DPO3_CLOPE
ID DPO3_CLOPE Reviewed; 1449 AA.
AC Q8XJR3;
DT 25-OCT-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 119.
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=CPE1691;
OS Clostridium perfringens (strain 13 / Type A).
OC Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=195102;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=13 / Type A;
RX PubMed=11792842; DOI=10.1073/pnas.022493799;
RA Shimizu T., Ohtani K., Hirakawa H., Ohshima K., Yamashita A., Shiba T.,
RA Ogasawara N., Hattori M., Kuhara S., Hayashi H.;
RT "Complete genome sequence of Clostridium perfringens, an anaerobic flesh-
RT eater.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:996-1001(2002).
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; BA000016; BAB81397.1; -; Genomic_DNA.
DR RefSeq; WP_003469123.1; NC_003366.1.
DR AlphaFoldDB; Q8XJR3; -.
DR SMR; Q8XJR3; -.
DR STRING; 195102.gene:10490955; -.
DR PRIDE; Q8XJR3; -.
DR EnsemblBacteria; BAB81397; BAB81397; BAB81397.
DR KEGG; cpe:CPE1691; -.
DR HOGENOM; CLU_003297_2_0_9; -.
DR OMA; YYAAYFT; -.
DR Proteomes; UP000000818; 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; 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 SMART; SM00479; EXOIII; 1.
DR SMART; SM00481; POLIIIAc; 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..1449
FT /note="DNA polymerase III PolC-type"
FT /id="PRO_0000204575"
FT DOMAIN 435..590
FT /note="Exonuclease"
FT REGION 194..231
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1449 AA; 163628 MW; AE24E2CE7D372B85 CRC64;
MSNEFVKQIN RSIKSDDNLN DLEFEITKFQ LLKKSNTLRT IIKSKDQLSE EQKKIIKQYI
KKAIGFEINI EIMYYIDISD ITLKQVVDQH WNHVCEKIIE KHPVLKEVLL NSPIVIEGEK
IIIKNGSEFL CTFVNKKHID REIKGYIKSF FGINSLVEVK YDESLANKNY NDEKLNENKE
IAKKVIETMK AQAAQEKPVK KESSDNKHKS NGGNKGGYEK KSYKDEPKNE NTILGRNIQG
DTIDISSIDM GSGIVTISGD VFKTDIFETK TGRIILTFFI TDYTSSIAVK CFLRDKDKEH
VLENVKKGLY CKVRGEATMD PYAKEVVIMA RDINKLTKIE RMDTAEEKRV ELHMHTTMSS
MDAVTAASKI VERAAKFGHK AVAITDHGVV QAFPDAQIAA KKNNIKVIYG VEGYLADNGT
PIVINGHEES FDDEYVVFDI ETTGFSSKND KIIEIGAVKL KDGEIVDSFS TFVDPKVNIP
YKITELTSIT QNMVNGQPTI DEVLPKFMEF VGNSVLVAHN AAFDVGFIKK NLMDMGKTLK
NPVMDTVPLA RYLYPDLKKV KLNLVAKHLG ISLENHHRAV DDAKATAEIL KFSFKKMKEE
MDIHDVKTLN EKYLSNIDVK KLPLHHIIIL AKNQTGIKNL YKLVSMAHLD YFARRPRLPK
SIITEYREGL IIGSACEAGQ LYKAVLEGKT DGELKEIASF YDYLEIQPIQ NNEFLIRKGN
VKDEEELREL NRKIYDLGKE MDKPVVATCD CHFLDPNDEV FRRIIMAGQG YGDADNQPPL
YFRTTNEMMK EFEYLGEEAC REVVIENTQK IADMVEAVKP IPDETFPPKI EGAEEEIRNM
TMNKVHSIYG ENLPEVVQKR LDKELNSIIN NGYAVLYLIA QKLVAKSLED GYLVGSRGSV
GSSFVATMSD ITEVNGLPPH YVCPNCKKSE FFLDGSISSG ADLPDKNCPD CGAKYIKDGH
DIPFETFLGF EGDKEPDIDL NFSGEYQAVV HKYTEVLFGK GYVFKAGTIG TVAEKTAYGF
VKKYLQERGL VVSQAEIERL TIGCTGIKRT SGQHPGGIMV VPNDNEIYNF CPIQHPADDV
NTDIITTHFD YHSISGRLLK LDILGHDDPT VLRMLQDLTG LDPKTIPLND PKVISLFTSP
DALGVTKEEL GCEVGSYGLP EFGTKFVRQM LVDTQPKSFA DLVRISGLSH GTDVWLNNAQ
YFIKEGYTTL KDCIATRDDI MVYLMYKDLP PKTAFTIMEK VRKGKGLSEE DEALMREKNV
PDWYIESCKR IKYMFPKGHA VAYVMMAVRI AYYKVYYPEA YYTTYFTVRA DDFDADLICK
GEEAIKAKME ELNSLGNNIS VKEKGLLTIL EISYEMYKRG LNFLKVDLYK SEATKFKIEE
DGIRPPLNAL QGVGDNAAKS IVECRVNGEF ISKEDLRLRS KVSKTVIETL DNHGCLEGMQ
ESNQLSLFG
