ID A0A1F6RDX4_9BACT Unreviewed; 951 AA.
AC A0A1F6RDX4;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE RecName: Full=DNA polymerase I {ECO:0000256|ARBA:ARBA00020311, ECO:0000256|RuleBase:RU004460};
DE EC=2.7.7.7 {ECO:0000256|ARBA:ARBA00012417, ECO:0000256|RuleBase:RU004460};
GN Name=polA {ECO:0000256|RuleBase:RU004460};
GN ORFNames=A3B68_06255 {ECO:0000313|EMBL:OGI18831.1};
OS Candidatus Melainabacteria bacterium RIFCSPHIGHO2_02_FULL_34_12.
OC Bacteria; Candidatus Melainabacteria.
OX NCBI_TaxID=1801607 {ECO:0000313|EMBL:OGI18831.1, ECO:0000313|Proteomes:UP000198265};
RN [1] {ECO:0000313|EMBL:OGI18831.1, ECO:0000313|Proteomes:UP000198265}
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 -!- FUNCTION: In addition to polymerase activity, this DNA polymerase
CC exhibits 5'-3' exonuclease activity. {ECO:0000256|RuleBase:RU004460}.
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:RU004460};
CC -!- SIMILARITY: Belongs to the DNA polymerase type-A family.
CC {ECO:0000256|ARBA:ARBA00007705, ECO:0000256|RuleBase:RU004460}.
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:OGI18831.1}.
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DR EMBL; MFRM01000020; OGI18831.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1F6RDX4; -.
DR STRING; 1801607.A3B68_06255; -.
DR Proteomes; UP000198265; Unassembled WGS sequence.
DR GO; GO:0008408; F:3'-5' exonuclease activity; IEA:InterPro.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003887; F:DNA-directed DNA polymerase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-UniRule.
DR GO; GO:0006261; P:DNA-templated DNA replication; IEA:UniProtKB-UniRule.
DR CDD; cd08637; DNA_pol_A_pol_I_C; 1.
DR CDD; cd06139; DNA_polA_I_Ecoli_like_exo; 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 Gene3D; 3.30.420.10; Ribonuclease H-like superfamily/Ribonuclease H; 1.
DR InterPro; IPR002562; 3'-5'_exonuclease_dom.
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; IPR001098; DNA-dir_DNA_pol_A_palm_dom.
DR InterPro; IPR043502; DNA/RNA_pol_sf.
DR InterPro; IPR020045; DNA_polI_H3TH.
DR InterPro; IPR018320; DNA_polymerase_1.
DR InterPro; IPR002298; DNA_polymerase_A.
DR InterPro; IPR008918; HhH2.
DR InterPro; IPR029060; PIN-like_dom_sf.
DR InterPro; IPR012337; RNaseH-like_sf.
DR InterPro; IPR036397; RNaseH_sf.
DR NCBIfam; TIGR00593; pola; 1.
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 Pfam; PF01612; DNA_pol_A_exo1; 1.
DR PRINTS; PR00868; DNAPOLI.
DR SMART; SM00474; 35EXOc; 1.
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 SUPFAM; SSF53098; Ribonuclease H-like; 1.
PE 3: Inferred from homology;
KW DNA damage {ECO:0000256|ARBA:ARBA00022763, ECO:0000256|RuleBase:RU004460};
KW DNA repair {ECO:0000256|ARBA:ARBA00023204, ECO:0000256|RuleBase:RU004460};
KW DNA replication {ECO:0000256|ARBA:ARBA00022705,
KW ECO:0000256|RuleBase:RU004460};
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000256|RuleBase:RU004460};
KW DNA-directed DNA polymerase {ECO:0000256|ARBA:ARBA00022932,
KW ECO:0000256|RuleBase:RU004460}; Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695,
KW ECO:0000256|RuleBase:RU004460};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU004460}.
FT DOMAIN 4..266
FT /note="5'-3' exonuclease"
FT /evidence="ECO:0000259|SMART:SM00475"
FT DOMAIN 345..540
FT /note="3'-5' exonuclease"
FT /evidence="ECO:0000259|SMART:SM00474"
FT DOMAIN 710..915
FT /note="DNA-directed DNA polymerase family A palm"
FT /evidence="ECO:0000259|SMART:SM00482"
SQ SEQUENCE 951 AA; 108398 MW; B72DF1FA28994AD6 CRC64;
MSEQNNTIIL IDAPNLAFRM FFAMERTNMR TLGGIPTWAT YGFLKALFDL LDRTKPKAIA
AAYDCKEPTF RHKAYEEYKA NRPEEMPEEL SVQWPYIREG LESFEIPIYE LPGYEADDVI
GTLAKKAEKN GQNVLILTGD RDAFQLVNDK VKVLVPSKGE LKEYGRDEVY EYWGIWPEQV
VDFKSLSGDA SDNIPGIKGI GEKTAAKLLN EYGTLENIYK NVKNISKKGL QEKIINGEKS
ALLSKKLAAI HTDVPININF KDSHLNMPEM NKLVGFLQKF EFNSFIKRLP KVLASFNEGK
EVDIKNTEKF IVKRTEQMKL DIGDNGKDPH HEDPLEHLKS PDLEVVVIDT EKELEDLTDE
LKKKKIICID LETTSIDTMS CQIVGIGLSW FTGVKDGKDA KDEKIKACYI PIGHNSGKQL
KEETVIKKLK PILENPEVEK IAQNCKFEYK ILKRYGISIG ENVYDTMLAS YVSNPDEKHG
LKDQTAKILG VRMTKIDELI GSGKKQISMA EVDIEKAAPY SVSDTTYTLE LAKHYKKNLD
KSLSKVLEEI ENPLVPVLSE MELNGVRIDV KVLKDLSREI TKKVRELEKY IFEVAKEPFN
INSPQQLGKV LFEKLEIEHE GKVTKSGQYS TDVRTLEALS QHDKTGIITA IIEYRQLSKL
ISTYTDSLPE QINKKTGNIH CDFNQTITTT GRLSSSNPNL QNIPIRSELG KKIRKAFTSS
FDDGMLLSAD YSQIELRILA HMSGDPVLVK AFKAGEDIHK RTAMEIYGVP ENKVTSEMRS
HGKTLNFALI YQQGAFATAR QLDISQKEAQ EFIDKYFESF KKVKPFFENI LDEARKKNYV
ETIYGRRRYF KNLHIRNKAL QREDERAACN APLQGTAADI MKLAMIKVYN ELKNYKSKLI
LQVHDELILD VYPNENNKVE KMLKEAMELE QPLEVPLVVN LSWGKNWYEC G
//
