ID A0A291Q672_9ACTN Unreviewed; 913 AA.
AC A0A291Q672;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 31.
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=KY5_1959c {ECO:0000313|EMBL:ATL26977.1};
OS Streptomyces formicae.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1616117 {ECO:0000313|EMBL:ATL26977.1, ECO:0000313|Proteomes:UP000221011};
RN [1] {ECO:0000313|EMBL:ATL26977.1, ECO:0000313|Proteomes:UP000221011}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KY5 {ECO:0000313|EMBL:ATL26977.1,
RC ECO:0000313|Proteomes:UP000221011};
RA Holmes N.A., Devine R., Qin Z., Seipke R.F., Wilkinson B., Hutchings M.I.;
RT "Complete Genome Sequence of Streptomyces formicae KY5, the formicamycin
RT producer.";
RL Submitted (AUG-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; CP022685; ATL26977.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A291Q672; -.
DR KEGG; sfk:KY5_1959c; -.
DR Proteomes; UP000221011; Chromosome.
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:UP000221011};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU004460}.
FT DOMAIN 20..282
FT /note="5'-3' exonuclease"
FT /evidence="ECO:0000259|SMART:SM00475"
FT DOMAIN 669..876
FT /note="DNA-directed DNA polymerase family A palm"
FT /evidence="ECO:0000259|SMART:SM00482"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..16
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 913 AA; 99512 MW; 9C62961842A9F5CD CRC64;
MAEKAAKKKS ETATKPSGEQ RPRLLLMDGH SLAYRAFFAL PAENFTTATG QPTNAIYGFA
SMLANTLRDE APTHFAVAFD VSRKTWRSEE FPEYKANRSK TPDEFKGQVE LIGEMLDAMH
AVRFAVDGFE ADDVIATLAT QAEAAGFEVL IVTGDRDSFQ LITEHVTVLY PTKGVSELTR
FTPEKVEEKY GLTPSQYPDF AALRGDPSDN LPGIPGVGEK TAAKWINQFG SFADLVERAE
EVKGKAGQNF RDHLDAVKLN RRLTEMVRDV ELPKTVAELE RAPYDRTTLA MVLDTLEIRN
PSLRERLLAV DPGAEEAEQT PAEPGVELDG KVLGTGELAP WLAEHGTAVL GVATVDTWQL
GAGSVTEVAL AAAGGAAAWF DPAALDEADE KAFAAWIADA HKPKVLHNAK AVMRVFPEHG
WRVDGVSMDT ALAAYLVKPG RRSFALDALS LEYLGRELAP ASAAEGQLAF GTEEDDTAEA
ESLMAQARTV LDLGTAFGEK LQEVGASDLL TDIELPTSTL LARLERHGIA ADRAHLEAME
QQFAGAVQQA VKEAHEAAGH EFNLGSPKQL QEVLFGELNL PKTKKTKTGY TTDADALAWL
AAQTENELPV IMLRHREQAK LRVTVEGLIK TIAADGRIHT TFNQTVAATG RLSSTDPNLQ
NIPVRTDEGR AIRRGFVVGE GFESLMTADY SQIELRVMAH LSEDEGLLEA FTSGEDLHTT
VASQVFGVDG SDVDAEMRRK IKAMSYGLAY GLSAFGLSQQ LNIDAGEARA LMDTYFERFG
GVRDYLRRAV DEARATGYTE TMLGRRRYLP DLNSDNRQRR EMAERMALNA PIQGTAADIV
KIAMLNVHRA LTEAKLESRM LLQVHDEIVL EIAAGERAKV EELVRREMAG AVSLRAPLDV
SVGVGADWES AAH
//
