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Database: UniProt
Entry: A0A3N4NHF1_9FLAO
LinkDB: A0A3N4NHF1_9FLAO
Original site: A0A3N4NHF1_9FLAO 
ID   A0A3N4NHF1_9FLAO        Unreviewed;       945 AA.
AC   A0A3N4NHF1;
DT   13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT   13-FEB-2019, sequence version 1.
DT   27-MAR-2024, entry version 25.
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   ECO:0000313|EMBL:RPD95852.1};
GN   ORFNames=EGM88_11575 {ECO:0000313|EMBL:RPD95852.1};
OS   Aureibaculum marinum.
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Aureibaculum.
OX   NCBI_TaxID=2487930 {ECO:0000313|EMBL:RPD95852.1, ECO:0000313|Proteomes:UP000270856};
RN   [1] {ECO:0000313|EMBL:RPD95852.1, ECO:0000313|Proteomes:UP000270856}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BH-SD17 {ECO:0000313|EMBL:RPD95852.1,
RC   ECO:0000313|Proteomes:UP000270856};
RA   Ji X.;
RT   "Aureibaculum marinum gen. nov., sp. nov., a member of the family
RT   Flavobacteriaceae isolated from the Bohai Sea.";
RL   Submitted (NOV-2018) 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}.
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:RPD95852.1}.
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DR   EMBL; RPFJ01000015; RPD95852.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A3N4NHF1; -.
DR   OrthoDB; 9806424at2; -.
DR   Proteomes; UP000270856; 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:UP000270856};
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          352..533
FT                   /note="3'-5' exonuclease"
FT                   /evidence="ECO:0000259|SMART:SM00474"
FT   DOMAIN          702..909
FT                   /note="DNA-directed DNA polymerase family A palm"
FT                   /evidence="ECO:0000259|SMART:SM00482"
FT   REGION          294..317
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        299..313
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   945 AA;  107289 MW;  3856A43374F6F4BA CRC64;
     MSNQKRLFLL DAYALIFRGY YAFIKNPIIN SKGMDTSAIM GFMNSLLDVI KREQPDHLAV
     CFDKGGSVDR VEMFAEYKAN RDETPEAIKI AVPYIQEILK AMHIPIMVKE GFEADDVIGT
     LAKKAEKEGY QTFMVTPDKD FAQLVSENIF MYRPRFGGGY ETWGIPEVLE KFGVTDPLQV
     IDFLAMKGDA IDNIPGLPGV GDKTAKKFLA AYGSIEGLFE NSHELKGKMK EKVEANVELG
     LLSKKLATIM LDVPVEFDAK DFELNTPDIS KVKEIFEELE FRRLMVNLTN TFSPKEENTD
     IKPQTEKNKP EAKNNPSENV QFDLFAAPGS GNSTQKTEAN GYNTIKNTSH FYQFANTPLS
     RKLLIQQLLA QKSVCFDTET TGLKSLEVEL IGIAFSWEHN KGFYVHFPKN QEDTQQILEE
     FRPFFENESI EKVGHNLKYD IKVLSNYNMP VKGKLFDTMI AHYLINPDMR HSMDILAETY
     LNYQPVSITE LIGKKGKNQG NMRDVDLEKL TEYAVEDADI TLQLKTHFTK ELENGNLTDL
     FGKVEMPLVA VLSAMEIEGI NINIDFLKEL SVALSKDIER LEKGIYEQAG EEFNLASPKQ
     LGPILFDKLK LVDKPKKTKT GQYSTAEDVL TYLAKDHQII RDIQEFRQYK KLQSTYVDAL
     PNEVNPKTHR IHTVYAQAVA ATGRLSSNNP NLQNIPIRTE RGREVRKAFI PRDENYTLLA
     ADYSQIELRI IAALSQEENM INAFKNHEDI HASTAAKVFN VPLSEVSREQ RSNAKTVNFG
     IIYGVSAFGL SNQTTLSRSE AKELIDTYYK TYPKLRTYMD GQIHFARENG YVETVLGRRR
     YLKDINSRNA VVRGAAERNA VNAPIQGSAA DIIKLAMINI YNRFQKEQFK SKMLLQVHDE
     LVFDAHNDEL ETITPIIKTE MENAYKLIVP LDVEIGLGKN WLEAH
//
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