ID A0A1M6FUY0_9FIRM Unreviewed; 896 AA.
AC A0A1M6FUY0;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-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=SAMN02745751_01549 {ECO:0000313|EMBL:SHJ01505.1};
OS Dethiosulfatibacter aminovorans DSM 17477.
OC Bacteria; Bacillota; Tissierellia; Dethiosulfatibacter.
OX NCBI_TaxID=1121476 {ECO:0000313|EMBL:SHJ01505.1, ECO:0000313|Proteomes:UP000184052};
RN [1] {ECO:0000313|EMBL:SHJ01505.1, ECO:0000313|Proteomes:UP000184052}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 17477 {ECO:0000313|EMBL:SHJ01505.1,
RC ECO:0000313|Proteomes:UP000184052};
RA Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL Submitted (NOV-2016) to the EMBL/GenBank/DDBJ databases.
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 -!- SUBUNIT: Single-chain monomer with multiple functions.
CC {ECO:0000256|RuleBase:RU004460}.
CC -!- SIMILARITY: Belongs to the DNA polymerase type-A family.
CC {ECO:0000256|ARBA:ARBA00007705, ECO:0000256|RuleBase:RU004460}.
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DR EMBL; FQZL01000009; SHJ01505.1; -; Genomic_DNA.
DR RefSeq; WP_073049009.1; NZ_FQZL01000009.1.
DR AlphaFoldDB; A0A1M6FUY0; -.
DR STRING; 1121476.SAMN02745751_01549; -.
DR OrthoDB; 9806424at2; -.
DR Proteomes; UP000184052; 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; cd06140; DNA_polA_I_Bacillus_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; 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; 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.
DR PROSITE; PS00447; DNA_POLYMERASE_A; 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 Reference proteome {ECO:0000313|Proteomes:UP000184052};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU004460}.
FT DOMAIN 4..262
FT /note="5'-3' exonuclease"
FT /evidence="ECO:0000259|SMART:SM00475"
FT DOMAIN 315..487
FT /note="3'-5' exonuclease"
FT /evidence="ECO:0000259|SMART:SM00474"
FT DOMAIN 654..860
FT /note="DNA-directed DNA polymerase family A palm"
FT /evidence="ECO:0000259|SMART:SM00482"
SQ SEQUENCE 896 AA; 102812 MW; 864BAABD8804BB34 CRC64;
MEKKKFLILD GNSILFRAFY ALPPLKNKKG IYTNAVYGFL SMMYKLLDEY KPDYIVTAFD
PKKPTFRHEK YKEYKAGRAK APNELVMQFG LIRDVLELHG IKHLEIEGYE ADDVAGSLSK
FAAAQGIEVY MVTSDRDYLQ LVDDDVYVLI TKKGVTNTVK YTRELMEEEY GMTPKQFIDL
KALMGDSSDN IPGVKGVGEK TGMKLIHQFE TLEGIYENIG EVKGKLKEKL ESEKMQAYMS
RDLATIVTEI PMECSMEDFL YKEVDGDELM EMYKEFGFRQ FMNRLKSEDK QLSLFSMGEG
DKEEDRKPES KKVEVVEIDS KKLYGEINSA SQMAIKVLYD GERALYSKPV AMGVMIDDKR
VFYIEDNIEE SIVSIKEILE NPSVEKFSHD IKDEIILFDK LGISLEGVKF DTMIGKYLLE
PSESSYSIDK LVFEYLDLDI KGEKDYLGSG KNKKVFSGIE PEDRKEFLSN QLSGVWNIKD
KMEKQIMEAD MDSLYNEIEL PLVEIMASME ILGFKINTEE LKAIGERLGR KIEILEEIIY
DFADEVFNIN SPKQLGEILF DKLGLPVIKK TKTGYSTNAE VLDKLKLKHP IVLKILEYRQ
LAKLKSTYVD GLLNVVDKET GRVHSSFKQT IASTGRISST EPNLQNIPVK TEEGRELRKV
FVHEVGRKLV DADYSQIELR VLAHLSDDEN LKSAFINNED IHRKTAAQVF HVEEDEVTSI
MRSRAKAVNF GIVYGISDYG LSRDLDIPRK ESKEYIENYL NFFGGVKDYM DNIVKQGKKD
GYVDTIFGRR RYIPELNSRN FNIRALGERL ALNTPVQGTA ADIIKKAMIN VYFRLKENNM
KSRLILQIHD ELIIEAVEEE LEDVKLILKN EMEKAAELKV PLTVDMNIGD TWYDTK
//
