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Database: UniProt
Entry: A0A1K2IEA7_9FLAO
LinkDB: A0A1K2IEA7_9FLAO
Original site: A0A1K2IEA7_9FLAO 
ID   A0A1K2IEA7_9FLAO        Unreviewed;       948 AA.
AC   A0A1K2IEA7;
DT   15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT   15-FEB-2017, sequence version 1.
DT   27-MAR-2024, entry version 37.
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=SAMN05428642_1011095 {ECO:0000313|EMBL:SFZ90711.1};
OS   Flaviramulus basaltis.
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Flaviramulus.
OX   NCBI_TaxID=369401 {ECO:0000313|EMBL:SFZ90711.1, ECO:0000313|Proteomes:UP000182544};
RN   [1] {ECO:0000313|EMBL:SFZ90711.1, ECO:0000313|Proteomes:UP000182544}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 18180 {ECO:0000313|EMBL:SFZ90711.1,
RC   ECO:0000313|Proteomes:UP000182544};
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; FPKV01000001; SFZ90711.1; -; Genomic_DNA.
DR   RefSeq; WP_072400707.1; NZ_FPKV01000001.1.
DR   AlphaFoldDB; A0A1K2IEA7; -.
DR   STRING; 369401.SAMN05428642_1011095; -.
DR   OrthoDB; 9806424at2; -.
DR   Proteomes; UP000182544; 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:UP000182544};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU004460}.
FT   DOMAIN          5..265
FT                   /note="5'-3' exonuclease"
FT                   /evidence="ECO:0000259|SMART:SM00475"
FT   DOMAIN          355..536
FT                   /note="3'-5' exonuclease"
FT                   /evidence="ECO:0000259|SMART:SM00474"
FT   DOMAIN          705..912
FT                   /note="DNA-directed DNA polymerase family A palm"
FT                   /evidence="ECO:0000259|SMART:SM00482"
FT   REGION          299..343
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        299..321
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   948 AA;  106592 MW;  43390276A207A9C9 CRC64;
     MSDQKRLFLV DAYALIFRGY YAFIKNPRIN SKGVDTSAIM GFMNSLLDVI KRERPDHLAV
     CFDKGGSADR VEMFEAYKAN RDATPEAIKI AVPYIQDILK AMHIPIMVKE GFEADDVIGT
     LSKQAEKEGY KTFMVTPDKD FAQLVSENIF MYRPVFGGGY ETWGIPEVQK KFEVTDPLQV
     IDFLGMMGDS SDNIPGLPGV GEKTAKKFLA QYGSMENLLA NTHELKGKMK EKIEAAKELG
     MLSKKLATIM LDVPVEFHAE NFEMSHPDIP KVTEIFQELE FRRLIDNFTK AFSVEATAET
     ATQETSSEAK ATPQETKSAG AGQFSLFGAD PSSSKEAEPV SEFTRKTTKT SSHFYQSVAS
     GMATKLFVKN LMNQTSVCFD TETTSLNPLV AELVGIAFSW EVGKGFYLPF PENREEAQEL
     IEQLRPFFES ENIEKIGQNL KYDIKVLAKY NIDVKGKFFD TMLAHYLINP DMRHSMDVLA
     ETYLNYTPIP IEALIGKKGK NQGNMRDVPL EKQTEYAVED ADITLQLKEH FEKELGEANT
     QKLFDDIEIP LLRVLAAMEL EGINLDKDFL NSLSEQLTID IKALETIIYT EAGEEFNIAS
     PKQLGDILFD KMKLVDKPKK TKTGQYATSE DILSYLAKDH EIIQHILDFR GLSKLKSTYV
     DALPNQVEPS TGRVHTDYMQ TVAATGRLSS NNPNLQNIPI RTERGRQVRK AFIPRNEDYT
     LLAADYSQIE LRIIAALSKE ETMIEAFKNG EDIHASTASK VFNVPLEAVT REQRGNAKTV
     NFGIIYGVSA FGLSNQTDLS RGEAKELIDT YYETYPKLRA YMSELVDFAR DNGYVQTVLG
     RRRYLKDINS RNAVVRGAAE RNAVNAPIQG SAADIIKIAM INIYNKLEAG NYKTKMLLQV
     HDELVFDVYK PELKDMKTLI KTEMENAFTL DVPLDVEVGV GADWLEAH
//
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