ID A0A242DC08_9ENTE Unreviewed; 1447 AA.
AC A0A242DC08;
DT 25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT 25-OCT-2017, sequence version 1.
DT 24-JAN-2024, entry version 21.
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=A5875_001397 {ECO:0000313|EMBL:OTO20048.1};
OS Enterococcus sp. 3H8_DIV0648.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Enterococcaceae;
OC Enterococcus.
OX NCBI_TaxID=1834178 {ECO:0000313|EMBL:OTO20048.1, ECO:0000313|Proteomes:UP000194623};
RN [1] {ECO:0000313|EMBL:OTO20048.1, ECO:0000313|Proteomes:UP000194623}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=3H8_DIV0648 {ECO:0000313|EMBL:OTO20048.1,
RC ECO:0000313|Proteomes:UP000194623};
RG The Broad Institute Genomics Platform;
RG The Broad Institute Genomic Center for Infectious Diseases;
RA Earl A., Manson A., Schwartman J., Gilmore M., Abouelleil A., Cao P.,
RA Chapman S., Cusick C., Shea T., Young S., Neafsey D., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Enterococcus sp. 3H8_DIV0648.";
RL Submitted (MAY-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:OTO20048.1}.
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DR EMBL; NGLG01000001; OTO20048.1; -; Genomic_DNA.
DR Proteomes; UP000194623; 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; 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; SSF50249; Nucleic acid-binding proteins; 1.
DR SUPFAM; SSF53098; Ribonuclease H-like; 1.
PE 3: Inferred from homology;
KW Coiled coil {ECO:0000256|SAM:Coils};
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};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_00356}.
FT DOMAIN 337..404
FT /note="Polymerase/histidinol phosphatase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00481"
FT DOMAIN 422..588
FT /note="Exonuclease"
FT /evidence="ECO:0000259|SMART:SM00479"
FT COILED 167..205
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 1447 AA; 163046 MW; FFA1E216D7636052 CRC64;
MSKNRELFEN LLRQIELAET EQQHPMIQAA EIKEVVVHEK SRVWEFYIQT PEILPAKLFY
AFYQKLQIAF QSIAKVKLHI VPEDNQFEEE LLQNYWQLAL SEQDCDTPLV KQVLSKPLPV
IQGKRIVLLI DNETVIPFLK QQYLPLIEEN LVSYGFPHLR IDPEVDKEQA DKKLQEFEVR
KQAQAQAMQE QAAASIAQYE SKKKEQKVSA AHFDGPIQMG RNIPADEAIT PMGNIIEEER
RITIEGFIFD KEVRELRSKR KILIIKMTDY TSSFVVKKFS NGEKDEAIFE AIANNSWIRV
RGSVQEDTFM RDLVMNAQDI QEVKHPERQD TATEKRSELH LHTNMSTMDA INGASELVAQ
AGKWGHRAIA ITDHGGAQSF PDAHAAGKKA GVKILYGVEA NVVSDGVPIA YNDAHESLTD
ATYVVFDVET TGLSAVYDTI IELAAVKMHK GNVIDTFEEF IDPGHPLSET TINLTGITDE
MVRGSKPEKE VMELFEKFCE GSILVAHNAT FDIGFINTTY VRHDMPETPN PVIDTLELAR
FLYPEFKRFG LGVLTKKFGI NLEQHHRAVY DAEATGHLAW IFVKEAIEKH DMNYHDQLND
HVGEGDSYKR ARPFHATILA KNQAGLKDLF KLISMSNVEY FERVPRIPRS QLNKLRENLL
VGSACSQGEI FEAMMQKGVE EAKNRAAFYD YIEVMPKAVY APLIEQELVK NESDLEDILR
NLIQIGKDLN KTVVATGDVH YLNKEDAIYR KILISSMGGA NPLNRHSLPD VHFRTTDEML
QAFSFLGPEL AKEIVVDGPN AVVDSCEEIV PVKDDLYTPK IPGSEEEIKK LSYDRARELY
GDPLPDIIEK RLEKELTSII GNGFSVIYLI SQKLVHKSNA DGYLVGSRGS VGSSFVATMT
GITEVNPLPP HYYCPDCQYS EFFEDGSYGS GFDLPEKACP KCGARLNKDG HDIPFETFLG
FHGDKVPDID LNFSGDYQAK AHDYTKVLFG EDYVYRAGTI GTVADKTAYG FVKGYERDHN
LHFRNAEIDR LAKGATGVKR TTGQHPGGII VIPDYMDVYD FTPIQFPADD RNSEWKTTHF
DFHSIHDNVL KLDILGHDDP TVIRMLQELS GVDPKTIPTD DPEVMKIFAG PQVLGVEPDQ
IYSKTGTLGI PEFGTRFVRG MLEETGPTTF AELLQISGLS HGTDVWLGNA EELISRGEAN
LAEVIGCRDD IMVYLIHAGL DSGMAFKIME TVRKGQWNKI DDELRETYLA AMKENNVPDW
YIDSCSKIKY MFPKAHAAAY VLMALRVAYF KVYFPILYYC AYFSVRADDF DLVAMAKGKD
AVKAAMKAIT DKGMDASTKE KNQLTVLELC NEMLERGFHF GMIDLYKSDA QDFVIDGDTL
IAPFRAVPSL GMNVAKQIVE ARKDGIFLSK EDLASRGKVS KTLIEYMDTH GVLKDLPDEN
QLSLFDM
//
