ID A0A1D3TPU2_9FIRM Unreviewed; 878 AA.
AC A0A1D3TPU2;
DT 30-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 30-NOV-2016, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE RecName: Full=DNA polymerase I {ECO:0000256|RuleBase:RU004460};
DE EC=2.7.7.7 {ECO:0000256|RuleBase:RU004460};
GN Name=polA {ECO:0000256|RuleBase:RU004460};
GN ORFNames=SAMN05421730_1001593 {ECO:0000313|EMBL:SCP95470.1};
OS Anaerobium acetethylicum.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae;
OC Anaerobium.
OX NCBI_TaxID=1619234 {ECO:0000313|EMBL:SCP95470.1, ECO:0000313|Proteomes:UP000199315};
RN [1] {ECO:0000313|EMBL:SCP95470.1, ECO:0000313|Proteomes:UP000199315}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GluBS11 {ECO:0000313|EMBL:SCP95470.1,
RC ECO:0000313|Proteomes:UP000199315};
RA Capua I., De Benedictis P., Joannis T., Lombin L.H., Cattoli G.;
RL Submitted (SEP-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|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; FMKA01000001; SCP95470.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1D3TPU2; -.
DR STRING; 1619234.SAMN05421730_1001593; -.
DR OrthoDB; 9806424at2; -.
DR Proteomes; UP000199315; Unassembled WGS sequence.
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:0016788; F:hydrolase activity, acting on ester bonds; IEA:UniProt.
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; 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 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};
KW Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695,
KW ECO:0000256|RuleBase:RU004460};
KW Reference proteome {ECO:0000313|Proteomes:UP000199315};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU004460}.
FT DOMAIN 4..265
FT /note="5'-3' exonuclease"
FT /evidence="ECO:0000259|SMART:SM00475"
FT DOMAIN 636..842
FT /note="DNA-directed DNA polymerase family A palm"
FT /evidence="ECO:0000259|SMART:SM00482"
SQ SEQUENCE 878 AA; 99184 MW; F6F1A4ABF87B39B3 CRC64;
MNDKKIVLID GNSILNRAFY GLPDLTNSEG LHTNAVFGFL SILFKVLDEE HADHLTVAFD
RKEPTFRHEM FGDYKGTRKE MPEELKEQVP VMKEVLKSMN VPVIEKAGYE ADDLIGTMAK
RAEEEGYQVS VVSGDRDLLQ LATDKVKIRI PKTKKGRTEV EDYYAKDVLE AYQVSPVQII
ELKALMGDQS DNIPGVPGIG EKTATRIIAE YGSIENAFGN VADIKPNKAR ESLQNHYDMA
QMSKKLATIK TDCEIDYDFQ EAEIGNLFTE EAYRQFKRLD FKNFMSRFEV EIPANRVEGY
FHKITGFNEV EELFAKALEA ETAGFQFVEQ GELFGAAIAF GDKDICFVQA QGFVTKEYII
DKIQKILDTV KRASFINLKE ALIYISPANE GTLFDAGIAA YLLNPLKNSY EYEDLAKEYL
SLLIPSRQDM LGKLSYEKAE EEKPEAFLNC VCYMAYVAYA AAGILEEKLK ETGMESLFRT
VEMPLVQAIY DMETAGIRVD KEQLKEYGDA LQVRIEELEK EIYEAAGEQF NINSPKQLGE
ILFERLKLPH AKKTKTGYST AADVLEKLAS EHSIVPMILE YRQITKLKST YADGLANYIS
EDGRIHGKFN QTITATGRIS STEPNLQNIP IKMELGRLIR KVFIPEQDYV MVDADYSQIE
LRVLAHLSND ERLIKAYSDA KDIHRITASQ VFHTPLDEVT PLQRSNAKAV NFGIVYGISS
FGLSQGLSIS RKEAGEYINQ YFETYPGVKK FLDEAVENAK ETGYVTTIFG RRRPVPELKS
SNFVQRSFGE RVAMNSPIQG AAADIIKIAM VNVNKKIKER KLKSRLILQV HDELLVEAHK
DEVDQVREIL LSEMSGAADL AVPLEIDMHT GDSWYEAK
//
