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Database: UniProt
Entry: A0A160T1R8_9CHLR
LinkDB: A0A160T1R8_9CHLR
Original site: A0A160T1R8_9CHLR 
ID   A0A160T1R8_9CHLR        Unreviewed;       932 AA.
AC   A0A160T1R8;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2016, sequence version 2.
DT   27-MAR-2024, entry version 37.
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   ECO:0000313|EMBL:CUS03129.2};
GN   ORFNames=CFX0092_A1251 {ECO:0000313|EMBL:CUS03129.2};
OS   Candidatus Promineifilum breve.
OC   Bacteria; Chloroflexota; Ardenticatenia; Candidatus Promineifilales;
OC   Candidatus Promineifilaceae; Candidatus Promineifilum.
OX   NCBI_TaxID=1806508 {ECO:0000313|EMBL:CUS03129.2, ECO:0000313|Proteomes:UP000215027};
RN   [1] {ECO:0000313|EMBL:CUS03129.2, ECO:0000313|Proteomes:UP000215027}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Cfx-K {ECO:0000313|EMBL:CUS03129.2,
RC   ECO:0000313|Proteomes:UP000215027};
RA   Oliw E.H.;
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}.
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DR   EMBL; LN890655; CUS03129.2; -; Genomic_DNA.
DR   AlphaFoldDB; A0A160T1R8; -.
DR   KEGG; pbf:CFX0092_A1251; -.
DR   OrthoDB; 9806424at2; -.
DR   Proteomes; UP000215027; Chromosome i.
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:UP000215027};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU004460}.
FT   DOMAIN          4..264
FT                   /note="5'-3' exonuclease"
FT                   /evidence="ECO:0000259|SMART:SM00475"
FT   DOMAIN          311..515
FT                   /note="3'-5' exonuclease"
FT                   /evidence="ECO:0000259|SMART:SM00474"
FT   DOMAIN          686..895
FT                   /note="DNA-directed DNA polymerase family A palm"
FT                   /evidence="ECO:0000259|SMART:SM00482"
SQ   SEQUENCE   932 AA;  102927 MW;  B2D58FCF317C1FF3 CRC64;
     MTAEKLVLID GHALAYRMFF ALPLESFTTK SGEPTNATFG FTRTLLDLIL AAEPPRYLAV
     SFDTGATFRD DLFADYKGTR EKMPDELSVQ IERIKQVVRA LNIPILELEG FEADDVLGTV
     AGQVRGQAPV HIITGDRDLL QLVDDNTRVE LPSRRPGQPG EVYDAEGVVG YLGVRPDQVV
     DYKALVGDIS DNIPGVKGIG EKTAVKLLAE YGTLANLYAH LDDIKGALRQ KLADGRPAAD
     LSYQLARIVI DAPITINLQE CLTRDFDAAP VLALFRELEF RSLAKSLMAG LDAEDVAEPV
     VEGQGWQPTQ VVIVRDEAAL EEMRQALDGA KWISFDLETD SLERMSTGIV GFCLAVAPPT
     AYYVPVGHLS GAAQADSGQM NLFAGSAEPA PGQLSIARVL DAIRPALTNP AIPKVAHNAK
     FDCMILERYG IDVAPVRFDT MIAEWLTDPA TKHKGLKDLA RHRLGAEMTD IENLIGRGKT
     QVTFAQVPIE TAAPYGAADA DMTLRLLPLL QREVEEKGLT KLNDLEMALM PVIAAMERAG
     VRIDVDFFRH MSQDLAAALL RLEQIIYEIA GEPFNINSTQ QLSDILFKKL QLPREGLKKI
     ASGHYSTAAD VLEGLKASDS TGIIAAILEH RELGKLKSTY TDALPLLINP ATGRLHTSFS
     QIGAVTGRLA SSNPNLQNIP IRSEVGQQLR RGFVTEPGWL FLSADYSQVE LRILAHITHD
     ETLVSAFRDD LDIHTATAAA IYGIPLESVT KNQRRFAKTI NFGLIYGMGA FRLARETGLT
     LGEAEKYVVK YFDQLPGVER YLQETKHMAR TKGYVETLFG RRRYFPVFKS LMGDANRQAT
     QRAEREAINH PIQGTAADII KYAMIRLHDE LTARYRARLL LQVHDELLLE VPQEEIEEVR
     QLVIDVMTNA FELDVPLKVE VETGNNWLEL KS
//
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