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Database: UniProt
Entry: V6SAC7_9FLAO
LinkDB: V6SAC7_9FLAO
Original site: V6SAC7_9FLAO 
ID   V6SAC7_9FLAO            Unreviewed;       944 AA.
AC   V6SAC7;
DT   19-FEB-2014, integrated into UniProtKB/TrEMBL.
DT   19-FEB-2014, sequence version 1.
DT   27-MAR-2024, entry version 53.
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=Q767_06845 {ECO:0000313|EMBL:KGO95978.1};
OS   Flavobacterium enshiense DK69.
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Flavobacterium.
OX   NCBI_TaxID=1107311 {ECO:0000313|EMBL:KGO95978.1, ECO:0000313|Proteomes:UP000030149};
RN   [1] {ECO:0000313|Proteomes:UP000030149}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DK69 {ECO:0000313|Proteomes:UP000030149};
RA   Zeng Z., Chen C.;
RL   Submitted (SEP-2013) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KGO95978.1, ECO:0000313|Proteomes:UP000030149}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DK69 {ECO:0000313|EMBL:KGO95978.1,
RC   ECO:0000313|Proteomes:UP000030149};
RX   PubMed=26561515; DOI=10.1186/s40793-015-0084-z;
RA   Zeng Z., Chen C., Du H., Wang G., Li M.;
RT   "High quality draft genomic sequence of Flavobacterium enshiense DK69(T)
RT   and comparison among Flavobacterium genomes.";
RL   Stand. Genomic Sci. 10:92-92(2015).
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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KGO95978.1}.
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DR   EMBL; JRLZ01000005; KGO95978.1; -; Genomic_DNA.
DR   AlphaFoldDB; V6SAC7; -.
DR   STRING; 1107311.Q767_06845; -.
DR   PATRIC; fig|1107311.3.peg.1288; -.
DR   eggNOG; COG0258; Bacteria.
DR   eggNOG; COG0749; Bacteria.
DR   OrthoDB; 9806424at2; -.
DR   Proteomes; UP000030149; 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   Reference proteome {ECO:0000313|Proteomes:UP000030149};
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          350..531
FT                   /note="3'-5' exonuclease"
FT                   /evidence="ECO:0000259|SMART:SM00474"
FT   DOMAIN          701..908
FT                   /note="DNA-directed DNA polymerase family A palm"
FT                   /evidence="ECO:0000259|SMART:SM00482"
SQ   SEQUENCE   944 AA;  106887 MW;  E4CAD9AA3053607F CRC64;
     MSQKRLFLLD AYALIFRGYY AFIKNPRINS KGVDTSAVLG FMNSLLDVIR REKPDHLAVA
     FDKGGSVVRS EMFAEYKANR DATPEAIKIA VPYIQDFLRA MHIPIIEEAG YEADDLIGTL
     AKQAEKEGYQ VFMVTPDKDF GQLVSENIFM YRPARLGNDI EIWGVPEVLE KFEIQDPLQV
     IDYLGMMGDA VDNIPGLPGV GEKTAKKLLA EFGSMENLLD NTDKLKGALK TKIEANKEQG
     ILSKKLATIL LDCPVTFNET DYELSKPDVE KTDALFIELE FRQMRTQFDK LFGGGQEYDE
     INGNGDATPK AAKKTAKNED QFSLFDSGDS EAPAGHHSYY NTLENTNHHY EIVQGNLGVQ
     LFMQNLLQQK SVCFDTETTG IDALNAELVG MSFSWEKGKA FYIPFPENQD EAKALLEKIV
     PFFENEEIEK IGQNIKYDLK ILANYGVTVR GKLFDTMIAH YLINPDMRHN MDVLSETYLK
     YSPMPIENLI GKKGKNQKSM RDVPLEDIKE YAAEDADITL QLKEVFDPKL DSTGTKKLFE
     EIEIPLIEVL AAMEREGIRL DVNYLKSMSK DMDVEIKELE LKIYETAGEK FNLASPKQLG
     EVLFEKMKIG GAKQKKTKTG QYATGEEVLS YLANEHEIVR QILEWRQMVK LQSTYIVSLP
     EQVDEGTNRV HTDYMQTVAA TGRLSSNNPN LQNIPIRTER GRLIRKAFIA RDENYTLLSA
     DYSQIELRVI AAMSGEENMI KAFQHGEDIH KSTAAKVFHV PLEEVTKEQR SHAKTVNFGI
     IYGVSAFGLS NQTNLSRSES AALIDAYYKT YPRLREYIQE QIEFARNHGY VQTVSGRRRY
     LKDINSANAV VRGAAERNAV NAPIQGSAAD IIKIAMINIH KKLISENWKS KMLLQVHDEL
     VFDVHNSELE KIKPLIKFEM ENAFKLAVPF EVDLGTGRDW LEAH
//
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