ID A0A1F6VEN8_9BACT Unreviewed; 795 AA.
AC A0A1F6VEN8;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:OGI68113.1};
GN ORFNames=A2738_02935 {ECO:0000313|EMBL:OGI68113.1};
OS Candidatus Nomurabacteria bacterium RIFCSPHIGHO2_01_FULL_42_15.
OC Bacteria; Candidatus Nomurabacteria.
OX NCBI_TaxID=1801742 {ECO:0000313|EMBL:OGI68113.1, ECO:0000313|Proteomes:UP000178235};
RN [1] {ECO:0000313|EMBL:OGI68113.1, ECO:0000313|Proteomes:UP000178235}
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:OGI68113.1}.
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; MFTS01000005; OGI68113.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1F6VEN8; -.
DR Proteomes; UP000178235; 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 6..278
FT /note="5'-3' exonuclease"
FT /evidence="ECO:0000259|SMART:SM00475"
FT DOMAIN 544..752
FT /note="DNA-directed DNA polymerase family A palm"
FT /evidence="ECO:0000259|SMART:SM00482"
SQ SEQUENCE 795 AA; 89722 MW; 76E7DC0E231ADDEA CRC64;
MSTTNNKPKT LVLLDAHAII HRAYHALPEF LSSKGEPTGA LYGLASMLMK IVTDLKPDYI
VACYDLPGKT FRHEAYDAYK AGRAKTDDAL IVQLKNSRAI FEAFNVPIYD AKGFEADDVL
GTICEKYKKD QNLKIIIASG DMDAMQLVDD KKVQVYTLKK GINDTILYDE DAIVNRFGFK
PNLLPDYKGL RGDASDNIIG IKGIGEKTAT ILIKNFGSIE EIYKKLKKDS ELFSDAGCSP
RVIELLKNNE EEAMFSKTLA KIRTDAPIDF SIPSKTFWEN ADLKKIEKVF ALFEFRSLFG
RLKNFFSSQK TQEKNVLLNV SSPKIDSIKL QEASIALWLI NSEISNPQLD DILMFAGADS
FDVAYEYIFK KLKENNLDKV FEEIERPIMH IVKEMEDYGI LIDKKYFENL SAEYHKELDK
LTAKIYKIAE IEFNINSPKQ IGEVLFGKMG IKSPGKSAKK SASGNFSTKV SVLEELEETN
PIITEILSYR ELQKLLSTYI DVIPKMAGPD SRLHAKFLQN GSTTGRFSSQ DPNLQNLPIK
TELGKRIRGG FVAGAGSKLC AFDYSQIELR VAAMLSGDKK MTEIFREGKD IHAGVASFVF
GVSIEEVDRE MRRKAKVINF GIIYGMGVTA LRKNLGGTRE EAQKFYDNYF NQFSGVRNYL
EEVKKFALEN FFTETLFGRR RYFSNINSRI PFLKNMAERT ATNAPIQGTA ADIIKLAIRY
VEEDLREAGL EGKVHLILQI HDELVYEIEE SVLTKAGEII KNAMRNVLAR SYLRYKTDIP
LEVHSGSGDN FGEVK
//
