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DPO3_STRPG
ID   DPO3_STRPG              Reviewed;        1465 AA.
AC   A2RGI3;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   06-MAR-2007, sequence version 1.
DT   03-AUG-2022, entry version 90.
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=SpyM51644;
OS   Streptococcus pyogenes serotype M5 (strain Manfredo).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=160491;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Manfredo;
RX   PubMed=17012393; DOI=10.1128/jb.01227-06;
RA   Holden M.T.G., Scott A., Cherevach I., Chillingworth T., Churcher C.,
RA   Cronin A., Dowd L., Feltwell T., Hamlin N., Holroyd S., Jagels K.,
RA   Moule S., Mungall K., Quail M.A., Price C., Rabbinowitsch E., Sharp S.,
RA   Skelton J., Whitehead S., Barrell B.G., Kehoe M., Parkhill J.;
RT   "Complete genome of acute rheumatic fever-associated serotype M5
RT   Streptococcus pyogenes strain Manfredo.";
RL   J. Bacteriol. 189:1473-1477(2007).
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; AM295007; CAM30965.1; -; Genomic_DNA.
DR   RefSeq; WP_011889165.1; NC_009332.1.
DR   AlphaFoldDB; A2RGI3; -.
DR   SMR; A2RGI3; -.
DR   KEGG; spf:SpyM51644; -.
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_1000048488"
FT   DOMAIN          427..583
FT                   /note="Exonuclease"
SQ   SEQUENCE   1465 AA;  164739 MW;  B07252A9561833A7 CRC64;
     MSDLFAKLMD QIEMPLDMRR SSAFSSADII EVKVHSVSRL WEFHFAFAAV LPIATYRELH
     DRLIRTFEAA DIKVTFDIQA AQVDYSDDLL QAYYQEAFEH APCNSASFKS SFSKLKVTYE
     NDKLIIAAPR FVNNDHFRKN HLPNLVKQLE AFGFGTLTID MVSDQEMTEH LTKDFVSSRQ
     ALVKKAVQDN LEAQKSLEAM MPPVEEATPA PKFDYKERAA KRQAGFEKAT ITPMIEIETE
     ENRIVFEGMV FDVERKTTRT GRHIINFKMT DYTSSFALQK WAKDDEELRK FDMIAKGAWL
     RVQGNIETNP FTKSLTMNVQ QVKEIVHHER KDLMPEGQKR VELHAHTNMS TMDALPTVES
     LIDTAAKWGH KAVAITDHAN VQSFPHGYHR ARKAGIKAIF GLEANIVEDK APISYDPVDM
     DLHEATYVVF DVETTGLSAM NNDLIQIAAS KMFKGNIVEQ FDEFIDPGHP LSAFTTELTG
     ITDKHLQGAK PLVTVLKAFQ DFCKDSILVA HNASFDVGFM NANYERHDLP KITQPVIDTL
     EFARNLYPEY KRHGLGPLTK RFQVSLDHHH MANYDAEATG RLLFIFLRDA REKHGIKNLL
     QLNTDLVAED SYKKARIKHA TIYVQNQVGL KNMFKLVSLS NIKYFEGVPR IPRTVLDAHR
     EGLLLGTACS DGEVFDAVLT KGIDAAVDLA KYYDFIEIMP PAIYQPLVVR ELIKDQAGIE
     QVIRDLIEVG KRANKPVLAT GNVHYLEPEE EIYREIIVRS LGQGAMINRT IGRGEGAQPA
     PLPKAHFRTT NEMLDEFAFL GKDLAYQVVV ENTQDFADRI 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 GVATLKTVIG CRDDIMVYLM HAGLEPKMAF TIMERVRKGL WLKISEEERN
     GYIDAMRENN VPDWYIESCG KIKYMFPKAH AAAYVLMALR VAYFKVHHPI MYYCAYFSIR
     AKAFELKTMS DGLDAVKARM EDITIKRKNN EATNVENDLF TTLEIVNEML ERGFKFGKLD
     LYKSDAIEFQ IKGDTLIPPF IALEGLGENV AKQIVKARQE GEFLSKMELR KRGGASSTLV
     EKMDEMGILG NMPEDNQLSL FDDFF
 
 
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