DPO3_LIMRD
ID DPO3_LIMRD Reviewed; 1443 AA.
AC A5VJD5;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 10-JUL-2007, sequence version 1.
DT 03-AUG-2022, entry version 92.
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=Lreu_0694;
OS Limosilactobacillus reuteri (strain DSM 20016) (Lactobacillus reuteri).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae;
OC Limosilactobacillus.
OX NCBI_TaxID=557436;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 20016;
RX PubMed=21379339; DOI=10.1371/journal.pgen.1001314;
RA Frese S.A., Benson A.K., Tannock G.W., Loach D.M., Kim J., Zhang M.,
RA Oh P.L., Heng N.C., Patil P.B., Juge N., Mackenzie D.A., Pearson B.M.,
RA Lapidus A., Dalin E., Tice H., Goltsman E., Land M., Hauser L., Ivanova N.,
RA Kyrpides N.C., Walter J.;
RT "The evolution of host specialization in the vertebrate gut symbiont
RT Lactobacillus reuteri.";
RL PLoS Genet. 7:E1001314-E1001314(2011).
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; CP000705; ABQ82959.1; -; Genomic_DNA.
DR RefSeq; WP_003668188.1; NZ_AZDD01000017.1.
DR AlphaFoldDB; A5VJD5; -.
DR SMR; A5VJD5; -.
DR STRING; 557436.Lreu_0694; -.
DR EnsemblBacteria; ABQ82959; ABQ82959; Lreu_0694.
DR GeneID; 66470835; -.
DR KEGG; lre:Lreu_0694; -.
DR PATRIC; fig|557436.17.peg.561; -.
DR eggNOG; COG2176; Bacteria.
DR HOGENOM; CLU_003297_0_0_9; -.
DR OMA; YYAAYFT; -.
DR Proteomes; UP000001991; 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; -; 1.
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; IPR028112; DNA_PolC-type_N_I.
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; PF14480; DNA_pol3_a_NI; 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 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..1443
FT /note="DNA polymerase III PolC-type"
FT /id="PRO_1000059838"
FT DOMAIN 426..582
FT /note="Exonuclease"
SQ SEQUENCE 1443 AA; 163272 MW; 78FBFEDF2F45C8AC CRC64;
MGLSRQELFG KLLEQIHFPE KDNSAFRNAA VQSVVVHKKS RQWEFHLIFN KALPYDLFTQ
FNQSLQLGFK DIAKVSLKIS TPMTELDESQ IANYWQFIIN KAISDTPMLQ QACLQTAPEV
KDGRVTLVVE NEVIKDLLAQ KALDKIEKSY QELGFPKFRI HPFVDQSASQ AKIEELKAKH
EKADAALAAK AAARIKKNEA AKKTAKKSAP VAPADGPVQL GRMIDSKQNV IQMKDIEGEE
RSVVVEGYVF NAEIRELRSG RQLLTFEITD YTSSFSVKKF SRNSDEEAQF ANIKAGMWLK
VRGPVQEDTW MRDLVITAYD VNEVTHIARQ DKAPQDDKRV ELHTHTTMSQ MDATNSITEL
ATRAHKWGHP AIAVTDHGNV QAFPEAFSVA QKTGIKMLYG MEANVVDDGI PLVYNENHEE
LAHQTYVIFD VETTGLSAIY DKVIELSAVK MQDGNVLERF DEFIDPGFPL SEQTTNLTSI
TTEMVQGSKT EEEVFQMFKD FCKGCIIAGH NVSFDMGFMN TGYERHQMGK IAEPVIDTLP
LARFLYPDMR GYRLNTLSKK FKVALEHHHR ANYDSEATGH LLYKFLKDAE ARYDVKYVDD
LNKHMEENNA YRHARPFHVT IFAQTQAGLK NLFKLVSLSN VEYFYRVPRI PRTVLTKYRE
GLLLGTACSS GEVFTAMMEK GYDQALEKAR YYDFIEVQPK PNYAPLLEQH VIADEGHLED
ILKNMVKLGD ELEKTVVATG DVHYLDPHDG IYRKILINSQ GGANPLNRTE RPEVHFRTTD
EMLNEFAFLG EEKAHELVVE NSNKIAAEID DNIRPVKDKL YPPHMKGAEQ EIQDRTWNTA
RKWYGDPLPQ LVQDRIELEL NSIVKNGFSV HYLIAQRLVA KSNKDGYLVG SRGSVGSSVV
ATLSGITEVN PLPPHYRCPN CQFTHFYTQG EYSSGFDLPD KKCPKCGTLM VKDGHDIPFQ
TFLGFKGNKV PDIDLNFSGD YQPIAHNYMK VLFGEKNVFR AGTIGTVADK TAYGYVKAYE
RDTEKEFRKA EEDRLAKGAT GVKRTTGQHP AGIIIVPDDM DIYDFTPVQY PADDQTAAWE
TTHFDFHSIH DNILKMDILG HDDPTMIRAL QDLSGIDPQS IPMDDPGVMA LFSSPKVLGV
TEEQIQSKTG TLGLPEFGTR FVRGMLEDTH PKNYSQLLQI SGLSHGTGVW LDNAQELIKQ
GIATIANVIG CRDNIMTDLI HYGMDSEISF QIMEHVRKGR GIPDEWQEKM HEANVPQWYM
DSCLKIKYMF PRAHAAAYVL MALRIAYFKV YFPLVYYCAF FSVRADDFDV VAMSHGKDAV
KQRMKEINDK GNDASAKEKN LLTILELANE MLERGFKFKM VDIEKSDASD WLIDGDSLIA
PFRAVPGLGL NVAKQIVAAR EERPFLSKED LAERGKVSQT LIDFLTDNHV LDKLPDENQL
SLF
