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Database: UniProt
Entry: A0A285EA98_9ACTN
LinkDB: A0A285EA98_9ACTN
Original site: A0A285EA98_9ACTN 
ID   A0A285EA98_9ACTN        Unreviewed;       916 AA.
AC   A0A285EA98;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 29.
DE   RecName: Full=DNA polymerase I {ECO:0000256|RuleBase:RU004460};
DE            EC=2.7.7.7 {ECO:0000256|RuleBase:RU004460};
GN   Name=polA {ECO:0000256|RuleBase:RU004460};
GN   ORFNames=SAMN06893097_101948 {ECO:0000313|EMBL:SNX95144.1};
OS   Geodermatophilus sabuli.
OC   Bacteria; Actinomycetota; Actinomycetes; Geodermatophilales;
OC   Geodermatophilaceae; Geodermatophilus.
OX   NCBI_TaxID=1564158 {ECO:0000313|EMBL:SNX95144.1, ECO:0000313|Proteomes:UP000219514};
RN   [1] {ECO:0000313|EMBL:SNX95144.1, ECO:0000313|Proteomes:UP000219514}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 46844 {ECO:0000313|EMBL:SNX95144.1,
RC   ECO:0000313|Proteomes:UP000219514};
RA   Ehlers B., Leendertz F.H.;
RL   Submitted (SEP-2017) 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; OBDO01000001; SNX95144.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A285EA98; -.
DR   OrthoDB; 9806424at2; -.
DR   Proteomes; UP000219514; Unassembled WGS sequence.
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:0016788; F:hydrolase activity, acting on ester bonds; IEA:UniProt.
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; IPR020046; 5-3_exonucl_a-hlix_arch_N.
DR   InterPro; IPR002421; 5-3_exonuclease.
DR   InterPro; IPR036279; 5-3_exonuclease_C_sf.
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   PRINTS; PR00868; DNAPOLI.
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.
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|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};
KW   Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695,
KW   ECO:0000256|RuleBase:RU004460};
KW   Reference proteome {ECO:0000313|Proteomes:UP000219514};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU004460}.
FT   DOMAIN          22..284
FT                   /note="5'-3' exonuclease"
FT                   /evidence="ECO:0000259|SMART:SM00475"
FT   DOMAIN          672..879
FT                   /note="DNA-directed DNA polymerase family A palm"
FT                   /evidence="ECO:0000259|SMART:SM00482"
FT   REGION          1..24
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   916 AA;  99571 MW;  75F81E5806F5CAF5 CRC64;
     MSAPVSAPAS TAVPTGEGGS PPRPRLLLLD GHSLAYRAFF ALPVENFSTT TGQPTNAVYG
     FTSMLINILR DEQPSHLAVA FDVGRKTFRS EIYAEYKANR AESPTDFRGQ VSLIQEVLGA
     LRVPVITAEG YEADDVIATL TVQAVEQGMD VLIGTGDRDA LQLVNEHVTV LYPRKGVSDL
     TRFTPEEVEA KYGLSPVQYP DFAALRGDPS DNLPSIPSVG EKTAAKWVRE YGSLDALVDQ
     VDTVKGKVGE KLREHLSSVL QNRRLTELDR AVPLEVDPGD LAVRAWDRNE VHTLFDNLQF
     RVLRDRLFAT LTSAEPEVEG GFDVAVDEVP AGGLGAWLER HARTGRTGVI FRGTWGRGTG
     ELTGLALAAA DDSATFVDLG PDLDVADEQA LAAWLADPAA EKVVHEVKGP LLAVWARGWE
     LEGVVSDTAL AAYLALPGQR SFDLGDLAVR YLRRELKDTA EPEGQLTLDG LGPSEDDVAR
     EAAHADVLKA VAVNDLSDAL ESVLGQRGGD ALLGAIELPL TRVLAAMEYR GIAADLEFLQ
     ELQREFAEGV AAAAAECYAV IGREVNLGSP KQLQAVLFDE LGLPKTKKIK SGYTTDADAL
     TWLLAQTGHP FLEHLLRHRD VTRLRTVIDG LIPMVDDAGR IHTTFGQTIA ATGRLSSTDP
     NLQNIPIRTA EGRRIRQAFV VGPGYESLMT ADYSQIEMRI MAHLSGDEGL IEAFTSGEDL
     HSFVASRAFN IPIEDVDPEM RRRIKAMSYG LAYGLSAYGL SQQLRISTEE AREQMQAYFE
     RFGGIRDYLD SVVEEARLSG YTETTLGRRR YLPDLTSDNR QRREMAERMA LNAPIQGSAA
     DVIKVAMLNV EKAMAAGGLR SRMLLQVHDE LVLEVAPGER EALEAVVRRE MAGAAELSVP
     LEVSVGFGAS WDAAAH
//
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