DPO3_STRS2
ID DPO3_STRS2 Reviewed; 1463 AA.
AC A4W428;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 29-MAY-2007, sequence version 1.
DT 03-AUG-2022, entry version 86.
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=SSU98_1959;
OS Streptococcus suis (strain 98HAH33).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=391296;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=98HAH33;
RX PubMed=17375201; DOI=10.1371/journal.pone.0000315;
RA Chen C., Tang J., Dong W., Wang C., Feng Y., Wang J., Zheng F., Pan X.,
RA Liu D., Li M., Song Y., Zhu X., Sun H., Feng T., Guo Z., Ju A., Ge J.,
RA Dong Y., Sun W., Jiang Y., Wang J., Yan J., Yang H., Wang X., Gao G.F.,
RA Yang R., Wang J., Yu J.;
RT "A glimpse of streptococcal toxic shock syndrome from comparative genomics
RT of S. suis 2 Chinese isolates.";
RL PLoS ONE 2:E315-E315(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; CP000408; ABP93117.1; -; Genomic_DNA.
DR AlphaFoldDB; A4W428; -.
DR SMR; A4W428; -.
DR KEGG; ssv:SSU98_1959; -.
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..1463
FT /note="DNA polymerase III PolC-type"
FT /id="PRO_1000048490"
FT DOMAIN 425..581
FT /note="Exonuclease"
SQ SEQUENCE 1463 AA; 164109 MW; 09C2AF5E46AF7123 CRC64;
MSDKFQLLLQ QIGMPLDARQ SGAFSTATIE KVVLHKVSKL WEFTFRFETP LPLMDYQLFK
ARLATEFEKV GNKIQFSIVS DAEAFEAGLV EAYYPEAFTE DLCQSAGFKA LFQPLEVAYR
DGVLWIKGPE TIDTDHFRKN HLPNLVEQYK RFGFGNLAVD IQVCQEMTQQ QAEIFHAQNA
EIYQQANEEN LAALEQLAQM APPPEAAQPF VPEYKKNRPA KVNIEKAEIT PMIEVDSEEN
RIVFEGLVFE VEQKTTKTGR VIINFKMTDY TSSFTLQKWA KNEEEAQKFD MVKKGNWLRV
RGNVETNNFT RDLTMNVQEV QEVKKEIRKD LMPEGEKRVE FHAHTNMSTM DALPAVEDLV
ARAAAWGHKA VAITDHGNVQ SFPHGYHAAR KAGIKPLFGM EANIVEDSVP IAYNEADVVL
SDATYVVFDV ETTGLSAVNN ALIQIAASKM HKGNIIAEFD EFIDPGHPLS QFTTDLTGIT
DEHVRGSKPL EQVLREFQDF CQDSVMVAHN ATFDVGFMNV NYERAGLPII SQPVIDTLEF
ARNLYPDFKR HGLGPLTKRF GVALEHHHMA NYDAEATGRL LFIFLKDALE KHNLTNLNQL
NTELIAEDSY KKARVKHATL YVINQVGLKN MFKLVSLSNT KYFEGVPRIP RTVLNAHREG
LILGTACQEG EVFDDLLSKG IDEAVKTAAY YDFIEVMPPA LYAPMIAKEQ FKDMAEIEET
IKQLIEVGRR AGLPVLATGN VHYIDPEEEI YREIIVRALG QGAPINWTIG NGENAQPAPL
PKAHFRTTSE MLDEFAFLGE SLAREIVITN PNAMLDRFED VQVVKTDLYT PYIEKAEETV
AELTYQKAFE IYGNPLPDII DLRIEKELTS ILGNGFAVIY LASQMLVHRS NERGYLVGSR
GSVGSSFVAT MIGITEVNPM PPHYVCPNCQ HSEFITDGSY GSGFDLPDKD CEKCGTKYKK
DGQDIPFETF LGFDGDKVPD IDLNFSGDDQ PSAHLDVRDI FGEENAFRAG TVGTVAAKTA
YGFVRGYERD YGKFYRDVEV ERLAAGAAGV KRTTGQHPGG IIVFPDYMDV YDFTPVQYPA
DDVTASWQTT HFNFHDIDEN VLKLDILGHD DPTMVRKLQD LSGIDPQTIP ADDKGVMALF
SGTEILGVTP EQIGTPTGML GIPEFGTNFV RGMVEETKPT TFSELLQLSG LSHGTDVWLG
NAQDLIKAGI ANLSTVIGCR DDIMVYLMHA GLPPKMAFNI MERVRKGLWL KISEEERNGY
IQAMKDNKVP DWYIESCGKI KYMFPKAHAA AYVMMALRVA YFKVHHPLYY YCAYFSIRAK
AFDLATMSGG LERVKAKMEE IALKKKNNEA SNVEQDLYTT LELVNEMLER GFKFGKLDLY
KSHATDFLIE EDTLIPPFVA MDGLGENVAK QVVAARAEGE FLSKTELRKR GGLSGTLVEK
MDEMGILGKM PEDNQLSLFD DLF
