ID A0A2T0B1I2_9CLOT Unreviewed; 879 AA.
AC A0A2T0B1I2;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 27-MAR-2024, entry version 26.
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_3 {ECO:0000313|EMBL:PRR77317.1};
GN Synonyms=polA {ECO:0000256|RuleBase:RU004460};
GN ORFNames=CLLI_24890 {ECO:0000313|EMBL:PRR77317.1};
OS Clostridium liquoris.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=1289519 {ECO:0000313|EMBL:PRR77317.1, ECO:0000313|Proteomes:UP000239706};
RN [1] {ECO:0000313|EMBL:PRR77317.1, ECO:0000313|Proteomes:UP000239706}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 100320 {ECO:0000313|EMBL:PRR77317.1,
RC ECO:0000313|Proteomes:UP000239706};
RA Poehlein A., Daniel R.;
RT "Genome sequence of Clostridium liquoris DSM 100320.";
RL Submitted (MAR-2018) 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|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:PRR77317.1}.
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DR EMBL; PVXO01000066; PRR77317.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2T0B1I2; -.
DR OrthoDB; 9806424at2; -.
DR Proteomes; UP000239706; 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; cd06140; DNA_polA_I_Bacillus_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; 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:UP000239706};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU004460}.
FT DOMAIN 3..264
FT /note="5'-3' exonuclease"
FT /evidence="ECO:0000259|SMART:SM00475"
FT DOMAIN 636..843
FT /note="DNA-directed DNA polymerase family A palm"
FT /evidence="ECO:0000259|SMART:SM00482"
SQ SEQUENCE 879 AA; 101016 MW; 39C0DCD53C835418 CRC64;
MERKERLLIL DGNSLMNRAF YALPLLTNNE GLHTNAVYGF TTMLLKMKEE IAPDYIVCTF
DRSAPTFRHN EYKDYKAGRK RMPEELAEQF PLVKDLLHKL AIDIFEIDGF EADDLIGTLS
RFAEEKGIEV YIVTGDKDAL QLASDSTKVI ITKKGITEKE IYDKSRMIEE MGVTPSQFID
VKGLMGDSSD NIPGVPGIGE KTAFKLIKEY GSIENVLQNI DNISGKKIKE NLIEYSEQAI
FSKKLATIMR EVPIDIDLDS IKSNENYDEE GVKKIFIDLQ FKSLLDKLPH SEKVEEKNNE
IKIEYNFIEC LLDLKALFNV ISSEYKNSKL YITFQILNEN VYSKCYIEKI FINFEEKNYI
ISLQKILNEN HEETIKCLKK IFEDEKIEKV CHDIKIPHTI LHKMGVDLNG VKFDTKIAAY
LIDSSRGDYE LDTIIQQYLK IIINDDDDEG KIRETSLLKE VYKELENQIN VLNMGQLFYE
VELPLTTVLA SMESHGFKVD EDMLTHIGDK FAKEIEKVQK EIYSLSGEEF NINSPKQLGK
ILFEKLDLPV IKRTKTGYST NAEVLEALEG KHPIIEKITY YRQLTKLYST YVEGLKNVID
EDGKIHSSFN QTVTTTGRLS STEPNLQNIP IKYEMGREIR KVFVPNDKDS VIVSADYSQI
ELRVLAHIAH DENLINAFKH HDDIHTKTAS EVFRVPIDEV TPAMRSNAKA VNFGIVYGIG
DFSLAKDIKV SRKEAKEYID TYFERYPNVK KYMDDTVKKA GKDMYVTTIL NRRRFIPEIA
NSKKMIKALG ERLAMNSPIQ GSAADIIKMA MVKVYNELEK RHLKSTLILQ VHDELILNVY
KDELEEVKTI VKESMENVMP LSVPLEVDIN EGENWYEAK
//
