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Database: UniProt
Entry: A0A0P0E6L6_9MICO
LinkDB: A0A0P0E6L6_9MICO
Original site: A0A0P0E6L6_9MICO 
ID   A0A0P0E6L6_9MICO        Unreviewed;       568 AA.
AC   A0A0P0E6L6;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   27-MAR-2024, entry version 23.
DE   SubName: Full=3'-5' exonuclease {ECO:0000313|EMBL:ALJ20467.1};
GN   ORFNames=AOA12_11335 {ECO:0000313|EMBL:ALJ20467.1};
OS   Microbacterium sp. No. 7.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC   Microbacterium.
OX   NCBI_TaxID=1714373 {ECO:0000313|EMBL:ALJ20467.1, ECO:0000313|Proteomes:UP000059097};
RN   [1] {ECO:0000313|EMBL:ALJ20467.1, ECO:0000313|Proteomes:UP000059097}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=No. 7 {ECO:0000313|EMBL:ALJ20467.1,
RC   ECO:0000313|Proteomes:UP000059097};
RA   Ohtsubo Y., Nagata Y., Numata M., Tsuchikane K., Hosoyama A., Yamazoe A.,
RA   Tsuda M., Fujita N., Kawai F.;
RT   "Complete genome sequence of a polypropylene glycol-degrading strain
RT   Microbacterium sp. No. 7.";
RL   Submitted (SEP-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; CP012697; ALJ20467.1; -; Genomic_DNA.
DR   RefSeq; WP_054682756.1; NZ_CP012697.1.
DR   AlphaFoldDB; A0A0P0E6L6; -.
DR   STRING; 1714373.AOA12_11335; -.
DR   KEGG; mio:AOA12_11335; -.
DR   PATRIC; fig|1714373.3.peg.2339; -.
DR   OrthoDB; 4414061at2; -.
DR   Proteomes; UP000059097; 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   SMART; SM00482; POLAc; 1.
DR   SUPFAM; SSF56672; DNA/RNA polymerases; 1.
PE   3: Inferred from homology;
KW   Exonuclease {ECO:0000313|EMBL:ALJ20467.1};
KW   Hydrolase {ECO:0000313|EMBL:ALJ20467.1};
KW   Nuclease {ECO:0000313|EMBL:ALJ20467.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000059097}.
FT   DOMAIN          305..525
FT                   /note="DNA-directed DNA polymerase family A palm"
FT                   /evidence="ECO:0000259|SMART:SM00482"
SQ   SEQUENCE   568 AA;  60476 MW;  DDF91FD6E501B506 CRC64;
     MSAPPWTIVA RDDDGAVLVT VDGRGAEQAR RRVALAELPS ALGDDVRPVW NDTAQWYPAL
     LDAGMTLARC RDLRLSHAIL RDSALVDAPP LRAATAWDAG PSTVSGAPSP ALFELDELAP
     GIPDRVDEVL AEFARQQAAV DGSRDPGRLR LLLAAESAGA LVAAELHAAG VPWDRGVHEA
     ILTDVLGGRP GPGSHAPRAE ELATRIRELL GDPQASLDSQ PKLLRALHRV GVLASSTSRW
     ELAEHDHPVV APLLEYKRLT RLESANGWNW LDEWAGGGRF RPVYVPGGVV TGRWASSGGG
     ALQLPRQLRP AVRADEGWLL VVADVAQLEP RVLAAMSGDL ALADAARGTD LYQGIVASGV
     VGTRQEAKIA VLGAMYGGTT GDSGRLVPAL RRAYPRAMAL VDEAARVGEE GGVVSTWLGR
     SAPPPPASWH RVQQRAADPD ADDADRARAV RAARDRGRFT RNFVVQGTAA EWALAWLADL
     RGRLAALPVV PEDRRAPLSG VALGGRAHLA FFLHDEIVLH APEEQAELAA QAVRDAADAA
     TRLLFGTFPV DFPLDLRISR DAGKALLE
//
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