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Database: UniProt
Entry: A0A0F7N1G5_9ACTN
LinkDB: A0A0F7N1G5_9ACTN
Original site: A0A0F7N1G5_9ACTN 
ID   A0A0F7N1G5_9ACTN        Unreviewed;       556 AA.
AC   A0A0F7N1G5;
DT   22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT   22-JUL-2015, sequence version 1.
DT   27-MAR-2024, entry version 26.
DE   SubName: Full=3'-5' exonuclease {ECO:0000313|EMBL:AKH81283.1};
GN   ORFNames=AA958_02830 {ECO:0000313|EMBL:AKH81283.1};
OS   Streptomyces sp. CNQ-509.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=444103 {ECO:0000313|EMBL:AKH81283.1, ECO:0000313|Proteomes:UP000034283};
RN   [1] {ECO:0000313|EMBL:AKH81283.1, ECO:0000313|Proteomes:UP000034283}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CNQ-509 {ECO:0000313|EMBL:AKH81283.1,
RC   ECO:0000313|Proteomes:UP000034283};
RA   Ruckert C., Albersmeier A., Leipoldt F., Winkler A., Zeyhle P.,
RA   Kalinowski J., Heide L., Kaysser L.;
RT   "Complete Genome Sequence of Streptomyces sp. CNQ-509, a Prolific Producer
RT   of Meroterpenoid Chemistry.";
RL   Submitted (MAY-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) =
CC         diphosphate + DNA(n+1); Xref=Rhea:RHEA:22508, Rhea:RHEA-COMP:17339,
CC         Rhea:RHEA-COMP:17340, ChEBI:CHEBI:33019, ChEBI:CHEBI:61560,
CC         ChEBI:CHEBI:173112; EC=2.7.7.7;
CC         Evidence={ECO:0000256|ARBA:ARBA00024632};
CC   -!- SIMILARITY: Belongs to the DNA polymerase type-A family.
CC       {ECO:0000256|ARBA:ARBA00007705}.
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DR   EMBL; CP011492; AKH81283.1; -; Genomic_DNA.
DR   RefSeq; WP_047014646.1; NZ_CP011492.1.
DR   AlphaFoldDB; A0A0F7N1G5; -.
DR   STRING; 444103.AA958_02830; -.
DR   KEGG; strc:AA958_02830; -.
DR   PATRIC; fig|444103.5.peg.605; -.
DR   OrthoDB; 4414061at2; -.
DR   Proteomes; UP000034283; Chromosome.
DR   GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR   GO; GO:0003887; F:DNA-directed DNA polymerase activity; IEA:InterPro.
DR   GO; GO:0004527; F:exonuclease activity; IEA:UniProtKB-KW.
DR   GO; GO:0006261; P:DNA-templated DNA replication; IEA:InterPro.
DR   CDD; cd06444; DNA_pol_A; 1.
DR   Gene3D; 3.30.70.370; -; 1.
DR   Gene3D; 1.10.150.20; 5' to 3' exonuclease, C-terminal subdomain; 1.
DR   InterPro; IPR001098; DNA-dir_DNA_pol_A_palm_dom.
DR   InterPro; IPR043502; DNA/RNA_pol_sf.
DR   InterPro; IPR002298; DNA_polymerase_A.
DR   PANTHER; PTHR10133; DNA POLYMERASE I; 1.
DR   PANTHER; PTHR10133:SF62; DNA POLYMERASE THETA; 1.
DR   Pfam; PF00476; DNA_pol_A; 1.
DR   PRINTS; PR00868; DNAPOLI.
DR   SMART; SM00482; POLAc; 1.
DR   SUPFAM; SSF56672; DNA/RNA polymerases; 1.
PE   3: Inferred from homology;
KW   Exonuclease {ECO:0000313|EMBL:AKH81283.1};
KW   Hydrolase {ECO:0000313|EMBL:AKH81283.1};
KW   Nuclease {ECO:0000313|EMBL:AKH81283.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000034283}.
FT   DOMAIN          313..515
FT                   /note="DNA-directed DNA polymerase family A palm"
FT                   /evidence="ECO:0000259|SMART:SM00482"
FT   REGION          432..456
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   556 AA;  59533 MW;  2142F8218518747B CRC64;
     MRWAMADGPR GGVIVCPVDA AGDPQGPEHT YPHPAHALRH HPTADRWIWS STAAFYPRLL
     DAGETVPRCH DVEAAEAILL GHEGMWGLPR SLAAAWARLR GLPVPKDPPP RSFAGEPQPT
     LFDAAPARPH GTDDLPALLA VHAAQQDRVA ASAHPHRLRL LLAAESAGML VAAEMHHAGL
     PWRADVHDAL LTELLGGRYP GGLEPPRLAA LADDVSRAFG ERVRPDLPAE VVRAFRKAGV
     RITSTRKWEL QDIDHPAVAP LLEYKKLYRL HTAHGWSWLQ TWVHGGRFRP EYLPGGAMSG
     RWTTHGGGAL QIPRVVRRAV VADEGWRLVV ADADQMEPRV LAAVSGDAGL MAAADGTRDL
     YEALAARAFA GGRAEAKLAL LGAIYGQTSG DALTYLADLR RRFPAAVAYV DEAARAGEEG
     RLVRSHLGRT CAPSEAADDG EAGLPQEDDG GGAAARGGAA ARARGRFTRN FVVQASAAEW
     ALCLLAALRQ ELAGMRAELV FFQHDEVIVH CPEAEAPAVE KALAVASARA GEVMFGQTPV
     VFSFTTAVVE CYADAR
//
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