ID   F4LIQ8_TREBD            Unreviewed;      1179 AA.
AC   F4LIQ8;
DT   28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT   28-JUN-2011, sequence version 1.
DT   27-MAR-2024, entry version 62.
DE   RecName: Full=DNA-directed DNA polymerase {ECO:0000256|ARBA:ARBA00012417};
DE            EC=2.7.7.7 {ECO:0000256|ARBA:ARBA00012417};
GN   OrderedLocusNames=Trebr_0797 {ECO:0000313|EMBL:AEE16233.1};
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:AEE16233.1, 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   -!- 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};
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DR   EMBL; CP002696; AEE16233.1; -; Genomic_DNA.
DR   AlphaFoldDB; F4LIQ8; -.
DR   STRING; 906968.Trebr_0797; -.
DR   KEGG; tbe:Trebr_0797; -.
DR   eggNOG; COG0587; Bacteria.
DR   HOGENOM; CLU_001600_0_0_12; -.
DR   Proteomes; UP000006546; Chromosome.
DR   GO; GO:0008408; F:3'-5' exonuclease activity; IEA:InterPro.
DR   GO; GO:0003887; F:DNA-directed DNA polymerase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
DR   CDD; cd04485; DnaE_OBF; 1.
DR   CDD; cd12113; PHP_PolIIIA_DnaE3; 1.
DR   Gene3D; 1.10.150.870; -; 1.
DR   Gene3D; 1.10.10.1600; Bacterial DNA polymerase III alpha subunit, thumb domain; 1.
DR   Gene3D; 3.20.20.140; Metal-dependent hydrolases; 1.
DR   InterPro; IPR011708; DNA_pol3_alpha_NTPase_dom.
DR   InterPro; IPR041931; DNA_pol3_alpha_thumb_dom.
DR   InterPro; IPR040982; DNA_pol3_finger.
DR   InterPro; IPR004805; DnaE2/DnaE/PolC.
DR   InterPro; IPR029460; DNAPol_HHH.
DR   InterPro; IPR004013; PHP_dom.
DR   InterPro; IPR003141; Pol/His_phosphatase_N.
DR   InterPro; IPR016195; Pol/histidinol_Pase-like.
DR   NCBIfam; TIGR00594; polc; 1.
DR   PANTHER; PTHR32294; DNA POLYMERASE III SUBUNIT ALPHA; 1.
DR   PANTHER; PTHR32294:SF0; DNA POLYMERASE III SUBUNIT ALPHA; 1.
DR   Pfam; PF07733; DNA_pol3_alpha; 1.
DR   Pfam; PF17657; DNA_pol3_finger; 1.
DR   Pfam; PF14579; HHH_6; 1.
DR   Pfam; PF02811; PHP; 1.
DR   SMART; SM00481; POLIIIAc; 1.
DR   SUPFAM; SSF89550; PHP domain-like; 1.
PE   4: Predicted;
KW   DNA replication {ECO:0000256|ARBA:ARBA00022705};
KW   DNA-directed DNA polymerase {ECO:0000256|ARBA:ARBA00022932};
KW   Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695,
KW   ECO:0000313|EMBL:AEE16233.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006546};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:AEE16233.1}.
FT   DOMAIN          30..97
FT                   /note="Polymerase/histidinol phosphatase N-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00481"
SQ   SEQUENCE   1179 AA;  133086 MW;  20AB1B7FA28CF2ED CRC64;
     MDGICGNAGG GVAKKRAHRY NIRMAVTDFV HLHVHSDYSL LDGAAKVKTL VARAKELGMS
     ALALTDHGNM FGALRFEQLC HKEGIKPLVG CEFYVAGSSR HEHKGTEQGN KYYHLILIAK
     NVEGYRNLMM LTSRSYTEGM YYKPRIDEEL IREYSGGLVC LSACLAGQLP QLLLNNQNKE
     AEDLVRRYRD IFGAENYFIE LQDHGIAQQK EVAPKLIDIA RKLGVPMVVT NDIHYCLKED
     YIAQDVLVCI GTKKTRDDPR RMKFEGTEFY MKTGEEMAQL FPAYPEMIEN TKRVADMCDL
     TIPQFSTKEL KDCLPVYQIP PEFKTQDDYV RHLVYKGLEK RYPEITEEIR QRAEYELGII
     FQMGFSGYFL IVWDFINWAK QNDIPVGPGR GSGAGSLVAY AMTITDIDPF RFNLIFERFL
     NPERISMPDF DVDICYEGRQ DVIEYTRRKY GDPQVGHIVT FGTLKAKAVI KDVARVLDIP
     LSEVNILTKL VPDGPKVHLK DAFEVNEKIP GSGQLAPYRN DPRYKELFDL CFKLEDNNRN
     TSLHASGIVI GKSKLPEWAP VYKDSKTGKV AVQYTMDIIE PCGLVKMDYL GLKTLTLIKY
     AERIIRKRPG YEQFRADEVS ETDEKTFDLF CAGQTSAVFQ FESPGMQKIL KQAQPRRLED
     IVALNALYRP GPMDYIPQYI EGKFDSSKIT YPDPCLKSIL EETYGVMVYQ EQVMQVAQRI
     AGYSLGGADM LRRAMGKKKV EVMAAEKTKF IEGAVKNGFT AEHAADIFEI MIPFAGYGFN
     KSHAAAYSVV AYRTAYLKAN FPAEFIAANL TNEITSTDKL PEYITEGRSM GLEIDPPDIN
     RSDKVFDVVD GRIVFGLLGI KGLGEAAADA IIAERKANGP YTDFMNFLDR VNTHDVNKKA
     IEVLIKTGAF DKLDKNRATL TANMERAIDY AESKKSAGRF GQVSLFEDSG VQEFADFKYE
     EQPEIPVMEM LNMEKELIGC YVSGHPLDKY RETIKNAATV TSATMGRAQE GKQYQIIGLL
     KNIRTITTKK GAQMAFAQLE DLNGSFDLTF FPKTWEQIKA TGRVAEETVQ AFAGKVDKSR
     DPDAPSFLVD ELLDPAALQV KTARELHVKL SSFFTKEQQL YPLRDFLFGT TGTCCVYFHM
     ETDNKDYIVK SNAQMTVPGT DSFISELESQ PLVDSVWRE
//