ID A0Q0R1_CLONN Unreviewed; 1444 AA.
AC A0Q0R1;
DT 09-JAN-2007, integrated into UniProtKB/TrEMBL.
DT 09-JAN-2007, sequence version 1.
DT 27-MAR-2024, entry version 114.
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 ECO:0000313|EMBL:ABK61332.1};
GN OrderedLocusNames=NT01CX_2140 {ECO:0000313|EMBL:ABK61332.1};
OS Clostridium novyi (strain NT).
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=386415 {ECO:0000313|EMBL:ABK61332.1, ECO:0000313|Proteomes:UP000008220};
RN [1] {ECO:0000313|EMBL:ABK61332.1, ECO:0000313|Proteomes:UP000008220}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NT {ECO:0000313|EMBL:ABK61332.1,
RC ECO:0000313|Proteomes:UP000008220};
RX PubMed=17115055; DOI=10.1038/nbt1256;
RA Bettegowda C., Huang X., Lin J., Cheong I., Kohli M., Szabo S.A., Zhang X.,
RA Diaz L.A. Jr., Velculescu V.E., Parmigiani G., Kinzler K.W., Vogelstein B.,
RA Zhou S.;
RT "The genome and transcriptomes of the anti-tumor agent Clostridium novyi-
RT NT.";
RL Nat. Biotechnol. 24:1573-1580(2006).
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; CP000382; ABK61332.1; -; Genomic_DNA.
DR RefSeq; WP_011722213.1; NC_008593.1.
DR STRING; 386415.NT01CX_2140; -.
DR KEGG; cno:NT01CX_2140; -.
DR PATRIC; fig|386415.7.peg.1245; -.
DR eggNOG; COG2176; Bacteria.
DR HOGENOM; CLU_003297_2_0_9; -.
DR Proteomes; UP000008220; 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; 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; 2.
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; 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; PF11490; DNA_pol3_a_NII; 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; 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 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:UP000008220};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_00356}.
FT DOMAIN 346..413
FT /note="Polymerase/histidinol phosphatase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00481"
FT DOMAIN 430..595
FT /note="Exonuclease"
FT /evidence="ECO:0000259|SMART:SM00479"
FT REGION 192..228
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 192..221
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1444 AA; 162388 MW; D17072706940507D CRC64;
MNASLVQILK TELDSNNVYD ENIRILKVKY LSKSNKLKIV LKSTNELEES TKHLIKSVIS
KKLIGFENID LLCYKDISNV SLEDITNKYW VDIVENVSKI IPVCKQVLMS CNKVVEENLL
VIHIGDKFMC NLLQNKNLNK IIQNVISDIF GVKTIVTIKY NSQLKETNYI AVKEQEEKEI
IVSTLKENKA NISSGASKES SHNKNENNKN SNKNTYYKKN HGPKNPNAIF GRDVQGEIED
MVNINETSGV VNICGDIFKV NIIETKSGRK IITFFITDYT SSITVKCFPK PKETDELLEE
IKAGLHCKVR GEAVHDSFAR EVVIMARDIV KTSKLEKMDT CEEKRVELHM HTQMSAMDGL
SSATSLIERA AKWGHPAVAI TDHGVVQAFP EAMDAAKKFN IKVIYGVEAY LVNDGVPIAT
NVKNQNIDDT FVVFDLETTG FSSQYDKIIE FGAVKIKNGN IIDSFSAFVN PEIKIPYKIT
ELTSITNDDV KDAETIDKVL PKFIKFAEGT VLVAHNSNFD MSFIRKNCKD LNIECNYTVM
DTIPLAKFLF PELKRYKLNT IAKHLGVSLE NHHRAVDDAK ATGDILVHCF KLLKEMNITY
LDDLNNKFLG NIDVKKLPTY HLIILAKNQV GLKNLYKLIS FSNLDYFYKK PRMPKSLIEQ
YKEGLIIGSA CEAGEVYKAV LEGKSNEDLK EIIKFYDYLE IQPIMNNEFM LRKGIVKNQD
QLKEINRKIY ELGINNNMPV VATGDVHFLD PKDGKFREIL MAGQGFSDAE NQPPLYLKTT
NEMLKEFEYL GEDIAKEVVI NNPQKIANAV EFVKPIPDET FPPKIDGAEE DIRNMTLEKA
YSIYGNPLPK VVHDRLEKEL NSIINNGYAV LYLIAHKLVA KSLEDGYLVG SRGSVGSSLV
ATMSDITEVN GLPPHYVCPN CKNSEFFTDG SVSSGADLPP KKCPKCGADY NRDGHDIPFE
TFLGFNGDKE PDIDLNFSGD NQGDIHKYTE VLFGKGHTFK AGTIGTIADK TAYGFVKKYL
DEKNMVVSQA EIERLTQGCT GVKRTSGQHP GGIMVVPSDN EIYNFCPIQH PADDANSDII
TTHFDYHSIS GRLLKLDILG HDDPTVLRML KDITGLDPIK IPIGDEKVLS LFTSPEALGV
TAEELECPVG CYGIPEFGTK FVRQMLVDTK PKTFSDLVRI SGLSHGTDVW LNNAQYFIKE
GYTTLKDCIA TRDDIMVYLL HKGLPPKDAF TIMEKVRKGK GLSEEHEALM REHKVPDWYI
ESCKKIKYMF PKGHAVAYVM MAVRIAYYKV YYPEAYYATY FTVRGIDDFD ADLIVKGEEV
IKRKMDEINA LGNSATQKDK GLLTNLELAF EMYKRNIKFL KVDIYKSHPT KFLIEGNYIR
LPIGSLSGVG LNAAKSIADA REGGEFISKE DLRKRSKVSK TVIEALSEHG CLEGLPDTNQ
LSLF
//
