ID A0A1I7N8C6_9BACT Unreviewed; 934 AA.
AC A0A1I7N8C6;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 28.
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=SAMN05660895_0897 {ECO:0000313|EMBL:SFV30816.1};
OS Thermoflavifilum thermophilum.
OC Bacteria; Bacteroidota; Chitinophagia; Chitinophagales; Chitinophagaceae;
OC Thermoflavifilum.
OX NCBI_TaxID=1393122 {ECO:0000313|EMBL:SFV30816.1, ECO:0000313|Proteomes:UP000199537};
RN [1] {ECO:0000313|Proteomes:UP000199537}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 14807 {ECO:0000313|Proteomes:UP000199537};
RA Varghese N., Submissions S.;
RL Submitted (OCT-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 -!- SIMILARITY: Belongs to the DNA polymerase type-A family.
CC {ECO:0000256|ARBA:ARBA00007705, ECO:0000256|RuleBase:RU004460}.
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DR EMBL; FPCJ01000001; SFV30816.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I7N8C6; -.
DR STRING; 1393122.SAMN05660895_0897; -.
DR OrthoDB; 9806424at2; -.
DR Proteomes; UP000199537; 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; 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 Coiled coil {ECO:0000256|SAM:Coils};
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:UP000199537};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU004460}.
FT DOMAIN 4..265
FT /note="5'-3' exonuclease"
FT /evidence="ECO:0000259|SMART:SM00475"
FT DOMAIN 338..519
FT /note="3'-5' exonuclease"
FT /evidence="ECO:0000259|SMART:SM00474"
FT DOMAIN 688..895
FT /note="DNA-directed DNA polymerase family A palm"
FT /evidence="ECO:0000259|SMART:SM00482"
FT COILED 504..570
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 934 AA; 106436 MW; 00BF2D808B66C517 CRC64;
MAQQKLFLLD AMALIYRAYY ALIRNPRITT YGKNTNAQFG FTSTLFELIQ KEKPTHMAVA
FDTEAPTERH DTYVAYKANR QETPEDILSS IPDIKRIIRA FEIPIIEKDG YEADDIIGTL
ALQAAEQGFE VFMVTADKDY GQLLHNHIYI YKPPYMGNKE EILSAKDICE KWQIQDVKQV
IDILGLMGDS VDNIPGIPGI GEKTATKLIQ QYHSVENVIA HADEIGGKLG EKIKEFADQA
LMSKQLATII TDVPVQFHEE DFRLKEWNKT ELENIFRELE FKTLGKRILG EDFSISPIQP
DLFAPSDAEI AKKADKKNQE ENHPSDHYKT IHDVAHQYFV CDDENAIQQL IKKFETSKNI
SIDTETTHID AMQAELVGMS LCVKPHEAYY IPFDADYKKA TQRLEQLSKL LNRTDVCWIG
HNIKYDMLVL KKYGIELKGS YFDTLIAHYL LHPEGRRSLD DVAMQYLQYA PVSIETLIGK
KGKHQGSMRD VELEKIKEYA AEDADIAFQL KDKLEKELQK NELEKIFYEI ECPLIPVLAE
MEFTGVKIDV DFLREYAKEL SREARQLEEK IYQQAGVRFN IASPKQLGEV LFEKLKLDEN
AKTTRTGQYA TGEEVLIKLA PKHPIVVDIL AYREITKLQS TYVEALPDMM DPKTGKIHTS
YNQTVAVTGR LSSNNPNLQN IPIRTDRGKE IRKAFIPSEK GNRLVSADYS QIELRIVAAM
SGDKNMIEAF QKGWDIHTAT AARVFGVPLD QVTKEMRYRS KSVNFGIIYG QGPFGLAQNL
GISRTEAKEL IDNYFKQYPG IKAYMDAQIA FAKKHGYVQT LMGRKRWLPD IHSSNNTVRG
YAERNAINMP IQGTAADMIK LAMIRIHDKL QQKKLKARMI LQVHDELVLD VPEQEVDVVS
KLVIREMQEA LPLPHDVPVV AEVGVGKNWL EAHA
//
