ID A0A1Q5U187_9GAMM Unreviewed; 782 AA.
AC A0A1Q5U187;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=DNA polymerase {ECO:0000256|RuleBase:RU000442};
DE EC=2.7.7.7 {ECO:0000256|RuleBase:RU000442};
GN ORFNames=Xentx_02205 {ECO:0000313|EMBL:OKP06235.1};
OS Xenorhabdus thuongxuanensis.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Morganellaceae; Xenorhabdus.
OX NCBI_TaxID=1873484 {ECO:0000313|EMBL:OKP06235.1, ECO:0000313|Proteomes:UP000186277};
RN [1] {ECO:0000313|EMBL:OKP06235.1, ECO:0000313|Proteomes:UP000186277}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=30TX1 {ECO:0000313|EMBL:OKP06235.1,
RC ECO:0000313|Proteomes:UP000186277};
RA Kaempfer P., Tobias N.J., Phan Ke L., Bode H.B., Glaeser S.P.;
RT "Xenorhabdus thuongxuanensis sp. nov. and Xenorhabdus eapokensis sp. nov.,
RT isolated from Steinernema species.";
RL Submitted (SEP-2016) 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:OKP06235.1}.
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DR EMBL; MKGR01000014; OKP06235.1; -; Genomic_DNA.
DR RefSeq; WP_074020276.1; NZ_MKGR01000014.1.
DR AlphaFoldDB; A0A1Q5U187; -.
DR OrthoDB; 5807460at2; -.
DR Proteomes; UP000186277; 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; -; 1.
DR Gene3D; 3.30.70.2250; -; 1.
DR Gene3D; 1.10.132.60; DNA polymerase family B, C-terminal domain; 1.
DR Gene3D; 1.10.287.690; Helix hairpin bin; 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 Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU000442}.
FT DOMAIN 81..296
FT /note="DNA-directed DNA polymerase family B exonuclease"
FT /evidence="ECO:0000259|Pfam:PF03104"
FT DOMAIN 377..754
FT /note="DNA-directed DNA polymerase family B
FT multifunctional"
FT /evidence="ECO:0000259|Pfam:PF00136"
SQ SEQUENCE 782 AA; 90536 MW; 5C4688878547E5F9 CRC64;
MQINHVEQGL ILTRHWKDTP SGIELVYWLA TEAGARRITI PRQKAVAFAP QHDLPKIKPL
LTQERHCELK ALPLKDFNRQ PVAALYCPHY HQLQHLEKIF KEQNIPLYEA DIRPPDRFMM
ERFITAPVWF SQKPDGSYQM KPNPTYRPNL QWVSLDIETS QHGELYSIGL AGCGEKTVFM
LGPAQDDQQD LDFKLEYVAS RSIMLEKLNE WLAHYDPDAI IGWNLIQFDL RVLQQHAERY
NVPLKFGRNQ ALLEWREHGF NPGHFFASTE GRLIIDGIDA LKTATWNFPS FSLEYVAQQL
LGEGKAVDNP YDRMDEINRR FQQDKPALAH YNLQDCILVN RIFEKADLMA FLLERATVTG
LAVDRSGGSV SAFTHLYLPK MHRIGYVAPV QPTYFDDNSP GGFVMDSFPG LYDSVLVLDY
KSLYPSIIRT FLIDPVGMVE GLANTDSEHA VPGFRQAFFS RTQHCLPDIV TQIWHERDKA
KKQQNAPLSQ ALKIIMNAFY GVLGASGCHF FDPRLTSSIT MRGHQIMHQT RKLIESQGYQ
VIYGDTDSTF VWLKRPHSEE EACQIGLSLT QFVNQWWRNH LKTELNLEST LELEFETHYR
RFLMPTVRGM EQGSKKRYAG LSGDKVTFKG LETVRTDWTP LAQIFQKELY TLIFHQQPHQ
HYIREYIAKT LAGEFDDRLV YRKRLRRKLS DYQRNVPPHV RAARLADEYN QMHNRPLQYQ
NGGWINYVIT QAGPEPLENQ TSAPDYEHYI NKQLKPIADA ILPFIQDDFM PLLTGQMSIS
FE
//
