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 111.
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=MSC_0101;
OS Mycoplasma mycoides subsp. mycoides SC (strain PG1).
OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma.
OX NCBI_TaxID=272632;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PG1;
RX PubMed=14762060; DOI=10.1101/gr.1673304;
RA Westberg J., Persson A., Holmberg A., Goesmann A., Lundeberg J.,
RA Johansson K.-E., Pettersson B., Uhlen M.;
RT "The genome sequence of Mycoplasma mycoides subsp. mycoides SC type strain
RT PG1T, the causative agent of contagious bovine pleuropneumonia (CBPP).";
RL Genome Res. 14:221-227(2004).
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; BX293980; CAE76753.1; -; Genomic_DNA.
DR RefSeq; NP_975111.1; NC_005364.2.
DR AlphaFoldDB; Q6MUD1; -.
DR SMR; Q6MUD1; -.
DR STRING; 272632.MSC_0101; -.
DR PRIDE; Q6MUD1; -.
DR EnsemblBacteria; CAE76753; CAE76753; MSC_0101.
DR KEGG; mmy:MSC_0101; -.
DR PATRIC; fig|272632.4.peg.105; -.
DR eggNOG; COG1570; Bacteria.
DR HOGENOM; CLU_023625_3_1_14; -.
DR OMA; WPAVRFE; -.
DR Proteomes; UP000001016; 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..469
FT /note="Exodeoxyribonuclease 7 large subunit"
FT /id="PRO_1000200674"
SQ SEQUENCE 469 AA; 54427 MW; 354062854EFDFCCD CRC64;
MEKILTVQEL NEALKTLIEN KQEFKDIYVQ GELSNLTFNK SGHIYFSIKE QDAAINCMMW
KTNAYKIQSL NLEDGMQIIC YGRLTYYIPT GRVSFEVRDI QIHGIGDLQK IFEQRYKELE
QKGWFDPNLK KSIPEFVKNV GIITADSGAA IYDLIRTVHR RLPLINIYLF PAQVQGDKAE
IDITNKIKQA NNFKIDLDVL IVGRGGGSYE DLWAFNELEV LQAIKNSHIP IISAVGHEPD
WVLSDYVADI RAATPTAAGE LVSKSIIEIK NQLKHYYQNY KTLILNKLDF FNEKINNYKK
DQTKYIKDNF SFKYLQLKQL SIDNTKWTKN KIDSVIYKLE DYKHSINNSI IHIINSQNKA
LKNYLIADEQ KILNYLKKQI SEFNYTISSF KGHINQILKY EELSFDTLEN KLNSLDPLKP
LQNGYSIVTN LNHQKIRSYK QVKLNEDLKV ILTDSKLTVT IKEVKTNEQ
