ID A0A069DDP4_9BACL Unreviewed; 1438 AA.
AC A0A069DDP4;
DT 01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2014, sequence version 1.
DT 24-JAN-2024, entry version 41.
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 ORFNames=TCA2_0195 {ECO:0000313|EMBL:GAK38469.1};
OS Paenibacillus sp. TCA20.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX NCBI_TaxID=1499968 {ECO:0000313|EMBL:GAK38469.1, ECO:0000313|Proteomes:UP000028160};
RN [1] {ECO:0000313|EMBL:GAK38469.1, ECO:0000313|Proteomes:UP000028160}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TCA20 {ECO:0000313|EMBL:GAK38469.1,
RC ECO:0000313|Proteomes:UP000028160};
RA Fujinami S., Takeda-Yano K., Onodera T., Satoh K., Sano M., Takahashi Y.,
RA Narumi I., Ito M.;
RT "Draft Genome Sequence of Calcium-Dependent Paenibacillus sp. Strain TCA20,
RT Isolated from a Hot Spring Containing a High Concentration of Calcium
RT Ions.";
RL Genome Announc. 2:e00866-14(2014).
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:GAK38469.1}.
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DR EMBL; BBIW01000001; GAK38469.1; -; Genomic_DNA.
DR eggNOG; COG2176; Bacteria.
DR OrthoDB; 9804290at2; -.
DR Proteomes; UP000028160; 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; 2.
DR Pfam; PF17657; DNA_pol3_finger; 1.
DR Pfam; PF14579; HHH_6; 1.
DR Pfam; PF02811; PHP; 2.
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; SSF50249; Nucleic acid-binding proteins; 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:UP000028160};
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; 162324 MW; 6584BB0ADC9DFF21 CRC64;
MNGTDEKRKR FELLMKQVDL PAGIVEPHFI DGFIDQVEIS RMNREWHITI TKDTLVPAPV
FKAFCLHIRD KMSHIAKISF TFNYNSAVSE ADIVAEYWNL FLEWVHQQIP SVNGWMNRAT
QDVESGLLTL TMSDGMALEL ARKKQIDQAI TTYYDRYFKL PLKVKMVVGE SNREELEKFE
QKKREEERVV IENMMSMIEA EMAPIEEEEG DVRLQMGYEI KEPAVPIQEV QDEEKKITLQ
GTVFGLDKKE LRNGNTLYMF YLTDFTDSMQ MKVFAKSKED VKIMNLLANG KWVKVRGRVE
YDRFMQVPEL AMIPSDLVEV QAPPTRKDNA AEKRVEFHLH TKMSTMDAVT SIDTYVKTAA
KWGHKAIAVT DHGGVQVYPE AAKAAKKHGV KMIYGLEANI VNDAVEVVMK PQPLELKTAE
YIVFDIETTG LSVTQNKIIE IAAVKMQDDK EVDRFATFVN PHERIPYNIQ QLTNINDEMV
KDAPELEPVL HDFVKFVGDS ILVAHNARFD IGFIQANLKT IGMEPLENPV LDTLELARLL
HPTMKNHRLN TLADKYKVSL ENHHRAIDDT IALAGILTGL LNDAAQLKGI TMLDRLNDYV
GMDLSNARPF HSGIYALNGT GKKNLYKLVS LSHTEHFKRV ATIPKSKLVA HRDGLLIMSG
CEKGEFFEAV LNKSVEEAEE VAQFYDILEI QPVTMYMHLV DKGLVATPDE IKIAIRKVVE
IGEKLGKPVV ATGNVHYLDP RDKIYRDITI HGITGFSPLK DMRKPDAHFR TTDEMLEEFE
FLGKDKAYEV VVTNTSELAD RFEEIQLFPK ELFTPIIEGA EEEIRSKCYE TAKSIYGEEV
PDVVVKRLEK ELEPIIKFGF SANYLISEKL VKKSNEDGYL VGSRGSVGSS VVATFLGISE
VNPLPPHYIC VNPECRHSEW FLDGSVKSGF DLPSKDCPEC GTPYKGEGQD IPFETFLGFK
GDKVPDIDLN FSGEYQPKAH HFTKVMFGEK SVYRAGTIGT VAEKTAFGFA KKYEEAHHKS
WRGAELNRLA SGCTGVKRST GQHPGGIVVV PDYIEVEDVT PVQYPADDTS AEWKTTHFDY
HAFEDNLLKL DILGHDDPTM MRMLQDLTGV DPTTIPMNDP KVMSMFNSTD ALGVTPEQIR
TPVATYGVPE MGTKFVRQML QESQPSTFAD LLQISGLSHG TGVWLGNAQE LIKNGTCNIK
TVIGCRDDIM LFLIYKHGMD AALAFKITES VRKGKGLSQE WIDEMKNCKV PQWYIDSCLK
IQYMFPKAHA SAYVISAVRT AYYKLYYPIE YYATYFSVRA EDFDIELACQ GYEAISRKIV
EIEQLGFQAS TKEKSMLSVL EMALEMTARG FSFKMIDLYR SDATRFTIDG DSLIPPFSAL
AGIGDNAARN IAAAREYGEF LSIEDFQQKS KASKTAVELL TQMGCFRGLP ESNQLSLF
//
