ID A0A1T2XDE5_9BACL Unreviewed; 1438 AA.
AC A0A1T2XDE5;
DT 10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT 10-MAY-2017, sequence version 1.
DT 24-JAN-2024, entry version 24.
DE RecName: Full=DNA polymerase III PolC-type {ECO:0000256|HAMAP-Rule:MF_00356};
DE Short=PolIII {ECO:0000256|HAMAP-Rule:MF_00356};
DE EC=2.7.7.7 {ECO:0000256|HAMAP-Rule:MF_00356};
GN Name=polC {ECO:0000256|HAMAP-Rule:MF_00356,
GN ECO:0000313|EMBL:OPA77633.1};
GN ORFNames=BVG16_14400 {ECO:0000313|EMBL:OPA77633.1};
OS Paenibacillus selenitireducens.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX NCBI_TaxID=1324314 {ECO:0000313|EMBL:OPA77633.1, ECO:0000313|Proteomes:UP000190188};
RN [1] {ECO:0000313|EMBL:OPA77633.1, ECO:0000313|Proteomes:UP000190188}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ES3-24 {ECO:0000313|EMBL:OPA77633.1,
RC ECO:0000313|Proteomes:UP000190188};
RA Xu D., Yao R., Zheng S.;
RT "Genome analysis of Paenibacillus selenitrireducens ES3-24.";
RL Submitted (JAN-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Required for replicative DNA synthesis. This DNA polymerase
CC also exhibits 3' to 5' exonuclease activity.
CC {ECO:0000256|ARBA:ARBA00003452, ECO:0000256|HAMAP-Rule:MF_00356}.
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, ECO:0000256|HAMAP-
CC Rule:MF_00356};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496,
CC ECO:0000256|HAMAP-Rule:MF_00356}.
CC -!- SIMILARITY: Belongs to the DNA polymerase type-C family. PolC
CC subfamily. {ECO:0000256|HAMAP-Rule:MF_00356}.
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:OPA77633.1}.
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DR EMBL; MSZX01000005; OPA77633.1; -; Genomic_DNA.
DR STRING; 1324314.BVG16_14400; -.
DR OrthoDB; 9804290at2; -.
DR Proteomes; UP000190188; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0008408; F:3'-5' exonuclease activity; IEA:UniProtKB-UniRule.
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:0006261; P:DNA-templated DNA replication; IEA:UniProtKB-UniRule.
DR CDD; cd06127; DEDDh; 1.
DR CDD; cd07435; PHP_PolIIIA_POLC; 1.
DR CDD; cd04484; polC_OBF; 1.
DR Gene3D; 1.10.150.870; -; 1.
DR Gene3D; 3.30.1900.20; -; 2.
DR Gene3D; 6.10.140.1510; -; 1.
DR Gene3D; 3.20.20.140; Metal-dependent hydrolases; 2.
DR Gene3D; 2.40.50.140; Nucleic acid-binding proteins; 1.
DR Gene3D; 1.10.150.700; PolC, middle finger domain; 1.
DR Gene3D; 3.30.420.10; Ribonuclease H-like superfamily/Ribonuclease H; 1.
DR HAMAP; MF_00356; DNApol_PolC; 1.
DR InterPro; IPR011708; DNA_pol3_alpha_NTPase_dom.
DR InterPro; IPR040982; DNA_pol3_finger.
DR InterPro; IPR024754; DNA_PolC-like_N_II.
DR InterPro; IPR028112; DNA_PolC-type_N_I.
DR InterPro; IPR004805; DnaE2/DnaE/PolC.
DR InterPro; IPR029460; DNAPol_HHH.
DR InterPro; IPR006054; DnaQ.
DR InterPro; IPR013520; Exonuclease_RNaseT/DNA_pol3.
DR InterPro; IPR012340; NA-bd_OB-fold.
DR InterPro; IPR004365; NA-bd_OB_tRNA.
DR InterPro; IPR004013; PHP_dom.
DR InterPro; IPR003141; Pol/His_phosphatase_N.
DR InterPro; IPR006308; Pol_III_a_PolC-type_gram_pos.
DR InterPro; IPR044923; PolC_middle_finger_sf.
DR InterPro; IPR012337; RNaseH-like_sf.
DR InterPro; IPR036397; RNaseH_sf.
DR NCBIfam; TIGR00573; dnaq; 1.
DR NCBIfam; TIGR01405; polC_Gram_pos; 1.
DR PANTHER; PTHR32294:SF5; DNA POLYMERASE III POLC-TYPE; 1.
DR PANTHER; PTHR32294; DNA POLYMERASE III SUBUNIT ALPHA; 1.
DR Pfam; PF14480; DNA_pol3_a_NI; 1.
DR Pfam; PF11490; DNA_pol3_a_NII; 1.
DR Pfam; PF07733; DNA_pol3_alpha; 1.
DR Pfam; PF17657; DNA_pol3_finger; 1.
DR Pfam; PF14579; HHH_6; 1.
DR Pfam; PF02811; PHP; 1.
