ID A0A0M8KBI9_9CHLR Unreviewed; 918 AA.
AC A0A0M8KBI9;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 27-MAR-2024, entry version 41.
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=ARMA_2659 {ECO:0000313|EMBL:GAP64236.1}, SE16_08810
GN {ECO:0000313|EMBL:KPL87696.1};
OS Ardenticatena maritima.
OC Bacteria; Chloroflexota; Ardenticatenia; Ardenticatenales;
OC Ardenticatenaceae; Ardenticatena.
OX NCBI_TaxID=872965 {ECO:0000313|EMBL:GAP64236.1, ECO:0000313|Proteomes:UP000037784};
RN [1] {ECO:0000313|EMBL:GAP64236.1, ECO:0000313|Proteomes:UP000037784}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=110S {ECO:0000313|EMBL:GAP64236.1,
RC ECO:0000313|Proteomes:UP000037784};
RA Kawaichi S., Yoshida T., Sako Y., Nakamura R.;
RT "Draft Genome Sequence of a Heterotrophic Facultative Anaerobic
RT Thermophilic Bacterium, Ardenticatena maritima Strain 110ST.";
RL Genome Announc. 3:e01145-15(2015).
RN [2] {ECO:0000313|EMBL:KPL87696.1, ECO:0000313|Proteomes:UP000050502}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=110S {ECO:0000313|EMBL:KPL87696.1,
RC ECO:0000313|Proteomes:UP000050502};
RA Hemp J., Ward L.M., Pace L.A., Fischer W.W.;
RT "Whole genome sequence of Ardenticatena maritima DSM 23922.";
RL Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|Proteomes:UP000037784}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=110S {ECO:0000313|Proteomes:UP000037784};
RA Kawaichi S., Yoshida T., Sako Y., Nakamura R.;
RT "Draft Genome Sequence of a Heterotrophic Facultative Anaerobic Bacterium
RT Ardenticatena maritima Strain 110S.";
RL Submitted (AUG-2015) 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:GAP64236.1}.
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DR EMBL; BBZA01000235; GAP64236.1; -; Genomic_DNA.
DR EMBL; LGKN01000005; KPL87696.1; -; Genomic_DNA.
DR RefSeq; WP_054493954.1; NZ_LGKN01000005.1.
DR AlphaFoldDB; A0A0M8KBI9; -.
DR STRING; 872965.SE16_08810; -.
DR PATRIC; fig|872965.6.peg.1797; -.
DR InParanoid; A0A0M8KBI9; -.
DR OrthoDB; 9806424at2; -.
DR Proteomes; UP000037784; Unassembled WGS sequence.
DR Proteomes; UP000050502; 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:UP000037784};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU004460}.
FT DOMAIN 2..263
FT /note="5'-3' exonuclease"
FT /evidence="ECO:0000259|SMART:SM00475"
FT DOMAIN 306..495
FT /note="3'-5' exonuclease"
FT /evidence="ECO:0000259|SMART:SM00474"
FT DOMAIN 665..874
FT /note="DNA-directed DNA polymerase family A palm"
FT /evidence="ECO:0000259|SMART:SM00482"
SQ SEQUENCE 918 AA; 103344 MW; CAF13C47B376D933 CRC64;
MSRPKIVLID GHSLAYRAFF ALPPTLATSK GELTNAVYGF ASMLLEVLEN ERPDYIAVAF
DVGRTFRHEL FDDYKGHRAK QPDELAVQFE RIYQLVDAFN IPIFTAEGYE ADDVIGTLAR
QAVEQGLDVV IVTGDTDAFQ LINAHTVVLT SGRRFSDVRR YDVDAVRERY GLEPHQLVDY
KALVGDPSDN IPGVRGIGDK TARKLLQTYG SLEGIYEHLD EIKPARVQNA LREGRELAFL
SRDLVRIRTD VPITLDLDAA RTRDFDRRRV LDLFRELEFN SLVERIPPPA GQTEPMQTEE
AARPVAYHIV QPDDLHTLAQ RLGDADFITF DVETDDLDPH TANLVGLALS VREGEGFYIP
IAHKGLEASA YNVPLEDVRA LIGPFLAARR IPARAHNAKF DMLVLWRHGF DITNVDFDTM
IAAWLINPGR RTYGLKALAF ERLGVEMTPI EELIGAKKRD QISMAEVPVE DVAPYACADV
DMTTRLARLL EADLRDLALW DLFANVEMPL VPVLAEMERV GVALDVDVLA ALRAELRERL
DAIEREIYDL VGYEFNINSN QQLSDVLFGK LGLDKRASSK TKSGHYSTSA RVLENLRGAH
PVVDLILEHR HLSKLLSTYI EQLPRMVNPA TGRIHTDFNQ TGTETGRLSS SNPNLQNIPI
RTDVGRRIRR AFVAEPGYVL LSADYSQIEL RVLAHLSGDD ALRRAFLEDG DIHRATAAAV
FGVPAEEVTP EMRNLAKRVN FGLLYGMSAW RLATETGLSR EEAEAFLERY FERFPSIAAF
LDSIVEQARE RGYTETILGR RRYFPEFRAG AQIPANQLRA AERAARNHPI QGSAADIIKL
AMIDIHRTFR DRGVRSRMIL QVHDELLFEI HEDELGDIPP LVIDRMSNAY PLSVPLKVDA
KVGYNWEEMV SLDEFLHA
//
