ID A0A090Z1Q4_PAEMA Unreviewed; 889 AA.
AC A0A090Z1Q4;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 46.
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:KFM98375.1};
GN ORFNames=DJ90_4373 {ECO:0000313|EMBL:KFM98375.1}, GNQ08_24175
GN {ECO:0000313|EMBL:MUG25467.1};
OS Paenibacillus macerans (Bacillus macerans).
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX NCBI_TaxID=44252 {ECO:0000313|EMBL:KFM98375.1, ECO:0000313|Proteomes:UP000029278};
RN [1] {ECO:0000313|EMBL:KFM98375.1, ECO:0000313|Proteomes:UP000029278}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=8244 {ECO:0000313|EMBL:KFM98375.1,
RC ECO:0000313|Proteomes:UP000029278};
RA Bishop-Lilly K.A., Broomall S.M., Chain P.S., Chertkov O., Coyne S.R.,
RA Daligault H.E., Davenport K.W., Erkkila T., Frey K.G., Gibbons H.S., Gu W.,
RA Jaissle J., Johnson S.L., Koroleva G.I., Ladner J.T., Lo C.-C.,
RA Minogue T.D., Munk C., Palacios G.F., Redden C.L., Rosenzweig C.N.,
RA Scholz M.B., Teshima H., Xu Y.;
RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:MUG25467.1, ECO:0000313|Proteomes:UP000442469}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=3CT49 {ECO:0000313|EMBL:MUG25467.1,
RC ECO:0000313|Proteomes:UP000442469};
RA Olajide A.M., Chen S., Lapointe G.;
RT "Draft genome sequences of five Paenibacillus species of dairy origin.";
RL Submitted (NOV-2019) 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 -!- SUBUNIT: Single-chain monomer with multiple functions.
CC {ECO:0000256|ARBA:ARBA00011541, ECO:0000256|RuleBase:RU004460}.
CC -!- SIMILARITY: Belongs to the DNA polymerase type-A family.
CC {ECO:0000256|ARBA:ARBA00007705, ECO:0000256|RuleBase:RU004460}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KFM98375.1}.
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DR EMBL; JMQA01000040; KFM98375.1; -; Genomic_DNA.
DR EMBL; WNZZ01000025; MUG25467.1; -; Genomic_DNA.
DR RefSeq; WP_036624367.1; NZ_WNZZ01000025.1.
DR AlphaFoldDB; A0A090Z1Q4; -.
DR STRING; 44252.DJ90_4373; -.
DR GeneID; 77008459; -.
DR PATRIC; fig|44252.3.peg.4941; -.
DR HOGENOM; CLU_004675_0_0_9; -.
DR OrthoDB; 9806424at2; -.
DR Proteomes; UP000029278; Unassembled WGS sequence.
DR Proteomes; UP000442469; Unassembled WGS sequence.
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; 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; 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 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:UP000029278};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU004460}.
FT DOMAIN 2..260
FT /note="5'-3' exonuclease"
FT /evidence="ECO:0000259|SMART:SM00475"
FT DOMAIN 307..482
FT /note="3'-5' exonuclease"
FT /evidence="ECO:0000259|SMART:SM00474"
FT DOMAIN 646..853
FT /note="DNA-directed DNA polymerase family A palm"
FT /evidence="ECO:0000259|SMART:SM00482"
SQ SEQUENCE 889 AA; 99778 MW; DFB85FA14DA66B0E CRC64;
MDKLILIDGN SIIYRAFFAM PPLTNSGGLH TNAVYGFTNM LLRLIQEEQP THILVAFDAG
KTTFRHEGYQ EYKGGRDKTP PELSEQFPLM RDLLESFGIS WFELPGYEAD DIIGTISKQA
EDSGREVLVV TGDKDMLQVV TDRVKVALTR KGVSEVEPYG PKEIEERYGL KPLQIIDLKG
LMGDASDNIP GVPGIGEKTA LKLLHQFGSV EEVLAHTDEL KGKMKENLVN HAEDARLSKQ
LATIFREVPV ERSWEDMKFS GIEEDKAVPM LRKLEFKSLL ERLSFTAGAG GNAAADGEAA
QAAEDVSVTM VDVDTLPEVS AQLAEVEGII IESYGDNPHH ATLMGLLLST PKRHFFLPFE
LLKREEAADV LSWLADENVP KRGYDLHRAD LALFWQGIAF AGAEHDVQLA AYLLDPTEND
QTISGLAAKY GLPHMPADED VYGKGAKFKV PDPETLGRHL ARKGDALLRI VPLQRADLEK
YEMHGLFYDL EMPLSRILAD MEKQGVAVNR EDLKELGVEF EAQINKLVAQ IYEIAGQEFN
LNSPKQLGEI LFDKLGLPVI KKTKTGYSTD AEVLEKLAPY HEIVQFILEY RQLAKLQSTY
VEGLLKEIMP RTGKVHTYFR QTVAATGRLS SQYPNLQNIP IRLEEGRKIR KVFVPSEEGW
FILAADYSQI ELRVLAHISG DKGLQEAFLH DMDIHTKTAM DVFGVGPDEV DANMRRSAKA
VNFGIVYGIS DYGLSQNLNI TRKEAARFIE QYFDAFQGVR RYMDDIVKDA KRDGYVKTLL
ERRRYLPEIN ASNFNLRSFA ERTAMNTPIQ GTAADIIKLA MVKMDKALYE HGLKSRMLLQ
VHDELVFEVP PEELDIMKKL VPETMENAIK LSVPLKAEVS SGVNWYEAK
//
