ID A0A1T4XME0_9CLOT Unreviewed; 1450 AA.
AC A0A1T4XME0;
DT 10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT 10-MAY-2017, sequence version 1.
DT 24-JAN-2024, entry version 26.
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=SAMN05428976_1158 {ECO:0000313|EMBL:SKA90697.1};
OS Clostridium sp. USBA 49.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=1881060 {ECO:0000313|EMBL:SKA90697.1, ECO:0000313|Proteomes:UP000190748};
RN [1] {ECO:0000313|EMBL:SKA90697.1, ECO:0000313|Proteomes:UP000190748}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=USBA 49 {ECO:0000313|EMBL:SKA90697.1,
RC ECO:0000313|Proteomes:UP000190748};
RA Peterson S.W.;
RL Submitted (FEB-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}.
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DR EMBL; FUYD01000015; SKA90697.1; -; Genomic_DNA.
DR STRING; 1881060.SAMN05428976_1158; -.
DR OrthoDB; 9804290at2; -.
DR Proteomes; UP000190748; 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 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 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; 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:UP000190748};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_00356}.
FT DOMAIN 336..405
FT /note="Polymerase/histidinol phosphatase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00481"
FT DOMAIN 422..587
FT /note="Exonuclease"
FT /evidence="ECO:0000259|SMART:SM00479"
SQ SEQUENCE 1450 AA; 164194 MW; 2B93357E24A2AB49 CRC64;
MKRINEIFSD YNMSGNISAA LVEAVVLKKK TKCLELKISS DKYIGVREFE YFNKFIKERF
ALEDSEISVK YTDGTDKKPL EEELKNILSF ISNKYPALKA VLTNSEYEIN NNTINFNFKI
AVSNFLKSMK YDKKIKEIIK NLYGTEYKIN FIDKISNEEL LKMEEIKRAN EMMIIQKEIK
SSNNNVIKLS EKTAEIKNES KIEENIKRGD SSLILGRSAN IKEPIIKITD ITPDEGRIAI
EGEISNIETK ELKSGKTLVS FDLYDGSSSM TCKAFLKPGE EDEVLSRLKK AKGVRLCGNS
GYSKFSGEIE LIANTIVETE GIKRIKRMDN AEIKRVELHM HTQMSQMDAM TSATDLIKRA
MSWGMKSIAI TDHGVVQAFP EAHKLLGRDN PDMKVIYGVE AYLAPDKKPS VTNSKGQSID
TTYCVLDLET TGFSPVTEKI TEIGIMKLKD GKVIDKFSCF VNPEKPIPQR VVEVTNITYD
MVKDAETIDK VFPKILDFIN GSVLVAHNAE FDIGFLKHNA KELGYDFDFT YIDTLSLAKE
VFPDFKTYKL GKIAKNLGIK VEVAHRALDD VDTTVKVFDI MLKKLKEKGV KTLDDIDTYG
YDDEAKKEEY KKLKTYHAII LAKNYVGLKN LYKLVSYSHL DYFYKKPRIL KSLYKKYSEG
LILGSACSEG ELYQAILLGK SDEEIEAIAH DYDYLEIQPI GNNDYLVRTE QVPDREYLKE
INKKIVALGE KLNKPVVATC DVHFMDPEDE IYRRILEAGQ GFKDADNQAP LYLRTTEEML
EEFSYLGEEK AYEVVVTNTN KIADMCEKIS PISPEKCPPH IEGCEQTIKD IAYKKAHELY
GDPLPDIVQQ RLDKELDSII KNGFSVMYII AQKLVWKSNE DGYLVGSRGS VGSSVVAYMT
GITEVNALPP HYRCPKCKYS DFTDYGFKIG FDLPDKTCPV CGEVLTKDGI DIPFETFLGF
NGDKEPDIDL NFSGEYQAKA HKYTEVIFGK GTTFKAGTIG TIAEKTAFGY VKKYFEERNI
HVNKAEITRI AKGCTGIKRT TGQHPGGIIV VPKGREIFEF CPVQHPADDP NSDIITTHFD
YHSIDQNLLK LDILGHDDPT VIKMLQDITG VDPKDIPMDD KETMSIFSST EALGVTPEQI
NSKVGTFGIP EFGTKFVRGM LLDTMPKTFS DLICISGLSH GTDVWLGNAK DLIDSGTVTL
SEAVCTRDDI MIYLIKKGLP PNTAFKIMET VRKGKALKDP KWPEYEALMK EHDVPQWYID
SCRKIKYMFP KAHAAAYVMM AFRIAWFKVH IPKAYYAAYF SIRAKAFDAE FMIFGKEKVK
EKMKEIEMMG NQASPKDKDM YDDLELVLEM YERGIKFLPI DLYKSHATKF LVEDEGLRPP
INSISGMGNV AAESIYNTIE QSIKEEKPIN SIEDLKKRAK IGNSAIDLLK KFGCLKHLPE
SNQLSFFDMI
//
