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Database: UniProt
Entry: A0A1W6ML22_9FLAO
LinkDB: A0A1W6ML22_9FLAO
Original site: A0A1W6ML22_9FLAO 
ID   A0A1W6ML22_9FLAO        Unreviewed;       950 AA.
AC   A0A1W6ML22;
DT   05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2017, sequence version 1.
DT   27-MAR-2024, entry version 34.
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=BST97_09900 {ECO:0000313|EMBL:ARN78277.1};
OS   Nonlabens spongiae.
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Nonlabens.
OX   NCBI_TaxID=331648 {ECO:0000313|EMBL:ARN78277.1, ECO:0000313|Proteomes:UP000193431};
RN   [1] {ECO:0000313|EMBL:ARN78277.1, ECO:0000313|Proteomes:UP000193431}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JCM 13191 {ECO:0000313|EMBL:ARN78277.1,
RC   ECO:0000313|Proteomes:UP000193431};
RA   Kumagai Y.;
RT   "Trade-off between light-utilization and light-protection in marine
RT   flavobacteria.";
RL   Submitted (NOV-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; CP019344; ARN78277.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1W6ML22; -.
DR   STRING; 331648.BST97_09900; -.
DR   OrthoDB; 9806424at2; -.
DR   Proteomes; UP000193431; Chromosome.
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:UP000193431};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU004460}.
FT   DOMAIN          9..270
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          707..914
FT                   /note="DNA-directed DNA polymerase family A palm"
FT                   /evidence="ECO:0000259|SMART:SM00482"
FT   REGION          308..344
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        308..334
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   950 AA;  107011 MW;  DF8235E10D6DEFBE CRC64;
     MTNDGTDDKR LFLLDAYALI FRGYYALIKN PRINSKGMDT SAIMGFTNSL FDVIRREKPE
     YLAVAFDKEG SAERTELYED YKANRDETPE AIRIAIPYIQ KILKAMHIPI VEIAGVEADD
     LIGTLSKQAE KEGFTVYMVT PDKDYAQLVS ENIFMYRPAR MGNGIEIWGI PEVQKRFEVE
     RPEQVIDYLG MMGDASDNIP GLPGVGDKTA KKFLKQFGSM EGLLDNTDQL KGKLKEKVIA
     NAELGRLSKQ LATIKLDCDV QFNAKNYTLD DPDVEQVHEV FDELEFRRAK ETMAKIFAPD
     GVPGVNYKEA SSASSSSSSS DSNSDGQFSL FDTPGSGTAA EADATGRKTL ATTDHLYQIV
     EEGLGMSLFL KKLMQQKSVC FDTETTSLDP LVAELVGIAF SWEAGKGFYL PFPEERDKAQ
     EIVNQLKPFF ESNEIEKIGQ NLKYDIKVLD KYDVEVAAPA FDTMLAHYLI NPDMRHNMDV
     LAETYLNYTP QSITELISKK GKNQKSMRDV ELEKQKEYAV EDADITLQLK QYFVKELDSA
     GTNKLFTEIE MPLVQVLADM EIEGINLDED YLGTLSRKLT EDIAQLEENI YKEAGEEFNI
     GSPKQLGEIL FGKLKLVDKP KKTKTGQYST AEDVLSYLAA NHQIIADVLE YRGLTKLQST
     YVDALPNQVN PKTQRIHTNY MQTVAATGRL SSTDPNLQNI PIRTERGRQV RNAFIPRDEN
     YTLMAADYSQ IELRIIAALS EEENMIAAFK NGEDIHASTA ARVFNVDIEK VTREQRSNAK
     TVNFGIIYGV SAFGLSNQTD LDRSEAKELI DTYYKTYPKL RAYMDDQVAF ARENGYVETV
     LGRRRYLKDI NSSNNVVRGA AERNAVNAPI QGSAADIIKI AMINIHEKFK ELNCKSKMLL
     QVHDELVFDI HNDELEDMKK LIQDEMQNAY KLSVPLDVEV GVGMNWLEAH
//
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