ID A0A1X6X7G4_9MICO Unreviewed; 926 AA.
AC A0A1X6X7G4;
DT 05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2017, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE RecName: Full=DNA polymerase I {ECO:0000256|RuleBase:RU004460};
DE EC=2.7.7.7 {ECO:0000256|RuleBase:RU004460};
GN Name=polA {ECO:0000256|RuleBase:RU004460};
GN ORFNames=FM110_11145 {ECO:0000313|EMBL:SLM94362.1};
OS Brachybacterium nesterenkovii.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Dermabacteraceae;
OC Brachybacterium.
OX NCBI_TaxID=47847 {ECO:0000313|EMBL:SLM94362.1, ECO:0000313|Proteomes:UP000195981};
RN [1] {ECO:0000313|EMBL:SLM94362.1, ECO:0000313|Proteomes:UP000195981}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CIP104813 {ECO:0000313|EMBL:SLM94362.1,
RC ECO:0000313|Proteomes:UP000195981};
RA Peterson S.W.;
RL Submitted (FEB-2017) 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 -!- SIMILARITY: Belongs to the DNA polymerase type-A family.
CC {ECO:0000256|ARBA:ARBA00007705, ECO:0000256|RuleBase:RU004460}.
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DR EMBL; FWFG01000099; SLM94362.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1X6X7G4; -.
DR Proteomes; UP000195981; Unassembled WGS sequence.
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:0016788; F:hydrolase activity, acting on ester bonds; IEA:UniProt.
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; 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 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 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|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};
KW Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695,
KW ECO:0000256|RuleBase:RU004460};
KW Reference proteome {ECO:0000313|Proteomes:UP000195981};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU004460}.
FT DOMAIN 33..293
FT /note="5'-3' exonuclease"
FT /evidence="ECO:0000259|SMART:SM00475"
FT DOMAIN 682..889
FT /note="DNA-directed DNA polymerase family A palm"
FT /evidence="ECO:0000259|SMART:SM00482"
SQ SEQUENCE 926 AA; 99913 MW; 16B5C6450F6545B5 CRC64;
MPEPVRGSSS VGCPWDTVAM TDAAAPSVPG QDMRLLLVDG HAMAFRAFFA LPADSFTDGR
GQSTNAVYGF ARMMINVVQS ERPTHVAVAF DLPGGTFRDR IYDQYKAGRD ETPEQFHGQI
ALIQQVLDAM GITWLTVEDY EADDIIATLA TRTAAAGGEV LIVSSDRDAI QLVGESVTLL
QPVKGVTELR RMDPAAVEEK YQVAPELYPD LAALVGESAD NLPGVPGVGP KTAAKWIAAH
GGLAGILAHA DEITGKAGQS LRDHVADVER NRRMNEAVRD LDLPTDPSRY ALGRGDRAAL
AGVFDDLAFG PTIRRDVPDL LLADDAAQQD AAEERAAEVM AELVRPDAER LATLLSDELA
AGAALEVEGS WELGEGDASA IALATADVIA VVDVAELDDA AERALAAWLA DPAVPKTAYD
TKASAHRLRA RGLQVAGWAM DLAIAEFLCR PDQRPTDLPG LALRHLQEDL ASSTAAAQQS
LDLEGTQDDA RAEQLGRRAD AVRRLEPLLR ADLVSHAVEP LLDDLELPLA DVLGRMEAVG
VAVDDGVLAD LDEQHARQQE AVAQSAFSHI GGDPINLGSP KQLQEVLFER LGMPKTRRTK
TGYTTNAEAL EDLFAQTGHP FLADLLAHRD VTKMRQIIET LRRSISPAGR IHTSFQQNVA
ATGRLSSIGP NLQNIPARTE EGRRIRSAFH ASAGFETLLT ADYSQIEMRI MAHLSGDEGL
IEAFRSGEDL HRYVASRVFD VAPEDVDPAM RSKTKAVSYG LAYGLSAFGL ARQLHISQKE
ATALRDGYFE RFGGVRDYLR ASVETARETG YTETILGRRR YLPDLTSDNR QRRENAERVA
LNSPIQGSAA DIIKLAMLRV DAALREASLA SRVLLQVHDE LVVEIAPGER EAVTSLIVEG
MGSAYELSVP LEVGVGTGRT WLDAAH
//
