ID A0A2H9LIZ6_9ARCH Unreviewed; 494 AA.
AC A0A2H9LIZ6;
DT 28-FEB-2018, integrated into UniProtKB/TrEMBL.
DT 28-FEB-2018, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=DNA-directed DNA polymerase {ECO:0000256|ARBA:ARBA00012417};
DE EC=2.7.7.7 {ECO:0000256|ARBA:ARBA00012417};
DE Flags: Fragment;
GN ORFNames=COS86_08365 {ECO:0000313|EMBL:PIU58651.1};
OS Candidatus Bathyarchaeota archaeon CG07_land_8_20_14_0_80_47_9.
OC Archaea; Candidatus Bathyarchaeota.
OX NCBI_TaxID=1974385 {ECO:0000313|EMBL:PIU58651.1, ECO:0000313|Proteomes:UP000228782};
RN [1] {ECO:0000313|EMBL:PIU58651.1, ECO:0000313|Proteomes:UP000228782}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CG07_land_8_20_14_0_80_47_9 {ECO:0000313|EMBL:PIU58651.1};
RA Probst A.J., Ladd B., Jarett J.K., Geller-Mcgrath D.E., Sieber C.M.,
RA Emerson J.B., Anantharaman K., Thomas B.C., Malmstrom R., Stieglmeier M.,
RA Klingl A., Woyke T., Ryan C.M., Banfield J.F.;
RT "Depth-based differentiation of microbial function through sediment-hosted
RT aquifers and enrichment of novel symbionts in the deep terrestrial
RT subsurface.";
RL Submitted (SEP-2017) 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 -!- 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:PIU58651.1}.
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DR EMBL; PEWI01000242; PIU58651.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2H9LIZ6; -.
DR Proteomes; UP000228782; 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-EC.
DR GO; GO:0000166; F:nucleotide binding; IEA:InterPro.
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; 1.
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 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 SUPFAM; SSF56672; DNA/RNA polymerases; 1.
PE 4: Predicted;
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125}.
FT DOMAIN 91..464
FT /note="DNA-directed DNA polymerase family B
FT multifunctional"
FT /evidence="ECO:0000259|Pfam:PF00136"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:PIU58651.1"
SQ SEQUENCE 494 AA; 55538 MW; 569011076A12D161 CRC64;
GGKTFFSYGR VYHKAPTRRL FGRVHIDVNN TFIYTACGLE GLIEVSRTCR VPLQRAARAS
IGSIMSSLQL YTAWKEGILI PWKKTEPESF KSGWELLVAD RGGFIFEPKL GFHTDVVEVD
FASMFPMLML TRNISAETVL CKCCPDSKLR VPELGYNICE KRKGIVPKTL DLLLRKRSKY
KSLMKEVEDK KLKHAYNMRQ AVLKWILVTC FGYLGYRNAR FGKVDAHIAV CAFARDGLLK
TAAMAEQHGF EVIHGIVDSL WLKKQGVSPR EVADFCREVS SAVGVQLSVE GKYRWIVFLP
SKVLEGVPVL NRYYGVFENG EVKMRGIEAR RGDTPRFLYK AQMEMIKKLA EANSLESFKA
KIAEALHVLG DYADELIDGH VDVEELLVTK RLSKAPSGYN HDVFQAVAAK QLEKAGFEVH
AGQTVQYLIV NAGSRRANGR VVAAQLLKPS TRYDAKEYLQ LLISAGETLL GVFGYTKSMI
EAETLYHEKQ VLLS
//
