ID G7M1Y2_9CLOT Unreviewed; 1447 AA.
AC G7M1Y2;
DT 25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT 25-JAN-2012, sequence version 1.
DT 24-JAN-2024, entry version 63.
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=CDLVIII_1931 {ECO:0000313|EMBL:EHI98615.1};
OS Clostridium sp. DL-VIII.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=641107 {ECO:0000313|EMBL:EHI98615.1, ECO:0000313|Proteomes:UP000005106};
RN [1] {ECO:0000313|EMBL:EHI98615.1, ECO:0000313|Proteomes:UP000005106}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DL-VIII {ECO:0000313|EMBL:EHI98615.1,
RC ECO:0000313|Proteomes:UP000005106};
RX PubMed=23929491;
RA Taghavi S., Izquierdo J.A., van der Lelie D.;
RT "Complete Genome Sequence of Clostridium sp. Strain DL-VIII, a Novel
RT Solventogenic Clostridium Species Isolated from Anaerobic Sludge.";
RL Genome Announc. 1:e00605-e00613(2013).
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; CM001240; EHI98615.1; -; Genomic_DNA.
DR RefSeq; WP_009169293.1; NZ_CM001240.1.
DR STRING; 641107.CDLVIII_1931; -.
DR eggNOG; COG2176; Bacteria.
DR HOGENOM; CLU_003297_2_0_9; -.
DR Proteomes; UP000005106; Chromosome.
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; 1.
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; SSF53098; Ribonuclease H-like; 1.
DR PROSITE; PS50890; PUA; 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:UP000005106};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_00356}.
FT DOMAIN 337..406
FT /note="Polymerase/histidinol phosphatase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00481"
FT DOMAIN 423..588
FT /note="Exonuclease"
FT /evidence="ECO:0000259|SMART:SM00479"
SQ SEQUENCE 1447 AA; 163231 MW; 62D218F5F9437A9B CRC64;
MKKVNEAFSD YESGGKINTA VIENVVLRKK TKILEMEISS DDYIDIEEIE SFNNFIKEKF
ELNDSRITIK YSDGVSIRPI EEELKNIVFS MSKKYPALKA AANNSEYEIA GNTINFNFKI
PVSGFLKAME YDKKINKTIK SLYGMQYNIN FIDKVSSEEI AKMQEDKRAN EIKVLKEIKT
TQGTNAPAAE AAPKVPENKT EIKVEGDSKK NPFLIMGRNA NIKEPIIKIN DITPNEGRIA
LEGEISNIEA KELRSGKMLI SFDLYDGSNS MTCKIFCKPG EYDEVFSRIK KAKGLRLAGN
AGYSNFSHEV ELIANTVIET DGIKKAKRMD NAEVKRVELH MHTQMSQMDA MTSATDLIKR
AMSWGMKSIA ITDHGVVQSF PEAHKLLGRD NPDMKIIYGV EAYLAPDKKP SVTNIKGQSI
DTTYCVLDLE TTGFSPKTEK ITEIGIMKIK DGKVIDKFST FVNPEKSIPM RVVEITNITD
EMVRDAETIG EVFPKMLEFI EGCVLVAHNA EFDINFLKHN ARVLGHDFDF TYLDTLSLAQ
DIFPEFKSYK LGRIAKNLGI KVEVAHRALD DVDTTVKVFN IMLEKLKERG AETLEDIEEY
ASDEESKKAA YKKVKTYHAI ILAKDYVGLK NLYKLVSYSH LDYFYKKPRI LKSMFKKYSE
GLIIGSACSE GELYQSILLG KSEEEIENIA KFYDYLEIQP LGNNDYLVRQ EQVPNKEYLK
EINKKIIRLA EKLNKPVVGT GDVHFMDPED EIYRRILEAG QGFKDADDQA PLYLRTTEEM
LKEFDYLGAE KAYEVVVTNT NKVADMCEQI SPISPEKCPP HIEGCEQTIK DIAYEKAHEL
YGDPLPEIVQ ARLDKELDSI IKNGFSVMYI IAQKLVWKSN EDGYLVGSRG SVGSSFVANM
TGITEVNALP PHYRCPKCKH SDFNDYGVLN GFDLPDKVCP VCGENLHKDG IDIPFETFLG
FNGDKEPDID LNFSGEYQAK AHRYTEVIFG KGTTFKAGTI GTIAEKTAFG YVKKYYEEKN
LPINKAETMR ISVGCTGIKR TTGQHPGGII VVPKGREIFE FCPVQHPADD PNSDIITTHF
DYHSIDQNLL KLDILGHDDP TVIRMLQDIT GVNPHEIPMD DKETMSLFFS TEALSVTPQQ
INSEVGTFGI PEFGTKFVRG MLVDTKPRTF ADLLCISGLS HGTDVWLGNA KDLIDSGVIT
SISDAVCTRD DIMVYLIKKG LPPNTAFKIM ETVRKGKALK EPKWGEYEAL MRENEVPEWY
IDSCKKIKYM FPKAHAAAYV MMAFRIAWFK VHIPQAYYAT YFSIRAKAFD AEFMIFGKEK
VKAKMQEIQA LGNDAAPKDK DMYDDLEIVL EMYERGFKFL PIDLYKSHAT KFQVEEDGIR
PPINSIAGMG NVAAEGIANA AIEKEFNSIE DVRKRSKIGN AAIELLKKFD CLKGLPESDQ
MCFFDAV
//