DR Pfam; PF00929; RNase_T; 1.
DR Pfam; PF01336; tRNA_anti-codon; 1.
DR SMART; SM00479; EXOIII; 1.
DR SMART; SM00481; POLIIIAc; 1.
DR SUPFAM; SSF53098; Ribonuclease H-like; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_00356};
KW DNA replication {ECO:0000256|ARBA:ARBA00022705, ECO:0000256|HAMAP-
KW Rule:MF_00356};
KW DNA-directed DNA polymerase {ECO:0000256|ARBA:ARBA00022932,
KW ECO:0000256|HAMAP-Rule:MF_00356};
KW Exonuclease {ECO:0000256|ARBA:ARBA00022839, ECO:0000256|HAMAP-
KW Rule:MF_00356};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|HAMAP-Rule:MF_00356};
KW Nuclease {ECO:0000256|ARBA:ARBA00022722, ECO:0000256|HAMAP-Rule:MF_00356};
KW Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695, ECO:0000256|HAMAP-
KW Rule:MF_00356}; Reference proteome {ECO:0000313|Proteomes:UP000190188};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_00356}.
FT DOMAIN 335..402
FT /note="Polymerase/histidinol phosphatase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00481"
FT DOMAIN 420..586
FT /note="Exonuclease"
FT /evidence="ECO:0000259|SMART:SM00479"
SQ SEQUENCE 1438 AA; 162493 MW; 4D6B1319ED20274F CRC64;
MSNLTEKRNR FDVLLKQAEI PNSMVDAYFT DGYIDRVETS RTNREWTIFI HRDTLLPSPA
YRTFGVQVRE RMSHIAKIKL VFDYASSVTV AEIVEEYWGL FIEWVQREIT SVNGWMSKAQ
IEVEDSLIIV TMSDAMTLEL ARKRQIDEAI QRFYETYFLK TVRVKLQAGE FNEVAYEEFQ
QKLVVDQREV IQQMVNNIEQ EDEVEEDNGE AVKLQVGYEI KEQAVPIQQI QDEEKKITIQ
GAIFGLDVKE LRNGNTLYTY YLTDFTDSLQ MKMFAKTKED VKIMNLLANG KWVRARGKVE
YDRFMQIPEL VMIPSDLVEV KSPPDRMDHA KEKRVEFHLH TTMSTMDAVN SVDEYIKLAA
KWGHKAIAVT DHGNVQCYPE AAKAAKKHGI QMIYGLEANV VNDGVDIVMQ PQPIELKTAT
YVVFDVETTG LSVTSNKIIE LAGVKMCEGR EIDRFAKFIN PHEKIPYNIT QLTNITDEMV
QDAPELEPVI REFIEFVGDS ILVAHNARFD MGFMQKALKK LDMPVITNPV LDTLELARLI
HPKLKNHRLN TLAAKYKVSL ENHHRAIDDS IALGGILYGL LQDAAEQKNM TMLDRLNDYV
GNDLSNVRPF HCGIYALNDV GKKNLFKLIS ISHTDYFKRV ACIPRSKLTE HREGLLVISG
CEKGELFETV LNKTLEEAEE IAQFYDVLEI QPLTMYMHLI EKGLVGSPGH IEQAIQTICR
LGQKLDKPVI ATGNVHYLNP RDKLYRDITI HGITGFSPLK DIRKPDAHLR TTDEMLEEFL
FLGKEKAYEV VVTNTMALAD RFEEIKMFPD NLFTPIIEGA DEEIRETCYS TAKAVYGEEL
PDVIIKRLEK ELVPIIKFGF SANYLISEKL VKKSNKDGYL VGSRGSVGSS VVAMFLGISE
VNPLPPHYVC KNSECRYHEW FLDGSVPSGF DLPNKVCPNC GQPMKGDGHD IPFETFLGFK
GDKVPDIDLN FSGDYQPIAH NFTKEMFGEK NVFRAGTIGT VAEKTAFGFA KKYEEDHHKK
WRGAELNRLA NGCTGVRRST GQHPGGIVVV PDYIDVEDVT PVQFPADDVN AEWKTTHFDY
HAFEANLLKL DILGHDDPTM MRMLQDLTGV DPTSIPMNDP KVMSLFSSTD ALGVRPDQIR
TPVATYGIPE MGTKFVRQML IEAKPSTFAD LLQISGLSHG TGVWLGNAQD LIKNGTCSIK
TVIGCRDEIM LFLIYKAGMD AGLAFKITEN VRKGKGLSDE WIQEMKNCKV PQWYIDSCLK
IQYMFPKAHA AAYVISAVRC AYYKIYHPIA FYATYFSVRG ADFDLDVLCK GYDAIQKMIT
EIEAKGFQAT PKEKGSLSIL EMALEMTARG FSFKPIDIYR SDATKFIVDG DSLIPPFAAI
QGIGENAAKG IAAAKDQGEF LSIEDFQMRS KASKTIVEVL TQMGCFRGLP ESNQLSLF
//
