ID A0A133XXK9_9ACTN Unreviewed; 912 AA.
AC A0A133XXK9;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 27-MAR-2024, entry version 37.
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=HMPREF3192_00073 {ECO:0000313|EMBL:KXB35668.1};
OS Atopobium deltae.
OC Bacteria; Actinomycetota; Coriobacteriia; Coriobacteriales; Atopobiaceae;
OC Atopobium.
OX NCBI_TaxID=1393034 {ECO:0000313|EMBL:KXB35668.1, ECO:0000313|Proteomes:UP000070675};
RN [1] {ECO:0000313|Proteomes:UP000070675}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DNF00019 {ECO:0000313|Proteomes:UP000070675};
RA Mitreva M., Pepin K.H., Mihindukulasuriya K.A., Fulton R., Fronick C.,
RA O'Laughlin M., Miner T., Herter B., Rosa B.A., Cordes M., Tomlinson C.,
RA Wollam A., Palsikar V.B., Mardis E.R., Wilson R.K.;
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 -!- 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:KXB35668.1}.
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DR EMBL; LSCR01000001; KXB35668.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A133XXK9; -.
DR STRING; 1393034.HMPREF3192_00073; -.
DR PATRIC; fig|1393034.3.peg.69; -.
DR Proteomes; UP000070675; 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; 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; 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.
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|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:UP000070675};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU004460}.
FT DOMAIN 1..250
FT /note="5'-3' exonuclease"
FT /evidence="ECO:0000259|SMART:SM00475"
FT DOMAIN 670..876
FT /note="DNA-directed DNA polymerase family A palm"
FT /evidence="ECO:0000259|SMART:SM00482"
FT REGION 448..472
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 912 AA; 100284 MW; 081E67834D75940A CRC64;
MHRAFHALSQ PMFAPDGRPT NAIYGFFNMF LKFYERFNPD GIICAFDKGK PRVRMEMLPQ
YKAQRPPMDP NLHEQFPMVK ALLEALRVPV VECEGWEGDD ILGTLATAGE KAGHSMLLVT
GDRDMYQLST ERVRVVSTRK GMSDVAIMTP ESVSDLYGGI TPDLVVDFYG LKGDSSDNIP
GVPGIGPKKA AALITQYGNL DEVLAHADEI KGKMGENIRA HVDDALLSRR VATIRRDAPI
SLDFADAIFP AFTSADALQD VSAAFSALGM MSTLQRLCNL VGAKQMPAVP TAPSMKLGEL
QKGEAAVRLL DDALRRSQWI ALSYKQVAPT GQLTLAFENT SAAELWIATT DGVGLFEHDA
VVDALCRLLH EGNIVCSDTK QLLHDLANNQ MLEALGVADV REITSLLDPR RIFDTSVAGY
LLDSDQSDFS YAALAQCYLK LTLPGADDSG TSATEKGSAA AEKGADTAGE KSTDAVDAAN
SAAIEVYIVR NLHNLLVKKL QADQLWKLFV DIEMPLLLVL FIMEQQGVHA DVLKLRQQSY
ELGKEIDQLV SDIHAKAGKA FNIASPEQLS HVLFDTWGLP TRGLKKTKRG FYSTNAGVLS
ELAQVDERVA EVLEYRERTK IKSTYLDALP DLIADDGRIH TSFNQTVAAT GRLSSSDPNL
QNIPTRSDLG HRVRMAFTVP AGCVFLACDY SQIELRLLAH LSNDEHLIAA FRSGADFHAA
TAARVFGVAL DEVTPQLRSR AKAVNFGIVY GQQAYGLSTS LGISRKEAQA MIDRYFEAYP
GVNAYLKQQI RLAREQGYVT TMYGRRRYAA DINSSNFQKR SFAERTAMNH PMQGSAADII
KIAMIRVQQA LTQHHLRSKL ILQIHDELDL EVPQDELDEV SELVKTTMQQ ACELRVPLIA
DISYGPTWAQ AK
//
