ID A0A1G2UMZ6_9BACT Unreviewed; 798 AA.
AC A0A1G2UMZ6;
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:OHB10784.1};
GN ORFNames=A3H60_01755 {ECO:0000313|EMBL:OHB10784.1};
OS Candidatus Zambryskibacteria bacterium RIFCSPLOWO2_02_FULL_44_12b.
OC Bacteria; Candidatus Zambryskibacteria.
OX NCBI_TaxID=1802772 {ECO:0000313|EMBL:OHB10784.1, ECO:0000313|Proteomes:UP000177202};
RN [1] {ECO:0000313|EMBL:OHB10784.1, ECO:0000313|Proteomes:UP000177202}
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:OHB10784.1}.
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DR EMBL; MHWP01000008; OHB10784.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G2UMZ6; -.
DR STRING; 1802772.A3H60_01755; -.
DR Proteomes; UP000177202; 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 3..263
FT /note="5'-3' exonuclease"
FT /evidence="ECO:0000259|SMART:SM00475"
FT DOMAIN 546..754
FT /note="DNA-directed DNA polymerase family A palm"
FT /evidence="ECO:0000259|SMART:SM00482"
SQ SEQUENCE 798 AA; 89953 MW; 4A725EA4200139A4 CRC64;
MTKKLILFDA HAIIHRAYHA FPEFSTSKGE PTGALYGLST MLIKIINELK PDYLVACFDL
PGPTHRHEAL ETYKAGRAKI DNNLVLQLER AKDVFTAFGI PIYSHPGFEA DDIIGTIVEY
VKGRTLEIII ASGDMDTLQL VDGKKVQVYT LKKGISDTIL YDEKKVSARF GFGPKLLVDY
KGLRGDPSDN IVGVKGIGEK TATILIQEFG TIENIYKNLE KVKLSDRIKT LLEENEKEAL
FSKTLATIRT DAPIHFILPK EWKENLDVDK LINFFKKLEF RTMGERVKGL LTSAGEKNSR
ALPSKAGLRR DSNFPLPPSY EERELCLALW VIDSNITNPN LEDVMRFTKA LSVDEARKII
EKELDKHKVR KVFEDIEKPI MPVVEKMNKW GVKIDKKVLE SLSAKYHGEL ERLEKAIWKE
AGEEPARTAE GVQSGGFNIN SPKVLSDILF NKLGLAEKSQ KKTSTGALST KESELEKLRD
KHPIISMILE YRELAKLLST YIDAIPPQLD KNSRLHSTFL QAGSTTGRMA SNSPNLQNIP
NKTLLGRAIR NAFVAEKGFK LVSLDYSQIE LRIAAILSED KKLIEIFKNG EDVHTGVAMR
VFKVPKEQVD KGMRTRAKTI NFGILYGMGV NALKVNLGVD RKEAQDFYDK YFKTFTGLAE
YIDKIKSDTK HKGYTETMFG RRRYFSGIKS PLPYVRAQAE RMAVNAPMQG TQADLIKIAM
RNIDEHIKSE KHEKDIHLIL QVHDELVYEV KDSLVNEVAK HFKQLMEGVL PKEKTLGVPI
IAEVQSGDNW GEMGKVAG
//
