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Database: UniProt
Entry: A0A142EJR2_9BACT
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ID   A0A142EJR2_9BACT        Unreviewed;       939 AA.
AC   A0A142EJR2;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   27-MAR-2024, entry version 39.
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=AO498_03090 {ECO:0000313|EMBL:AMQ55367.1};
OS   Algoriphagus sanaruensis.
OC   Bacteria; Bacteroidota; Cytophagia; Cytophagales; Cyclobacteriaceae;
OC   Algoriphagus.
OX   NCBI_TaxID=1727163 {ECO:0000313|EMBL:AMQ55367.1, ECO:0000313|Proteomes:UP000073816};
RN   [1] {ECO:0000313|Proteomes:UP000073816}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=M8-2 {ECO:0000313|Proteomes:UP000073816};
RA   Shintani M.;
RT   "Complete sequence of Algoriphagus sp. M8-2.";
RL   Submitted (SEP-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:AMQ55367.1, ECO:0000313|Proteomes:UP000073816}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=M8-2 {ECO:0000313|EMBL:AMQ55367.1,
RC   ECO:0000313|Proteomes:UP000073816};
RX   PubMed=27174266;
RA   Muraguchi Y., Kushimoto K., Ohtsubo Y., Suzuki T., Dohra H., Kimbara K.,
RA   Shintani M.;
RT   "Complete Genome Sequence of Algoriphagus sp. Strain M8-2, Isolated from a
RT   Brackish Lake.";
RL   Genome Announc. 4:0-0(2016).
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; CP012836; AMQ55367.1; -; Genomic_DNA.
DR   RefSeq; WP_067543649.1; NZ_CP012836.1.
DR   AlphaFoldDB; A0A142EJR2; -.
DR   STRING; 1727163.AO498_03090; -.
DR   KEGG; alm:AO498_03090; -.
DR   PATRIC; fig|1727163.4.peg.640; -.
DR   OrthoDB; 9806424at2; -.
DR   Proteomes; UP000073816; 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:UP000073816};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU004460}.
FT   DOMAIN          7..268
FT                   /note="5'-3' exonuclease"
FT                   /evidence="ECO:0000259|SMART:SM00475"
FT   DOMAIN          346..527
FT                   /note="3'-5' exonuclease"
FT                   /evidence="ECO:0000259|SMART:SM00474"
FT   DOMAIN          696..903
FT                   /note="DNA-directed DNA polymerase family A palm"
FT                   /evidence="ECO:0000259|SMART:SM00482"
SQ   SEQUENCE   939 AA;  105898 MW;  F29B773A4CC6F23C CRC64;
     MSQKQPHKLF LLDAMALIYR AHFAFSKNPR INSKGLNTGV MLGFTNTLLE VLEKEKPSHI
     AVAFDTKAPT FRHIQYEPYK ANRLDQPEDI MVSIPWVKEI VRAFRIPVLE MDGFEADDII
     GTIAKKAEKE HYTVYMMTPD KDYGQIVDDH IFLYKPAFMG NGVDVMGPKQ VCAKWDIEHV
     DQVRDILGLM GDAVDNIPGI PGIGEKTAVK LLKEFGTVEG LIANVDKLKG KQKENVENFA
     AQGILSKELA TIKIDVPVDF VEEELRYEGF DEEKLRAIFT ELEFRTLASR IFKDSPGKKA
     AIAAPAQMDL FAPAPASPSS EEEGIEEELP TVPTVFETIH GNVHQYHKIK GKVAVEELVS
     YLKLQDEICF DTETTDLDAM KAELVGLSFA YVPGEAYYIP VTSDLQETQE ILEVLRPIFE
     NESILKIGQN VKYDMLVLKN YGIEVKGTLY DTMLAHYLIE PEGKHGMDWL AQQYLNYKPV
     SITELIGKKG KNQGNMRDVD EDEVTAYAAE DADITLRLKE KLDPIIQSNG LKKLFDEVEN
     PLIRVLTDME FEGVRIDTGS LAELSVALDE ESKEIEKRVY ELAGVKFNLA SPKQLGEVLF
     EKLKLDPKAK KTKTGQYATG EEILSKMADE HEIAQAILDY RQMVKLKSTY VDALPTMINA
     KTGRIHTTYN QFVAATGRLS SINPNLQNIP IRTSRGREIR KAFVPRDENH VLLSADYSQI
     ELRLMAAFSQ DESMLEAFRN GRDIHATTAA KIFKVPLEEV TSDMRRKAKT ANFGIIYGIS
     AFGLAQRLSI PRGEAKEIID AYFSEFPAVK EYMDGAIEKA RKDEYVETIL GRRRYLRDIN
     SRNMTMRGFA ERNAINAPLQ GSAADLIKVA MIHVHQWMKK EKLKSKMILQ VHDELVFDAH
     KDEVELLKKN IPGLMSNAIQ LPVPIEVEVG VGTDWLQAH
//
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