ID A0PZF5_CLONN Unreviewed; 878 AA.
AC A0PZF5;
DT 09-JAN-2007, integrated into UniProtKB/TrEMBL.
DT 09-JAN-2007, sequence version 1.
DT 27-MAR-2024, entry version 116.
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 OrderedLocusNames=NT01CX_1677 {ECO:0000313|EMBL:ABK62148.1};
OS Clostridium novyi (strain NT).
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=386415 {ECO:0000313|EMBL:ABK62148.1, ECO:0000313|Proteomes:UP000008220};
RN [1] {ECO:0000313|EMBL:ABK62148.1, ECO:0000313|Proteomes:UP000008220}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NT {ECO:0000313|EMBL:ABK62148.1,
RC ECO:0000313|Proteomes:UP000008220};
RX PubMed=17115055; DOI=10.1038/nbt1256;
RA Bettegowda C., Huang X., Lin J., Cheong I., Kohli M., Szabo S.A., Zhang X.,
RA Diaz L.A. Jr., Velculescu V.E., Parmigiani G., Kinzler K.W., Vogelstein B.,
RA Zhou S.;
RT "The genome and transcriptomes of the anti-tumor agent Clostridium novyi-
RT NT.";
RL Nat. Biotechnol. 24:1573-1580(2006).
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; CP000382; ABK62148.1; -; Genomic_DNA.
DR RefSeq; WP_011721764.1; NC_008593.1.
DR AlphaFoldDB; A0PZF5; -.
DR STRING; 386415.NT01CX_1677; -.
DR KEGG; cno:NT01CX_1677; -.
DR PATRIC; fig|386415.7.peg.783; -.
DR eggNOG; COG0258; Bacteria.
DR eggNOG; COG0749; Bacteria.
DR HOGENOM; CLU_004675_0_0_9; -.
DR Proteomes; UP000008220; 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; 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; 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 Coiled coil {ECO:0000256|SAM:Coils};
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:UP000008220};
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..469
FT /note="3'-5' exonuclease"
FT /evidence="ECO:0000259|SMART:SM00474"
FT DOMAIN 635..842
FT /note="DNA-directed DNA polymerase family A palm"
FT /evidence="ECO:0000259|SMART:SM00482"
FT COILED 500..527
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 878 AA; 100903 MW; CD8B97D3E49BCE7D CRC64;
MNKERLLILD GHSLMYRAFF ALPPLTNKEG IHTNAIYGFI KMLLKMKEEI KPDYIVTTFD
KKAPTFRHKE YEEYKAGRAK MPDELNEQFP IVKDILNKLA INIFEIEGFE ADDLIGTLSK
FAEEKGIEVY IVTGDRDALQ LATDNVRVVI NKKGMSEKEI YDKNKMIEEY GVTPTEFIDV
KGLMGDKSDN IPGVPGIGNK TALKLIKEYG SIENVLENVE NISGKKMKQN LIDYREQAIL
SKKLATICKD VPIEINLDEI KSKEDYDIQG VRLLFQSLGF KSLLDNIGDN EGLDKEDEAE
VKESDINIKS TNINTIENFS KFVEGIDDSI YIQADFVDEN IYSKIEFNNL YVRHKEEVFV
ISANEIKDKD GAKYFEILKN LFENEKIKKV CHDSKKVYVV LKKHNIAAKN IAFDTKIAAY
LLQPSKSDYM LKDLIEEMLL LSLKDDDNIK INETYYIKDV YEKLEKDIKK SNMEELLYTV
ELPLIEVLAS MECEGFRVDE NRLTEIGEKF KKEIETLEKE IHELADEEFN IKSPKQLGKI
LFEKLDLPVI KKTKTGYSTN AEVLEKLKDS HPIIEKIIEY RQITKLDSTY VEGLKNVIDE
DAKIHSSFNQ TVTTTGRLSS TEPNLQNIPI KHEMGREIRK VFVPNNDESV IFSADYSQIE
LRILSHIADD EKLIDAFKHH KDIHTITASE VFKVPIDEVT PLMRSNAKAV NFGIVYGIGA
FSLSKDINVS RKEAKEYIDT YFSRYPNVKK YIDEIISKAE VDGFVTTILN RKRYIPEIQS
RNKIVRGFGE RLAMNTPIQG SAADIIKLAM VEVYNELKNR NLKSTLILQV HDELILNVYK
DELEEVKEMV VDKMENVMKL LVPLEADVNV GETWYEAK
//
