ID A0A399JGH8_9MICC Unreviewed; 600 AA.
AC A0A399JGH8;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE SubName: Full=Bifunctional 3'-5' exonuclease/DNA polymerase {ECO:0000313|EMBL:RII43787.1};
GN ORFNames=DWB68_00725 {ECO:0000313|EMBL:RII43787.1};
OS Galactobacter valiniphilus.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC Galactobacter.
OX NCBI_TaxID=2676122 {ECO:0000313|EMBL:RII43787.1, ECO:0000313|Proteomes:UP000265419};
RN [1] {ECO:0000313|EMBL:RII43787.1, ECO:0000313|Proteomes:UP000265419}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JZ R-35 {ECO:0000313|EMBL:RII43787.1,
RC ECO:0000313|Proteomes:UP000265419};
RA Hahne J., Isele D., Lipski A.;
RT "Arthrobacter sp. nov., isolated from raw cow's milk with high bacterial
RT count.";
RL Submitted (JUL-2018) 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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:RII43787.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; QQXK01000001; RII43787.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A399JGH8; -.
DR Proteomes; UP000265419; Unassembled WGS sequence.
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; -; 2.
DR Gene3D; 1.10.150.20; 5' to 3' exonuclease, C-terminal subdomain; 2.
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:RII43787.1};
KW Hydrolase {ECO:0000313|EMBL:RII43787.1};
KW Nuclease {ECO:0000313|EMBL:RII43787.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000265419}.
FT DOMAIN 313..559
FT /note="DNA-directed DNA polymerase family A palm"
FT /evidence="ECO:0000259|SMART:SM00482"
FT REGION 414..499
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 476..490
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 600 AA; 63174 MW; 8A1B08EAB825FE72 CRC64;
MTAYLLAPLA GEALAQPRGV VVPLDATGRP TGPGTQAPRA ELASVVAGIE AADPAARWVW
EDSRFAYPEL LEAGVEVRRC HDLGLTALLL HGAVDYVPTP GLPPRKLPEL PAEALATEQD
ALFSALTPDP PTPQALAEEY AAQLEALASA GARGRTLHLL ASLDSAGSLI AEEMRRDGVP
WDRAEHERLL AERLGPRVPH GARPAKLADL TEVLQDLLDA PRLNPDSQPE LLRALRGAGL
DARSTRRWDL EELHHPAIEP LLRYKKLQRL LTANGWAWLD AWVRGTRFHP EYVVAGVVTG
RWASQGGGAM QIPHDVRSAV RADPGHVLVV ADASQLEPRV LAAMSADHAL AEAARGRDLY
QSIADKVFGG DREMAKVAML GAMYGGTTGP SAAMAPRLAA AYPRATALLE EAARTGERGG
TVHTWLGRTS PRPAPFGGGT GSGFGPDGPG PGDEAPDAVG PGSRDTGMQA NAGGSGALGG
QGNSLSPSQD GAPRAAGDPA AAARAWGRFT RNFVVQGTAA EWAECWMADL RSRLRATAPG
SRQVFFLHDE IMVHAPESEA VDVEIALRAA ADGAARLIFG DIPVDFPISV GIARDYATAK
//