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Database: UniProt
Entry: F0RUZ1_SPHGB
LinkDB: F0RUZ1_SPHGB
Original site: F0RUZ1_SPHGB 
ID   F0RUZ1_SPHGB            Unreviewed;       948 AA.
AC   F0RUZ1;
DT   03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT   03-MAY-2011, sequence version 1.
DT   27-MAR-2024, entry version 76.
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=SpiBuddy_0815 {ECO:0000313|EMBL:ADY12642.1};
OS   Sphaerochaeta globosa (strain ATCC BAA-1886 / DSM 22777 / Buddy)
OS   (Spirochaeta sp. (strain Buddy)).
OC   Bacteria; Spirochaetota; Spirochaetia; Spirochaetales; Sphaerochaetaceae;
OC   Sphaerochaeta.
OX   NCBI_TaxID=158189 {ECO:0000313|EMBL:ADY12642.1, ECO:0000313|Proteomes:UP000008466};
RN   [1] {ECO:0000313|Proteomes:UP000008466}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-1886 / DSM 22777 / Buddy
RC   {ECO:0000313|Proteomes:UP000008466};
RA   Lucas S., Copeland A., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA   Zeytun A., Detter J.C., Han C., Tapia R., Land M., Hauser L., Kyrpides N.,
RA   Ivanova N., Mikhailova N., Pagani I., Ritalahti K.M., Loeffler F.E.,
RA   Woyke T.;
RT   "Complete sequence of Spirochaeta sp. Buddy.";
RL   Submitted (FEB-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; CP002541; ADY12642.1; -; Genomic_DNA.
DR   RefSeq; WP_013606495.1; NC_015152.1.
DR   AlphaFoldDB; F0RUZ1; -.
DR   STRING; 158189.SpiBuddy_0815; -.
DR   KEGG; sbu:SpiBuddy_0815; -.
DR   eggNOG; COG0258; Bacteria.
DR   eggNOG; COG0749; Bacteria.
DR   HOGENOM; CLU_004675_0_0_12; -.
DR   OrthoDB; 9806424at2; -.
DR   Proteomes; UP000008466; 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:UP000008466};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU004460}.
FT   DOMAIN          45..306
FT                   /note="5'-3' exonuclease"
FT                   /evidence="ECO:0000259|SMART:SM00475"
FT   DOMAIN          358..539
FT                   /note="3'-5' exonuclease"
FT                   /evidence="ECO:0000259|SMART:SM00474"
FT   DOMAIN          706..912
FT                   /note="DNA-directed DNA polymerase family A palm"
FT                   /evidence="ECO:0000259|SMART:SM00482"
FT   REGION          1..38
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   948 AA;  106319 MW;  59EBE1F60CB4B8E6 CRC64;
     MDELFSNQDF DQEKLASEAK DRVLSVPPKP QEPKVVPPTK LSSQKKLYII DGYSLIYRSF
     FGFFANPIRD TQGNNVSAVY GFFSTLLKLI RENNPDYLVV ALDSMGPTFR HTMYEPYKAN
     RDAAPEELHT QVPLIQNILT ALKVPTIAMP GFEADDIIAT LSEEATRHQI DTIMFTGDKD
     LLQLVDEHTF ALRPAKKNEK FYRLMGCKEV EEEYGIKPSQ IVDYLSLLGD SSDNVPGVKG
     IGEKGAAKLL QQFGSLEGIY SNLKLVAPGL QKKLAEGVEN AKLSKRLVEL KRDLFTVDTF
     DTEQYLVSDV DYDAAIPLFQ EIGMRSIIKE LGRVSSGESS SPIPAKVEAK SETKQAVYEA
     VTDVTQIKNL FEQAIKAGGV MAFDLETTGL DEMLAQVIGF SFCWEEGKSY YVPLVHETKE
     LVDREQVRSL LEEYLGSGRL SLVGQNIKYD YKVLRQWGIM PKNIYFDTMV AAWLLDSTSV
     FNMDYLAEKY LDYKTVHYTD IVPKDKLLSD IPLEQAVFYG AEDADVTFRL YKLFSELLGA
     RNLRSLLDEV EMPLLVIIAN MELAGIYLER KLIEPLSAEF EGRIDAIRNQ IFAICGHAFN
     LNSPQQLQEV LFVERNIPTG AKTRSGFSTS TDVLEPLRDD YPEVELILQY RTLNKLKTTY
     IDKLPLQINE KTHRIHPSFA QTGTETGRLS CKDPNLQNIP VRTEEGRRIR SAFVPQAGHV
     FLSADYSQIE LVVLAHMADD PGLKGAFAAG IDVHSSTASL IFDVPLDQVT PVQRRIAKTI
     NFGVMYGMGT HSLAMDLKIP HSEAKQFIDQ YFERYSSVRS FVEATKTMSQ QVGSVSTLLG
     HVRTITEINS RSAVERAKAE RIAVNTVIQG SAADIVKLAM LRVDSLLKQK KLGARLLLQI
     HDELIFEVPE AEIEETKAVV KEALEHAVKL SVPLRTSIEV GSNWGDIH
//
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