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Database: UniProt
Entry: A8UER8_9FLAO
LinkDB: A8UER8_9FLAO
Original site: A8UER8_9FLAO 
ID   A8UER8_9FLAO            Unreviewed;       948 AA.
AC   A8UER8;
DT   15-JAN-2008, integrated into UniProtKB/TrEMBL.
DT   15-JAN-2008, sequence version 1.
DT   27-MAR-2024, entry version 93.
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=FBALC1_15342 {ECO:0000313|EMBL:EDP72488.1};
OS   Flavobacteriales bacterium ALC-1.
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales.
OX   NCBI_TaxID=391603 {ECO:0000313|EMBL:EDP72488.1, ECO:0000313|Proteomes:UP000003630};
RN   [1] {ECO:0000313|EMBL:EDP72488.1, ECO:0000313|Proteomes:UP000003630}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ALC-1 {ECO:0000313|EMBL:EDP72488.1,
RC   ECO:0000313|Proteomes:UP000003630};
RA   Azam F., Ferriera S., Johnson J., Kravitz S., Beeson K., Sutton G.,
RA   Rogers Y.-H., Friedman R., Frazier M., Venter J.C.;
RL   Submitted (OCT-2007) 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:EDP72488.1}.
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DR   EMBL; ABHI01000001; EDP72488.1; -; Genomic_DNA.
DR   AlphaFoldDB; A8UER8; -.
DR   STRING; 391603.FBALC1_15342; -.
DR   eggNOG; COG0258; Bacteria.
DR   eggNOG; COG0749; Bacteria.
DR   OrthoDB; 9806424at2; -.
DR   Proteomes; UP000003630; 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:UP000003630};
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          310..339
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   948 AA;  106689 MW;  5F84BE4E79548C62 CRC64;
     MSNQKRLFLV DAYALIFRGY YAFIKNPRIN SKGEDTSAIM GFMNSLLDVI KRERPDHLAV
     CFDKGGSVDR VEMYQEYKAN RDETPEGIKT AVPYIYEILK AMHIPIMVKK GYEADDVIGT
     LAKKAEKEGY KTFMVTPDKD FAQLVSENIF MYRPVFGGGY ETWGIPEVQQ KFEVTDPLQV
     IDYLGMMGDA SDNIPGLPGV GPKTAKKFLA AYGSMEGLLA NTHELKGKMK EKVEANGELG
     LLSKKLATIM LDVPVEFDAK DFELDHPDIE KVKQIFQDLE FRRLTDNFLK TFSAETTAPT
     NEIPEKKVAP KVTTKEQKSA GAGQFSLFGG DDTSNTSEAT SEYTRNTAET SSHFYQSVAP
     GMATKLFVKN LMNQTSVCFD TETTGLNPLT AELVGIAFSW ETGKGFYVPF PEDKNEAQEL
     IEVLRPFFEN DNIEKIGQNL KYDIKVLAKY NVEVKGKLFD TMLAHYLINP DMRHNMDVLA
     ETYLNYTPIS ITELIGKKGK NQLSMREVPL DKQTEYAVED ADITLQLKEH FEKELGEANT
     QKLFNDIELP LLRVLAAMEL EGINLDKDFL NSLSEELNTD IANLEKSIYE AAGEEFNIAS
     PKQLGVILFE KMKLVDKPKK TKTGQYSTAE DVLSYLAKDH KIIQQVLDFR GLSKLKSTYV
     DALPLQVDES TGRVHTDYMQ TVAATGRLSS NNPNLQNIPI RTERGRQVRK AFVPRDENHI
     LLAADYSQIE LRIIAALSKE ETMIEAFKNG EDIHASTASK VFNVPITEVT REQRSNAKTV
     NFGIIYGVSA FGLSNQTDLS RSEAKELIET YYATYPKLRA YMSEQVDFAR DNGYVQTVLG
     RRRYLKDINS RNAVVRGAAE RNAVNAPIQG SAADIIKIAM INIYKKLQTG AYKTKMLLQV
     HDELVFDVYK PELEGLKNLI KTEMENAYEL SVPLDVDLDI GANWLEAH
//
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