ID A0A0P0EEL5_9MICO Unreviewed; 877 AA.
AC A0A0P0EEL5;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 39.
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=AOA12_09905 {ECO:0000313|EMBL:ALJ20208.1};
OS Microbacterium sp. No. 7.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Microbacterium.
OX NCBI_TaxID=1714373 {ECO:0000313|EMBL:ALJ20208.1, ECO:0000313|Proteomes:UP000059097};
RN [1] {ECO:0000313|EMBL:ALJ20208.1, ECO:0000313|Proteomes:UP000059097}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=No. 7 {ECO:0000313|EMBL:ALJ20208.1,
RC ECO:0000313|Proteomes:UP000059097};
RA Ohtsubo Y., Nagata Y., Numata M., Tsuchikane K., Hosoyama A., Yamazoe A.,
RA Tsuda M., Fujita N., Kawai F.;
RT "Complete genome sequence of a polypropylene glycol-degrading strain
RT Microbacterium sp. No. 7.";
RL Submitted (SEP-2015) 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; CP012697; ALJ20208.1; -; Genomic_DNA.
DR RefSeq; WP_054682396.1; NZ_CP012697.1.
DR AlphaFoldDB; A0A0P0EEL5; -.
DR STRING; 1714373.AOA12_09905; -.
DR KEGG; mio:AOA12_09905; -.
DR PATRIC; fig|1714373.3.peg.2049; -.
DR OrthoDB; 9806424at2; -.
DR Proteomes; UP000059097; 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; 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 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.
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};
KW Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695,
KW ECO:0000256|RuleBase:RU004460};
KW Reference proteome {ECO:0000313|Proteomes:UP000059097};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU004460}.
FT DOMAIN 5..268
FT /note="5'-3' exonuclease"
FT /evidence="ECO:0000259|SMART:SM00475"
FT DOMAIN 633..840
FT /note="DNA-directed DNA polymerase family A palm"
FT /evidence="ECO:0000259|SMART:SM00482"
SQ SEQUENCE 877 AA; 96224 MW; 32E4823C81740B0F CRC64;
MSDSEKPTLL VVDGHSLAYR AFFALPVDNF STKDGQHTNG IYGFLSMFVN LVKAEKPTHL
AVAFDTSRES FRTREYAEYK ANRSESPPEF KGQIPLLQDC LRAMNVTVLT KEDVEADDIL
ATLATQGAEQ GYDVLVCSGD RDTIQLVTEE VTLLYPSVQG VSQLKRYTPD AVVERYGVPP
ENYPDIAALV GETSDNLPGV PKVGEKTAVK WLTQFGTLDE LLARADEIKG VVGGNLREHL
DDVKRNRALN RLLRDVELDV TPAELEVRPV DAQAVRDIFA RLEFRTLLPR VFEALEADGE
DAGAAAAPKP PAPVRTDPAG LAAWAEAAEG PVALTVEIQG GLPTYIGAAT LAAAAESDWN
DDAADALRAW LQGDAPKVLA DAKPQLKALR RAGVHLGGLS YDPVLAGWLL RPSFPDKTLA
HLVDRFLGEE LPEADPSQLV PEKEGASAAE RSWFTLRVTE AMRDELPEGV ASVLVDIELP
TLLTLADMEL AGVAVSHEKL SAFSAELGER AEDTAQRAYA TIGREVNLGS PKQLQEVLFD
QLELPKTRKI KTGYSTDAAT LADLQESNPH PFLDLLLQHR ETTKLRQIIE SLDTAIADDG
RIHTTYLQTA SQTGRLSSTD PNLQNIPIRT EESRRIRGAF EVGEGYETLL TADYSQIEMR
IMAHLSEDAG LIDAFNSGED LHRYVGARVF NVDPSEVTGV MRTRVKAMSY GLVYGLSAFG
LSKQLRIEQA EARQLMQEYF ARFGAVRDYL RSSVERARED GYTATIFGRR RPFPDLTSPN
RVLRENAERA ALNAPIQGSA ADIMKIALNR IHAEFAAAGL ASRVLLQIHD ELVLEIAPGE
WDEAERIVRA RMGDAAELRV PLDVQIGRGP NWDEAGH
//
