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Database: UniProt
Entry: A0A1H0YBQ2_9FLAO
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Original site: A0A1H0YBQ2_9FLAO 
ID   A0A1H0YBQ2_9FLAO        Unreviewed;       948 AA.
AC   A0A1H0YBQ2;
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=SAMN05421664_0623 {ECO:0000313|EMBL:SDQ12557.1};
OS   Chryseobacterium soldanellicola.
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales; Weeksellaceae;
OC   Chryseobacterium group; Chryseobacterium.
OX   NCBI_TaxID=311333 {ECO:0000313|EMBL:SDQ12557.1, ECO:0000313|Proteomes:UP000199627};
RN   [1] {ECO:0000313|EMBL:SDQ12557.1, ECO:0000313|Proteomes:UP000199627}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 17072 {ECO:0000313|EMBL:SDQ12557.1,
RC   ECO:0000313|Proteomes:UP000199627};
RA   de Groot N.N.;
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; FNKL01000001; SDQ12557.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1H0YBQ2; -.
DR   STRING; 311333.SAMN05421664_0623; -.
DR   Proteomes; UP000199627; 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   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          10..271
FT                   /note="5'-3' exonuclease"
FT                   /evidence="ECO:0000259|SMART:SM00475"
FT   DOMAIN          357..538
FT                   /note="3'-5' exonuclease"
FT                   /evidence="ECO:0000259|SMART:SM00474"
FT   DOMAIN          706..912
FT                   /note="DNA-directed DNA polymerase family A palm"
FT                   /evidence="ECO:0000259|SMART:SM00482"
SQ   SEQUENCE   948 AA;  107615 MW;  3A52C72B3A2CD0F5 CRC64;
     MENMDATQDK RLFLIDAYAM IFRGYHAMYK SQRYTNSGME TTAIFGFMNS LIELIRKEKP
     THLAVVFDVG QASVRTNDYA DYKANRSETP EAIKTGVPYI HRILEAMHVP RLGIEGYEAD
     DVIGTIACKA EKEGYTTFMV TPDKDFGQLV TDKIKIYKPG YKGGDVQILG VEEINAKYEI
     EDPKQVIDYL AMMGDASDNI PGLEGVGEKT AMKFLKEFGS IENLLANTDK LKGKLKEKVE
     ASAERGILSK KLATIICDVP IEFHQEQYDL ETPDFEKVKE IFDEIEFRRL YENLYRAFAP
     STTETTVVTE VEVTISTETA QQKVAQAVGQ LDLFATYEEL DQATSTKSTI EHNDHLYQFI
     DNPKAQKILV QNLLKQKVVC FDTETTSLNE LEAELVGMSF SYKKGLAYYI PLSEDQGEVL
     QTLEIFRPFF EKEDLLKVAH NLKFDYKILK QYDITVKGAM FDTMIAHYLL NPDGRHGMDY
     LSEVYLNYKP VSIETIIGKK GKNQGTFRDA DLRTQTDYAA EDADITFQLY ELFAPQLKKE
     NLEDLFFNIE MPLMEVLAKM ELAGISLDEK WLAQESIDLE NDLRQLESKI FEFSGEEFNM
     NSPKQLGEVL FEKMQLDPKA KKTKTGQYAT SEDVLQKLAS KHEIIKHILE YRTYQKLKST
     YVDALPSQID KDERVHTNFS QTTAATGRLA SVNPNLQNIP IRTLRGQQIR GAFVSAEGKK
     IISADYSQIE LRLIAEISGE ENMIKAFQNG EDIHASTAAK LFKIPLEEVS KTQRSQAKTV
     NFGIIYGQGA FALAEQTGLS RTEAKQMIEA YFETYPKLKE YMAEQVNKAR QLGYVETILG
     RKRHLKDINS NNFVVRGHAE RNAVNAPVQG SAADVVKMAM IKIQKELEKE KLETKMLLQV
     HDELVFESPI NEIELATNII KIEMESAIET QVPLLVEVGV GNNWLEAH
//
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