DPO3_STRP8
ID DPO3_STRP8 Reviewed; 1465 AA.
AC Q8NZB5;
DT 25-OCT-2002, integrated into UniProtKB/Swiss-Prot.
DT 25-OCT-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}; Synonyms=dnaE;
GN OrderedLocusNames=spyM18_2028;
OS Streptococcus pyogenes serotype M18 (strain MGAS8232).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=186103;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MGAS8232;
RX PubMed=11917108; DOI=10.1073/pnas.062526099;
RA Smoot J.C., Barbian K.D., Van Gompel J.J., Smoot L.M., Chaussee M.S.,
RA Sylva G.L., Sturdevant D.E., Ricklefs S.M., Porcella S.F., Parkins L.D.,
RA Beres S.B., Campbell D.S., Smith T.M., Zhang Q., Kapur V., Daly J.A.,
RA Veasy L.G., Musser J.M.;
RT "Genome sequence and comparative microarray analysis of serotype M18 group
RT A Streptococcus strains associated with acute rheumatic fever outbreaks.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:4668-4673(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; AE009949; AAL98506.1; -; Genomic_DNA.
DR RefSeq; WP_011018243.1; NC_003485.1.
DR AlphaFoldDB; Q8NZB5; -.
DR SMR; Q8NZB5; -.
DR KEGG; spm:spyM18_2028; -.
DR HOGENOM; CLU_003297_2_0_9; -.
DR OMA; YYAAYFT; -.
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; 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; IPR016195; Pol/histidinol_Pase-like.
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; 2.
DR Pfam; PF17657; DNA_pol3_finger; 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 SUPFAM; SSF89550; SSF89550; 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; Transferase.
FT CHAIN 1..1465
FT /note="DNA polymerase III PolC-type"
FT /id="PRO_0000204604"
FT DOMAIN 427..583
FT /note="Exonuclease"
SQ SEQUENCE 1465 AA; 164742 MW; AE7BEDCE5B0E3052 CRC64;
MSDLFAKLMD QIEMPLDMRR SSAFSSADII EVKVHSVSRL WEFHFAFAAV LPIATYRELH
DRLIRTFEAA DIKVTFDIQA AQVDYSDDLL QAYYQEAFEH APCNSASFKS SFSKLKVTYE
DDKLIIAAPR FVNNDHFRNN HLPNLVKQFE AFGFGTLTID MVSDQEMTEH LTKDFVSSRQ
ALVKKAVQDN LEAQKSLEAM MPPVEEATPA PKFDYKERAA KRQAGFEKAT ITPMIEIETE
ENRIVFEGMV FDVERKTTRT GRHIINFKMT DYTSSFALQK WAKDDEELRK FDMIAKGAWL
RVQGNIETNP FTKSLTMNVQ QVKEIVHHDR KDLMPEGQKR VELHAHTNMS TMDALPTVES
LIDTAAKWGH KAVAITDHAN VQSFPHGYHR ARKAGIKAIF GLEANIVEDK VPISYDPVDM
DLHEATYVVF DVETTGLSAM NNDLIQIAAS KMFKGNIVEQ FDEFIDPGHP LSAFTTELTG
ITDKHLQGAK PLVTVLKAFQ DFCKDSILVA HNASFDVGFM NANYERHNLP KITQPVIDTL
EFARNLYPEY KRHGLGPLTK RFQVSLDHHH MANYDAEATG RLLFIFLRDA REKHGIKNLL
QLNTDLVAED SYKKARIKHA TIYVQNQVGL KNMFKLVSLS NIKYFEGVPR IPRTVLDAHR
EGLLLGTACS DGEVFDAVLT KGIDAAVDLA KYYDFIEIMP PAIYQPLVVR ELIKDQAGIE
QVIRDLIEVG KRAKKPVLAT GNVHYLEPEE EIYREIIVRS LGQGAMINRT IGRGEGAQPA
PLPKAHFRTT NEMLDEFAFL GKDLAYQVVV QNTQDFADRI EEVEVVKGDL YTPYIDKAEE
TVAELTYQKA FEIYGNPLPD IIDLRIEKEL TSILGNGFAV IYLASQMLVN RSNERGYLVG
SRGSVGSSFV ATMIGITEVN PMPPHYVCPS CQHSEFITDG SVGSGYDLPN KPCPKCGTPY
QKDGQDIPFE TFLGFDGDKV PDIDLNFSGD DQPSAHLDVR DIFGDEYAFR AGTVGTVAEK
TAYGFVKGYE RDYGKFYRDA EVDRLAAGAA GVKRTTGQHP GGIVVIPNYM DVYDFTPVQY
PADDVTASWQ TTHFNFHDID ENVLKLDILG HDDPTMIRKL QDLSGIDPIT IPADDPGVMA
LFSGTEILGV TPEQIGTPTG MLGIPEFGTN FVRGMVNETH PTTFAELLQL SGLSHGTDVW
LGNAQDLIKE GIATLKTVIG CRDDIMVYLM HAGLEPKMAF TIMERVRKGL WLKISEEERN
GYIDAMRENN VPDWYIESCG KIKYMFPKAH AAAYVLMALR VAYFKVHHPI MYYCAYFSIR
AKAFELKTMS GGLDAVKARM EDITIKRKNN EATNVENDLF TTLEIVNEML ERGFKFGKLD
LYKSDAIEFQ IKGDTLIPPF IALEGLGENV AKQIVKARQE GEFLSKMELR KRGGASSTLV
EKMDEMGILG NMPEDNQLSL FDDFF
