ID A0A1F6E2V5_9BACT Unreviewed; 793 AA.
AC A0A1F6E2V5;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:OGG67907.1};
GN ORFNames=A3C95_00210 {ECO:0000313|EMBL:OGG67907.1};
OS Candidatus Kaiserbacteria bacterium RIFCSPHIGHO2_02_FULL_56_30.
OC Bacteria; Candidatus Kaiserbacteria.
OX NCBI_TaxID=1798499 {ECO:0000313|EMBL:OGG67907.1, ECO:0000313|Proteomes:UP000177107};
RN [1] {ECO:0000313|EMBL:OGG67907.1, ECO:0000313|Proteomes:UP000177107}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=27774985; DOI=10.1038/ncomms13219;
RA Anantharaman K., Brown C.T., Hug L.A., Sharon I., Castelle C.J.,
RA Probst A.J., Thomas B.C., Singh A., Wilkins M.J., Karaoz U., Brodie E.L.,
RA Williams K.H., Hubbard S.S., Banfield J.F.;
RT "Thousands of microbial genomes shed light on interconnected biogeochemical
RT processes in an aquifer system.";
RL Nat. Commun. 7:13219-13219(2016).
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:OGG67907.1}.
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DR EMBL; MFLM01000019; OGG67907.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1F6E2V5; -.
DR STRING; 1798499.A3C95_00210; -.
DR Proteomes; UP000177107; 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:0016788; F:hydrolase activity, acting on ester bonds; IEA:UniProt.
DR GO; GO:0006261; P:DNA-templated DNA replication; IEA:InterPro.
DR CDD; cd08637; DNA_pol_A_pol_I_C; 1.
DR CDD; cd09898; H3TH_53EXO; 1.
DR CDD; cd09859; PIN_53EXO; 1.
DR Gene3D; 3.30.70.370; -; 1.
DR Gene3D; 1.10.150.20; 5' to 3' exonuclease, C-terminal subdomain; 2.
DR Gene3D; 3.40.50.1010; 5'-nuclease; 1.
DR InterPro; IPR020046; 5-3_exonucl_a-hlix_arch_N.
DR InterPro; IPR002421; 5-3_exonuclease.
DR InterPro; IPR036279; 5-3_exonuclease_C_sf.
DR InterPro; IPR019760; DNA-dir_DNA_pol_A_CS.
DR InterPro; IPR001098; DNA-dir_DNA_pol_A_palm_dom.
DR InterPro; IPR043502; DNA/RNA_pol_sf.
DR InterPro; IPR020045; DNA_polI_H3TH.
DR InterPro; IPR002298; DNA_polymerase_A.
DR InterPro; IPR008918; HhH2.
DR InterPro; IPR029060; PIN-like_dom_sf.
DR PANTHER; PTHR10133; DNA POLYMERASE I; 1.
DR PANTHER; PTHR10133:SF62; DNA POLYMERASE THETA; 1.
DR Pfam; PF01367; 5_3_exonuc; 1.
DR Pfam; PF02739; 5_3_exonuc_N; 1.
DR Pfam; PF00476; DNA_pol_A; 1.
DR PRINTS; PR00868; DNAPOLI.
DR SMART; SM00475; 53EXOc; 1.
DR SMART; SM00279; HhH2; 1.
DR SMART; SM00482; POLAc; 1.
DR SUPFAM; SSF47807; 5' to 3' exonuclease, C-terminal subdomain; 1.
DR SUPFAM; SSF56672; DNA/RNA polymerases; 1.
DR SUPFAM; SSF88723; PIN domain-like; 1.
DR PROSITE; PS00447; DNA_POLYMERASE_A; 1.
PE 3: Inferred from homology;
KW DNA damage {ECO:0000256|ARBA:ARBA00022763};
KW DNA repair {ECO:0000256|ARBA:ARBA00023204};
KW DNA replication {ECO:0000256|ARBA:ARBA00022705};
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW DNA-directed DNA polymerase {ECO:0000256|ARBA:ARBA00022932};
KW Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 9..278
FT /note="5'-3' exonuclease"
FT /evidence="ECO:0000259|SMART:SM00475"
FT DOMAIN 543..751
FT /note="DNA-directed DNA polymerase family A palm"
FT /evidence="ECO:0000259|SMART:SM00482"
SQ SEQUENCE 793 AA; 89035 MW; 5B41BC97032019F8 CRC64;
MAKKTKDKKR LVLLDTHAII HRAYHALPEF TGPGGQPTGA LYGLAAMLIK IIKELKPDYL
AATYDLAGPT VRHEAYGGYK AMRAKIDDSL SAQINESRKV FEAFSIPIYE RAGFEADDLL
GTIAHTMSTE KGIDVIIASG DMDALQLVDD ARVRVYTLKR GLNDTILYDE KAVKARYGFG
PKLIADYKGL CGDPSDNIKG VPGVGDKTAT ELITKFGSIE DMYKKLAKDE NAFTKKGVKP
RTIELLKKHK EDAEFSKSLA LIRTDAPIAF ALSPRPWREG VSADKVLELF DTLGFRSLRD
RARGALGAPR GEHEGAGELF PEEKVDPERF KEAQVMLWLL ASEFTNPTLP DLLAYAKAHT
FDEAYHALEK SIAETGCLKE VYAHIEKPLI DIVTAMEERG VLIDPAILEA LAREYRAELE
KIERRIYTVA GREFNISSPQ QLGAVLFDEL ELVPERHKVT PGGARSTRES ELEKLRGEHP
IIADILEYRE LKKLLSTYIE NLPPLLDTDN RLHAEFVQTG TTTGRMASQN PNLQNIPLHS
PRGKAIRNAF VAPRGFSLIA LDYSQIELRI AAVLSGDEKL RAVFRAGRDV HREVAAMVFG
VPHEKVDLEM RRRAKVINFG ILYGMGVNAL RAALGVTTVE AHKFYDDYFR TFKTLTEYLE
RTKGFARKHG YTETLFGRRR QFPEMRSPLP YVRAQAERMA INAPMQGTQA DIIKLAMVRV
DEWLKRENLR EETHLLLQVH DELVYEVRSE KAEEIGAKIK EIMESVLPRE KANDVPIIAV
VKTGKNWGEM TTV
//
