DPO3_CLOTE
ID DPO3_CLOTE Reviewed; 1427 AA.
AC Q895K2;
DT 03-JUL-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 121.
DE RecName: Full=DNA polymerase III PolC-type {ECO:0000255|HAMAP-Rule:MF_00356};
DE Short=PolIII {ECO:0000255|HAMAP-Rule:MF_00356};
DE EC=2.7.7.7 {ECO:0000255|HAMAP-Rule:MF_00356};
GN Name=polC {ECO:0000255|HAMAP-Rule:MF_00356}; OrderedLocusNames=CTC_01271;
OS Clostridium tetani (strain Massachusetts / E88).
OC Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=212717;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Massachusetts / E88;
RX PubMed=12552129; DOI=10.1073/pnas.0335853100;
RA Brueggemann H., Baeumer S., Fricke W.F., Wiezer A., Liesegang H.,
RA Decker I., Herzberg C., Martinez-Arias R., Merkl R., Henne A.,
RA Gottschalk G.;
RT "The genome sequence of Clostridium tetani, the causative agent of tetanus
RT disease.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:1316-1321(2003).
CC -!- FUNCTION: Required for replicative DNA synthesis. This DNA polymerase
CC also exhibits 3' to 5' exonuclease activity. {ECO:0000255|HAMAP-
CC 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; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_00356};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00356}.
CC -!- SIMILARITY: Belongs to the DNA polymerase type-C family. PolC
CC subfamily. {ECO:0000255|HAMAP-Rule:MF_00356}.
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DR EMBL; AE015927; AAO35838.1; -; Genomic_DNA.
DR RefSeq; WP_011099500.1; NC_004557.1.
DR AlphaFoldDB; Q895K2; -.
DR SMR; Q895K2; -.
DR STRING; 212717.CTC_01271; -.
DR EnsemblBacteria; AAO35838; AAO35838; CTC_01271.
DR GeneID; 64179060; -.
DR KEGG; ctc:CTC_01271; -.
DR HOGENOM; CLU_003297_2_0_9; -.
DR OMA; YYAAYFT; -.
DR OrthoDB; 561611at2; -.
DR Proteomes; UP000001412; 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 Gene3D; 1.10.150.700; -; 2.
DR Gene3D; 2.40.50.140; -; 1.
DR Gene3D; 3.30.420.10; -; 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; 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; PolC_gram_pos.
DR InterPro; IPR044923; PolC_middle_finger_sf.
DR InterPro; IPR012337; RNaseH-like_sf.
DR InterPro; IPR036397; RNaseH_sf.
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; SSF50249; 1.
DR SUPFAM; SSF53098; SSF53098; 1.
DR TIGRFAMs; TIGR00573; dnaq; 1.
DR TIGRFAMs; TIGR01405; polC_Gram_pos; 1.
PE 3: Inferred from homology;
KW Cytoplasm; DNA replication; DNA-directed DNA polymerase; Exonuclease;
KW Hydrolase; Nuclease; Nucleotidyltransferase; Reference proteome;
KW Transferase.
FT CHAIN 1..1427
FT /note="DNA polymerase III PolC-type"
FT /id="PRO_0000204576"
FT DOMAIN 413..568
FT /note="Exonuclease"
SQ SEQUENCE 1427 AA; 162360 MW; 23D6582BF9FAD4CD CRC64;
MELAKILEDN TFSQDSLEGI RVHRIQYFKK SNKLKVIVKS KKEVNNNQIT EIKKVFFKKF
QYFKEIEVLS YRDVSGINLK DICEKYWIDI VNSILTYIPF CKECLISSKR KVIDENTLKL
QYGNDFLYNI LKEKNFEKIL SSTIKDVFGV ECKVKFILDK SNGKCNYLDF KEEQEALIIK
NIIKESRIEK TIPKKDNNYN KREENKNSSI IVGKNINEDP VDISNIDETS GIISICGDVF
KTKIIETKTG RKIVTFYITD YTSSITVKLF PKPKDTERVI EEIKEGLYCK IRGEVVNDSY
AREIVIMARD IVKLNKIEKM DIAEEKRVEL HLHTKMSAMD GMNSAESLIK RAAKWGHKAV
AITDHGVVQA YPEAMEAAKK YNIKIIYGVE GYLVDDGIPI AINAGHRTLE DSYVVFDIET
TGFSNKNDKI IEIGAVKIKE GKVVDKYSTF VNPERIIPEK IIELTGIHDY MVKDAPKIEE
VLPKFIDFIE DSILVAHNAN FDVSFIKKNC KDFGIHFNNP ILDTIPLCKF LYPELKRYKL
NVVAKHLGIP LLNHHRAVED AKTTGDILLK AFEDLKDKEI MNLNMLNEEY FKNQDIKKSP
TYHVIILVKN KIGLKNLYKL ISESHLNHFY KKPRMPKSLI NKYREGLMIG SACEAGQVYK
EVLMDKSKEE LKEVISFYDY LEIQPIKNNY FMIRNGIVKD EEELRDINKK IYNLAEENNM
PVVATCDVHF LDKKDEVFRK ILMAGQGFSD AENQPPLYLR TTDEMLKEFE YLGKEKAYKA
VVTNTVKIAD SIDNIKPIPD ETFPPKIEGS EEEVRKMTIE KAHSIYGEVL PEIVEKRLEK
ELNSIINNGY AVLYLIAHKL VDKSVQDGYL VGSRGSVGSS LVATMTDITE VNGLPPHYVC
PGCKYNEFIT DGSVSSGADL PDKNCPNCGV LLSKDGHDIP FETFLGFEGD KEPDIDLNFS
GEYQAVVHKY TEVLFGEGKV FKAGTIGTIA EKTAYGFVKK YISEKDLNVR QAEIERLTLG
CSGVKRTTGQ HPGGIMVVPQ DNEIFNFTPI QRPADDNDTD IITTHFDYHS ISGRLLKLDI
LGHDDPTVLR MLQDLTGVDP KKIPLADPKV MSLFTSPKAL GVNAEELKCE VGTYGLPEFG
TKFVRQMLVD TQPNSFSDLV RISGLSHGTD VWLNNAQYYI KEGYTTLKDC IATRDDIMTY
LIQKDLPPKI AFTIMEKVRK GKGLTEEHEA IMREHDVPGW YIESCKKIKY MFPKGHAVAY
VMMAVRIAYF KVYYPTAYYA TYFSVRASDF DAETVFKGEE AILNKIDEIN SLGNNVTQKD
KGLLTVLEIC HEMNLRGIKF LKADLYKSNA SKFLIEEEGI RIPLSAIQGV GENAAKNIVE
AREEGEFISK EDLNKRGKAT KTVIENLENH GCLRGLPESN QLSLFNL
