ID A0A3R8Z2J7_9GAMM Unreviewed; 787 AA.
AC A0A3R8Z2J7;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 16.
DE RecName: Full=DNA polymerase {ECO:0000256|RuleBase:RU000442};
DE EC=2.7.7.7 {ECO:0000256|RuleBase:RU000442};
GN ORFNames=EGK14_10185 {ECO:0000313|EMBL:RRZ92162.1};
OS Erwinia sp. 198.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Erwiniaceae; Erwinia.
OX NCBI_TaxID=2022746 {ECO:0000313|EMBL:RRZ92162.1, ECO:0000313|Proteomes:UP000273595};
RN [1] {ECO:0000313|EMBL:RRZ92162.1, ECO:0000313|Proteomes:UP000273595}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=198 {ECO:0000313|EMBL:RRZ92162.1,
RC ECO:0000313|Proteomes:UP000273595};
RA D'Souza A.W., Potter R.F., Wallace M., Shupe A., Patel S., Sun S., Gul D.,
RA Kwon J.H., Andleeb S., Burnham C.-A.D., Dantas G.;
RT "Transmission dynamics of multidrug resistant bacteria on intensive care
RT unit surfaces.";
RL Submitted (OCT-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 ECO:0000256|RuleBase:RU000442};
CC -!- SIMILARITY: Belongs to the DNA polymerase type-B family.
CC {ECO:0000256|ARBA:ARBA00005755, ECO:0000256|RuleBase:RU000442}.
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:RRZ92162.1}.
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DR EMBL; RHUM01000006; RRZ92162.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3R8Z2J7; -.
DR OrthoDB; 5807460at2; -.
DR Proteomes; UP000273595; Unassembled WGS sequence.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003887; F:DNA-directed DNA polymerase activity; IEA:UniProtKB-KW.
DR GO; GO:0000166; F:nucleotide binding; IEA:InterPro.
DR GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
DR CDD; cd05784; DNA_polB_II_exo; 1.
DR CDD; cd05537; POLBc_Pol_II; 1.
DR Gene3D; 2.40.50.590; -; 2.
DR Gene3D; 1.10.132.60; DNA polymerase family B, C-terminal domain; 1.
DR Gene3D; 3.90.1600.10; Palm domain of DNA polymerase; 2.
DR Gene3D; 3.30.420.10; Ribonuclease H-like superfamily/Ribonuclease H; 1.
DR InterPro; IPR006172; DNA-dir_DNA_pol_B.
DR InterPro; IPR017964; DNA-dir_DNA_pol_B_CS.
DR InterPro; IPR006133; DNA-dir_DNA_pol_B_exonuc.
DR InterPro; IPR006134; DNA-dir_DNA_pol_B_multi_dom.
DR InterPro; IPR043502; DNA/RNA_pol_sf.
DR InterPro; IPR042087; DNA_pol_B_thumb.
DR InterPro; IPR023211; DNA_pol_palm_dom_sf.
DR InterPro; IPR012337; RNaseH-like_sf.
DR InterPro; IPR036397; RNaseH_sf.
DR PANTHER; PTHR10322; DNA POLYMERASE CATALYTIC SUBUNIT; 1.
DR PANTHER; PTHR10322:SF23; DNA POLYMERASE DELTA CATALYTIC SUBUNIT; 1.
DR Pfam; PF00136; DNA_pol_B; 1.
DR Pfam; PF03104; DNA_pol_B_exo1; 1.
DR Pfam; PF21474; DNApolII_N; 1.
DR PRINTS; PR00106; DNAPOLB.
DR SMART; SM00486; POLBc; 1.
DR SUPFAM; SSF56672; DNA/RNA polymerases; 1.
DR SUPFAM; SSF53098; Ribonuclease H-like; 1.
DR PROSITE; PS00116; DNA_POLYMERASE_B; 1.
PE 3: Inferred from homology;
KW DNA replication {ECO:0000256|RuleBase:RU000442};
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000256|RuleBase:RU000442};
KW DNA-directed DNA polymerase {ECO:0000256|ARBA:ARBA00022932,
KW ECO:0000256|RuleBase:RU000442};
KW Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695,
KW ECO:0000256|RuleBase:RU000442};
KW Reference proteome {ECO:0000313|Proteomes:UP000273595};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU000442}.
FT DOMAIN 205..280
FT /note="DNA-directed DNA polymerase family B exonuclease"
FT /evidence="ECO:0000259|Pfam:PF03104"
FT DOMAIN 380..758
FT /note="DNA-directed DNA polymerase family B
FT multifunctional"
FT /evidence="ECO:0000259|Pfam:PF00136"
SQ SEQUENCE 787 AA; 89878 MW; 9B5DA2D8C340D521 CRC64;
MNDARAGFLL TRHWRDTPNG TEIVLWLATD DGPQRIVLPP QESVAFIPQQ QQLAQAETLL
RAEKDIRLTP LTLKDFRQRP VAGLYCKQYR QLQKLEKLLR ENGVVVYEAD IRPPDRFLME
RFITAPVWFS GQQVGGSLTQ ARLKPNPDYR PPLKWVSLDI ETTRHGELYC IGLEGCGQRV
VYMLGPENGD ASRLDFRLEY VASRPALLEK LNAWFAEHDP DVLIGWNVVQ FDLRMLQKHA
DRYGIPLRLG RNNEALEWRE HGFKPGIYFA QATGRLIIDG IEALKSAFWD FPSFSLESVS
RELLGEGKAI NNPWDRMQEI DQRFAEDKPA LAHYNLKDCE LVTRIFQRTE IMPFLLERAT
VNGLPADRHG GSVASFSHLY LPRMHRAGYV APNMGEVAPE ASPGGYVMDS RPGLYDSVLV
LDYKSLYPSI IRTFLIDPVG LAEGMAHPDD SESVSGFRGA RFSRTLHCLP EIVGQIWQGR
ETAKKHGNKP LSQALKIIMN ALYGVLGTSA CRFFDPRLAS SITLRGHEIM RQTRELIEAE
GYDVIYGDTD STFVWLKTPH DEASAAAIGR RLVEKINAWW QQHLQETLGL TSALELEYET
HFSRFLMPTI RGAEQGSKKR YAGLIREGDQ ERMVFKGLET VRTDWTPLAK NFQQALYLRI
FKRQPYQDYI RETVRQLLDG ELDEQLTYSK KLRRPLEDYQ RNVPPHVRAA RLADEQNRQL
GRPLQYQKGG RICYVIATSG PEPLEARLTP LDYDHYLSRQ LQPVAEGILP FVQDDFATLV
TGQLGLF
//
