ID R7RP27_9CLOT Unreviewed; 1434 AA.
AC R7RP27;
DT 24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2013, sequence version 1.
DT 24-JAN-2024, entry version 56.
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=TCEL_01861 {ECO:0000313|EMBL:CDF57947.1};
OS Thermobrachium celere DSM 8682.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Thermobrachium.
OX NCBI_TaxID=941824 {ECO:0000313|EMBL:CDF57947.1, ECO:0000313|Proteomes:UP000014923};
RN [1] {ECO:0000313|EMBL:CDF57947.1, ECO:0000313|Proteomes:UP000014923}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 8682 {ECO:0000313|EMBL:CDF57947.1,
RC ECO:0000313|Proteomes:UP000014923};
RA Ciranna A., Larjo A., Kivisto A., Santala V., Roos C., Karp M.;
RT "Draft genome sequence of the hydrogen-ethanol-producing anaerobic
RT alkalithermophilic Caloramator celere.";
RL Submitted (MAR-2013) 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:CDF57947.1}.
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DR EMBL; CAVN010000092; CDF57947.1; -; Genomic_DNA.
DR RefSeq; WP_018661571.1; NZ_HF952018.1.
DR eggNOG; COG2176; Bacteria.
DR HOGENOM; CLU_003297_2_0_9; -.
DR OrthoDB; 9804290at2; -.
DR Proteomes; UP000014923; 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; cd07309; PHP; 1.
DR CDD; cd07435; PHP_PolIIIA_POLC; 1.
DR CDD; cd04484; polC_OBF; 1.
DR Gene3D; 1.10.150.870; -; 1.
DR Gene3D; 1.20.5.140; -; 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; 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; PF07733; DNA_pol3_alpha; 1.
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; SSF160975; AF1531-like; 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:UP000014923};
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 421..586
FT /note="Exonuclease"
FT /evidence="ECO:0000259|SMART:SM00479"
SQ SEQUENCE 1434 AA; 163797 MW; 82187DCC7C5FFB6E CRC64;
MSKALSEVLA NDIELKRYDF LDKLYIEKII IDKKTKKYEF FLKSYIDTDD KIKNNLIDIF
KSKFKIDNNL ELYIDYCKNY IDINNIDDSN IRLLLRDILK QYPSICSVLT SSNINVKEKL
IEFKIDNEFT VNMLKSRQID KLLKTELFKF TNEHLEIRFN YSEIELEEYN KIKYDEDNKI
INQYIQESRE KSDYKALDNN NNVIEKEVKE KEKEKESPYI YGKPVKADFT KISAINETSG
VVEIEGEVFK VDIKETKNGK FIFSFYITDY SSSITVKLFP KNDILDKVKS EISEGKYLKV
IGEATFDKFS NEVVIMAKFI DKKDPIKRMD TCDQKRVELH LHTQMSGMDG VTSATKLIQR
AKEWGHNAIA ITDHGVVQAF PEAMDAAKKY GIKVIYGVEG YLVDDGEPIV YNPKDVLLED
EFVVFDIETT GFNPQTEEII EIGAVKIKNY QIVDRFSVLI NPQKEISLEI EKLTGITNEM
VSDKQTIEEV LPAFIDFIGE AVLVAHNAKF DTGFIREKCK KLNLPFSFSI VDTLPLARWL
LPDLKKHKLN IIAEHLGISL ENHHRAVDDA EATAHIFLKF LDMLKERGAN KLTEVNELYS
GNFDIRKADT YHIVILVKNY QGLYNLYKLV SMAHCNYFFK RPRIPKSLLE QMRDGLIIGT
ACEAGQLYRA ILNNMPERDI EEIVKFYDYL EIQPIANNMF LYESGKVDSV EKLYEYNKKI
VELGEKYNKP VVATGDVHFL DPHDEYFRRI LMAGQGYDDA DNQAPLYFKT TNEMLEEFSY
LGEQKAFEVV VENPNKIADM VEEIKPIPEE TFPPKIDGAD EEIRKMTMDN AHRIYGEKLP
EVVEKRLEKE LNSIINNGYA VLYLIAHKLV AKSLSDGYLV GSRGSVGSSF VATMCGITEV
NPLPPHYVCP NCKNSEFFLD GSVGSGVDLP DKNCPVCNTK YKKDGHDIPF EVFLGFEGDK
EPDIDLNFSG EYQPIAHKYT EELFGEGHVF RAGTIGTIAE KTAYGFVKNY LEERGLKVSS
AEMERLVRGC TGVKRTTGQH PGGIMVVPRD KEIYEFTPIQ KPADDINSDV TTTHFDYHSI
SGRLLKLDIL GHDDPTVLRM LQDLTGIDPK EIPLDDKNVI KLFTSTEPLG ITQEDINCEV
GTLGLPEFGT KFVRQMLIDT QPQNFSDLVR ISGLSHGTDV WLNNAQDIIR QGLATLKEVI
CTRDDIMLYL IYSGVPPKTA FNIMERVRKG KGLRDEDIEI MKQNNVPDWY IQSCNKIKYM
FPKGHAVAYV MMAVRIAYFK VYYPEAYYAT YFTVRADDFD ADLIVKGERA IISKIKEIEA
LGNNVSQKDK GLLTILEIAL EMYKRGLKFI PVDLYKSDAT KFLITEEGIL PPFRALQGVG
ENAAKNIVAA REQGPFVSKE DLRIRAKVSK TVIEILDSHG CLKGLPETNQ LSLF
//
