ID A0A0X8GQ23_9BURK Unreviewed; 928 AA.
AC A0A0X8GQ23;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-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=VN23_18130 {ECO:0000313|EMBL:AMC36370.1};
OS Janthinobacterium sp. B9-8.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Oxalobacteraceae; Janthinobacterium.
OX NCBI_TaxID=1236179 {ECO:0000313|EMBL:AMC36370.1, ECO:0000313|Proteomes:UP000069577};
RN [1] {ECO:0000313|EMBL:AMC36370.1, ECO:0000313|Proteomes:UP000069577}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B9-8 {ECO:0000313|EMBL:AMC36370.1,
RC ECO:0000313|Proteomes:UP000069577};
RA Xu X., Jin W., Wu Q., Jiang L., Huang H.;
RT "The whole genome sequence of Janthinbacterium sp. B9-8, a bacterium
RT isolated from low temperature sewage.";
RL Submitted (JAN-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 -!- SUBUNIT: Single-chain monomer with multiple functions.
CC {ECO:0000256|ARBA:ARBA00011541}.
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; CP014222; AMC36370.1; -; Genomic_DNA.
DR RefSeq; WP_046353824.1; NZ_CP014222.1.
DR AlphaFoldDB; A0A0X8GQ23; -.
DR STRING; 1236179.VN23_18130; -.
DR KEGG; jab:VN23_18130; -.
DR OrthoDB; 9806424at2; -.
DR Proteomes; UP000069577; 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};
KW Exonuclease {ECO:0000256|ARBA:ARBA00022839};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Nuclease {ECO:0000256|ARBA:ARBA00022839};
KW Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695,
KW ECO:0000256|RuleBase:RU004460};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU004460}.
FT DOMAIN 1..260
FT /note="5'-3' exonuclease"
FT /evidence="ECO:0000259|SMART:SM00475"
FT DOMAIN 333..519
FT /note="3'-5' exonuclease"
FT /evidence="ECO:0000259|SMART:SM00474"
FT DOMAIN 686..892
FT /note="DNA-directed DNA polymerase family A palm"
FT /evidence="ECO:0000259|SMART:SM00482"
SQ SEQUENCE 928 AA; 102136 MW; 2B1B5C51501D38D1 CRC64;
MATLLLIDGS SYLYRAFHAI RDLAAPDGTP TNALYGFVNM LKKLRQQTPA DYIACVFDAK
GKTFRDDLYS EYKAHRPSMP DELRVQIAPI HAAVKAFGIK ILMVDGVEAD DVIGTLASWG
TEHGITTIMS TGDKDMAQLV NQYVRIENSM TEEVLDIEGV INKFGVRPEQ IVDYLALIGD
TVDNVPGVPK CGPKTAKKWL DEYQTLDAVM ANAAAIKGVV GENLRNTLEW LPMAKQLVTI
KCDLDLSSEL PQQFADLVPQ SEDWDTLLGI FRLANFRSWI REAESKAAAA SIPAPANDDL
FSLVASNGPI TEAESIAPII DSPAELTPAP RNYQTILSDT ELDDWLAQLM AASVVSLDTE
TTGLDALNSQ IVGMSFCISE GHAAYLPLAH RGPDAVDQLP LDATLAKLKP WLESANHKKL
GQNLKFDQHI FANHGIALAG VEDDTLLMSY VLASHEKHSM DAQAERELGV TTIKFEELCG
KGAKQIGFDE VAVDIASVYA AEDADITLQL AHALLPRLTG GLAHVYREIE MPSRSILFEM
ERTGVLLDSQ KLNQQSHEIG LRLLALEQNA YDLAGQPFNL SSPKQIGEIF FEQLKLPVIK
KTPKGAPSTD EEVLQELAKD FPLPKVLLEH RSLSKLKSTY TDKLPLMVNP RTGRVHTSYN
QTVAITGRLS SSEPNLQNIP VKSMEGRKIR EAFIAPKGWQ IMSADYSQIE LRIMAHLSGD
EAMIAAFNSG EDIHRTTAAE VFAVALDQVS SEQRRYAKSI NFGLIYGMGV FGLAAQLEIP
RDAAKNFIDR YFARFNGVAQ YMENIRASAK EYGYVETVFG RRLWLPEIKS ANAARRAGAE
RAAINAPMQG TAADLIKLAM INVADWIKTE GLQSRLIMQV HDELVLEVPD SEVEMMREQL
PLKMSAAAKL TVPLLAEVGV GLNWEEAH
//
