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Database: UniProt
Entry: F4LK29_TREBD
LinkDB: F4LK29_TREBD
Original site: F4LK29_TREBD 
ID   F4LK29_TREBD            Unreviewed;       926 AA.
AC   F4LK29;
DT   28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT   28-JUN-2011, sequence version 1.
DT   27-MAR-2024, entry version 74.
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=Trebr_2076 {ECO:0000313|EMBL:AEE17491.1};
OS   Treponema brennaborense (strain DSM 12168 / CIP 105900 / DD5/3).
OC   Bacteria; Spirochaetota; Spirochaetia; Spirochaetales; Treponemataceae;
OC   Treponema.
OX   NCBI_TaxID=906968 {ECO:0000313|EMBL:AEE17491.1, ECO:0000313|Proteomes:UP000006546};
RN   [1] {ECO:0000313|Proteomes:UP000006546}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 12168 / CIP 105900 / DD5/3
RC   {ECO:0000313|Proteomes:UP000006546};
RA   Lucas S., Han J., Lapidus A., Bruce D., Goodwin L., Pitluck S., Peters L.,
RA   Kyrpides N., Mavromatis K., Ivanova N., Mikhailova N., Pagani I.,
RA   Teshima H., Detter J.C., Tapia R., Han C., Land M., Hauser L.,
RA   Markowitz V., Cheng J.-F., Hugenholtz P., Woyke T., Wu D., Gronow S.,
RA   Wellnitz S., Brambilla E., Klenk H.-P., Eisen J.A.;
RT   "The complete genome of Treponema brennaborense DSM 12168.";
RL   Submitted (APR-2011) 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}.
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DR   EMBL; CP002696; AEE17491.1; -; Genomic_DNA.
DR   RefSeq; WP_013759194.1; NC_015500.1.
DR   AlphaFoldDB; F4LK29; -.
DR   STRING; 906968.Trebr_2076; -.
DR   KEGG; tbe:Trebr_2076; -.
DR   eggNOG; COG0749; Bacteria.
DR   HOGENOM; CLU_004675_0_0_12; -.
DR   OrthoDB; 9806424at2; -.
DR   Proteomes; UP000006546; 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; 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:UP000006546};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU004460}.
FT   DOMAIN          6..268
FT                   /note="5'-3' exonuclease"
FT                   /evidence="ECO:0000259|SMART:SM00475"
FT   DOMAIN          330..518
FT                   /note="3'-5' exonuclease"
FT                   /evidence="ECO:0000259|SMART:SM00474"
FT   DOMAIN          684..890
FT                   /note="DNA-directed DNA polymerase family A palm"
FT                   /evidence="ECO:0000259|SMART:SM00482"
SQ   SEQUENCE   926 AA;  101666 MW;  7F3A6FAA927FF528 CRC64;
     MNDFSDPDST LYILDSYGLI YRSYYAFINR PLTDKDGKNV SAVFGFFRNF KAVLDHYKPR
     YIAAAFDSRK ATFRHEMYAD YKATRQKTPE DLHAQVPVIE EILTALGIPV LRCDGFEADD
     VIATIASVCG AENRCCRILS ADKDLMQLVN DTTQILKPDK NGGWEIVGKD GVKAEWGVEP
     ELMLDLLSLI GDSSDNVPGV SGVGIKTALK LLDEYGSLDG IFAHADDISG AVGNKIRAGK
     DAAYFSKSLI ALRYDVPVDT CVPSFGTVSL DYEAASRLLF RYGVPAVAKQ YASVPLPAGS
     ETEAIQSKGP TGLIPDEPVF EELTKNTGDY MAVTSIAVLA SYIDEILASE PIEAAFDCET
     DSLDRIHTRI VGFSLSRRAG TGIYVPLSVP DALLTQTLIE KQDAFVQLER LFSVPACTLA
     MHNGKFDYEV LRSNGLAEPR CRIADTMVAA WLLDPDRSAY SLEALAADKL GLETIPYTDV
     VPKGSTFADI PLEQAVPYAA EDADLTWQLY RLFLPRLAAA KLGDLFWNLE MPVLPILAEM
     ELDGIHIEKS ELISYGEELT AEIERIRREI YELVGHEFNV ASTKQLQDVL FEERKLPPGK
     KTKTGYSTDT GVLETLAALD PVPRKILDYR LKTKLFSSYV DTLPLMVDGN DRIHTSFIQT
     GTATGRLSSR EPNLQNIPVR DEDGRRIRLA FTAEPGCQLI SADYSQIELV ILAHLSGDPN
     LCAAFSGGTD VHRATAALIF GVQPDAVTPD MRRTAKTINF GVMYGMSAFR LAGALGIPRT
     QAAEFIEAYF KTYAGVRNFM NEMVNAAQQS GFVETIFGRR RYIRAINSSS KIEKSGAERV
     AVNTPIQGSA ADIVKKAMID VAAALKKTGS PARLLLQVHD ELILECPQES AAETASLIKQ
     TMENVVSLRV PLKVSVEIGP RWGDFH
//
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