ID Q47QP2_THEFY Unreviewed; 929 AA.
AC Q47QP2;
DT 13-SEP-2005, integrated into UniProtKB/TrEMBL.
DT 13-SEP-2005, sequence version 1.
DT 27-MAR-2024, entry version 140.
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 OrderedLocusNames=Tfu_1189 {ECO:0000313|EMBL:AAZ55227.1};
OS Thermobifida fusca (strain YX).
OC Bacteria; Actinomycetota; Actinomycetes; Streptosporangiales;
OC Nocardiopsaceae; Thermobifida.
OX NCBI_TaxID=269800 {ECO:0000313|EMBL:AAZ55227.1};
RN [1] {ECO:0000313|EMBL:AAZ55227.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=YX {ECO:0000313|EMBL:AAZ55227.1};
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA Hammon N., Israni S., Pitluck S., Di Bartolo G., Chain P., Schmutz J.,
RA Larimer F., Land M., Lykidis A., Richardson P.;
RT "Complete sequence of Thermobifida fusca YX.";
RL Submitted (JUL-2005) 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; CP000088; AAZ55227.1; -; Genomic_DNA.
DR AlphaFoldDB; Q47QP2; -.
DR STRING; 269800.Tfu_1189; -.
DR KEGG; tfu:Tfu_1189; -.
DR eggNOG; COG0258; Bacteria.
DR eggNOG; COG0749; Bacteria.
DR HOGENOM; CLU_004675_0_0_11; -.
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; 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; 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 31..293
FT /note="5'-3' exonuclease"
FT /evidence="ECO:0000259|SMART:SM00475"
FT DOMAIN 340..518
FT /note="3'-5' exonuclease"
FT /evidence="ECO:0000259|SMART:SM00474"
FT DOMAIN 685..892
FT /note="DNA-directed DNA polymerase family A palm"
FT /evidence="ECO:0000259|SMART:SM00482"
FT REGION 1..33
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..22
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 929 AA; 102085 MW; C2FEE55DE54AC7F5 CRC64;
MSSAHPRIRR VVNTQATPEQ TRPAETGEGG GRPRLLLVDG HSMAFRAFYA LPAEKFVNSA
GQATNAIYGF TSMLVKLLRE EQPTHIAVAW DRSEPTFRHE EYAEYKAGRS ETPPEFPSQV
GLLQELLGLI GVTSLSVPGY EADDIIATLT TRGLAEGMDV LIASGDRDTF QLVGEHCTVL
YPGRSLSDLI RMTPEAVEAK YAVPPERYCD LAALVGEKSD NLPGVPGVGP KTAAKWLAKY
GSLDALVAHA HEIGGKAGQN LRDHLDDVLR NQRLNRLATD VELGVDVTGM TLGHWNRDGV
NLLFDNLEFA STLRDRLFAV LSEQAGDDSA EPVQDEGFSV ELVDPAPGTL GDWLAAEIAA
GARTGVALEW SGERDGDIIR LALAVPSGRA VCLDPTQLDP ADEAALTAWL ADPAYPKVLH
GVKWALRALW ARGWTLDGVE SDTAIAAYLL EPGRRNFELA TLCLRYLGRE LTEHNAEGAQ
LTLDLEGTGD DQDTARRELA LRALATVELA LALDAELTRR EGLDLLHNLE LPLAEVLARM
EDAGIAADLT YLRDLEAEFA AAVRQAVDEA HRLVGREFNL GSPKQLQQIL FDELGLPKTK
RIKTGYTTDA DALAWLAAQT DNELPVILLR HRDQTKLRTT VEGLIKTIAE DGRIHTTFHQ
TVTATGRLSS AEPNLQNIPV RTDAGRRIRR AFVVGEGYEQ LLTADYSQIE LRIMAHLSED
EALIEAFHSG FDFHAQIASR VFRIPVDQVD GEARARIKAM NYGLAYGLSD YGLAQQLGIS
PKEARVLMEE YFSHFGKVRD YLEAVVVRAR REGYTATILG RRRYLPDLNS DNRQRREMAE
RMALNAPIQG SAADIIKLAM LRVDRALREN GLASRMLLQV HDELVLEVAP GELDTVRELV
VEHMSQAQQL RVPLAVSVGV GPNWHDAAH
//
