EX7L_CYAP4
ID EX7L_CYAP4 Reviewed; 424 AA.
AC B8HMX6;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 03-MAR-2009, sequence version 1.
DT 25-MAY-2022, entry version 68.
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};
GN OrderedLocusNames=Cyan7425_3117;
OS Cyanothece sp. (strain PCC 7425 / ATCC 29141).
OC Bacteria; Cyanobacteria; Oscillatoriophycideae; Oscillatoriales;
OC Cyanothecaceae; Cyanothece; unclassified Cyanothece.
OX NCBI_TaxID=395961;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 7425 / ATCC 29141;
RX PubMed=21972240; DOI=10.1128/mbio.00214-11;
RA Bandyopadhyay A., Elvitigala T., Welsh E., Stockel J., Liberton M., Min H.,
RA Sherman L.A., Pakrasi H.B.;
RT "Novel metabolic attributes of the genus Cyanothece, comprising a group of
RT unicellular nitrogen-fixing Cyanobacteria.";
RL MBio 2:E214-E214(2011).
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; CP001344; ACL45445.1; -; Genomic_DNA.
DR RefSeq; WP_012628508.1; NC_011884.1.
DR AlphaFoldDB; B8HMX6; -.
DR STRING; 395961.Cyan7425_3117; -.
DR EnsemblBacteria; ACL45445; ACL45445; Cyan7425_3117.
DR KEGG; cyn:Cyan7425_3117; -.
DR eggNOG; COG1570; Bacteria.
DR HOGENOM; CLU_023625_3_1_3; -.
DR OMA; WPAVRFE; -.
DR OrthoDB; 1371775at2; -.
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..424
FT /note="Exodeoxyribonuclease 7 large subunit"
FT /id="PRO_1000200668"
SQ SEQUENCE 424 AA; 47239 MW; 624789C9562E673E CRC64;
MSFTQPNLLF PPTVLSVGGL TQYIQTLLEQ DEELMQVWVT GEVSSASQHR SGLFFTLQDP
DERVALRCIV WASQLEKLSI LPVPGEQVIL LGRIRVYPQR GEYQLMVWQA LPAGEGLMAL
RYRQLRDRLE TEGLFDPARK RPLPPHPQTI AVVTSPQAAA WGDIQRTLSH RYPGLRVLLS
PALVQGDQAP DSIVAAIERV EKDGRAEVLI LSRGGGATED MACFNHERVV RAIAECSIPV
IAGIGHQRDE SLADLVADVH VHTPTAAAQL AVPDLAELYT EHCQRLDHLI TAGQTRLALA
QNQLQHQNRR LKRLPLERQL VQEGRAIAHL KQQLIQTVSQ QLQQRLTHQQ LLAQKLQSLD
PRAILQRGYA IARRQNGQIL RTIAALQEGD DLTLQLSDGQ VKVQVRKIMA AGTGHEAESE
QMEL
