ID A0A3P1VDV6_9STRE Unreviewed; 1467 AA.
AC A0A3P1VDV6;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 24-JAN-2024, entry version 18.
DE RecName: Full=DNA polymerase III PolC-type {ECO:0000256|HAMAP-Rule:MF_00356};
DE Short=PolIII {ECO:0000256|HAMAP-Rule:MF_00356};
DE EC=2.7.7.7 {ECO:0000256|HAMAP-Rule:MF_00356};
GN Name=polC {ECO:0000256|HAMAP-Rule:MF_00356};
GN ORFNames=EII38_05275 {ECO:0000313|EMBL:RRD31625.1};
OS Streptococcus minor.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=229549 {ECO:0000313|EMBL:RRD31625.1, ECO:0000313|Proteomes:UP000281771};
RN [1] {ECO:0000313|EMBL:RRD31625.1, ECO:0000313|Proteomes:UP000281771}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OH4621_COT-116 {ECO:0000313|EMBL:RRD31625.1,
RC ECO:0000313|Proteomes:UP000281771};
RA Coil D.A., Jospin G., Darling A.E., Wallis C., Davis I.J., Harris S.,
RA Eisen J.A., Holcombe L.J., O'Flynn C.;
RT "Genomes From Bacteria Associated with the Canine Oral Cavity: a Test Case
RT for Automated Genome-Based Taxonomic Assignment.";
RL Submitted (NOV-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: DNA polymerase III is a complex, multichain enzyme
CC responsible for most of the replicative synthesis in bacteria. This DNA
CC polymerase also exhibits 3' to 5' exonuclease activity. The alpha chain
CC is the DNA polymerase. {ECO:0000256|ARBA:ARBA00025611}.
CC -!- FUNCTION: Required for replicative DNA synthesis. This DNA polymerase
CC also exhibits 3' to 5' exonuclease activity.
CC {ECO:0000256|ARBA:ARBA00003452, ECO:0000256|HAMAP-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;
CC Evidence={ECO:0000256|ARBA:ARBA00024632, ECO:0000256|HAMAP-
CC Rule:MF_00356};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496,
CC ECO:0000256|HAMAP-Rule:MF_00356}.
CC -!- SIMILARITY: Belongs to the DNA polymerase type-C family. DnaE
CC subfamily. {ECO:0000256|ARBA:ARBA00009496}.
CC -!- SIMILARITY: Belongs to the DNA polymerase type-C family. PolC
CC subfamily. {ECO:0000256|HAMAP-Rule:MF_00356}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:RRD31625.1}.
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DR EMBL; RQZA01000003; RRD31625.1; -; Genomic_DNA.
DR STRING; 1123309.GCA_000377005_00708; -.
DR Proteomes; UP000281771; Unassembled WGS sequence.
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 CDD; cd07435; PHP_PolIIIA_POLC; 1.
DR CDD; cd04484; polC_OBF; 1.
DR Gene3D; 1.10.150.870; -; 1.
DR Gene3D; 3.30.1900.20; -; 1.
DR Gene3D; 6.10.140.1510; -; 1.
DR Gene3D; 3.20.20.140; Metal-dependent hydrolases; 2.
DR Gene3D; 2.40.50.140; Nucleic acid-binding proteins; 1.
DR Gene3D; 1.10.150.700; PolC, middle finger domain; 1.
DR Gene3D; 3.30.420.10; Ribonuclease H-like superfamily/Ribonuclease H; 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; IPR004805; DnaE2/DnaE/PolC.
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; IPR004365; NA-bd_OB_tRNA.
DR InterPro; IPR004013; PHP_dom.
DR InterPro; IPR003141; Pol/His_phosphatase_N.
DR InterPro; IPR016195; Pol/histidinol_Pase-like.
DR InterPro; IPR006308; Pol_III_a_PolC-type_gram_pos.
DR InterPro; IPR044923; PolC_middle_finger_sf.
DR InterPro; IPR012337; RNaseH-like_sf.
DR InterPro; IPR036397; RNaseH_sf.
DR NCBIfam; TIGR00573; dnaq; 1.
DR NCBIfam; TIGR01405; polC_Gram_pos; 1.
DR PANTHER; PTHR32294:SF5; DNA POLYMERASE III POLC-TYPE; 1.
DR PANTHER; PTHR32294; DNA POLYMERASE III SUBUNIT ALPHA; 1.
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; PF14579; HHH_6; 1.
DR Pfam; PF02811; PHP; 2.
DR Pfam; PF00929; RNase_T; 1.
DR Pfam; PF01336; tRNA_anti-codon; 1.
DR SMART; SM00479; EXOIII; 1.
DR SMART; SM00481; POLIIIAc; 1.
DR SUPFAM; SSF50249; Nucleic acid-binding proteins; 1.
DR SUPFAM; SSF89550; PHP domain-like; 1.
DR SUPFAM; SSF53098; Ribonuclease H-like; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_00356};
KW DNA replication {ECO:0000256|ARBA:ARBA00022705, ECO:0000256|HAMAP-
KW Rule:MF_00356};
KW DNA-directed DNA polymerase {ECO:0000256|ARBA:ARBA00022932,
KW ECO:0000256|HAMAP-Rule:MF_00356};
KW Exonuclease {ECO:0000256|ARBA:ARBA00022839, ECO:0000256|HAMAP-
KW Rule:MF_00356};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|HAMAP-Rule:MF_00356};
KW Nuclease {ECO:0000256|ARBA:ARBA00022722, ECO:0000256|HAMAP-Rule:MF_00356};
KW Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695, ECO:0000256|HAMAP-
KW Rule:MF_00356}; Reference proteome {ECO:0000313|Proteomes:UP000281771};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_00356}.
FT DOMAIN 343..410
FT /note="Polymerase/histidinol phosphatase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00481"
FT DOMAIN 428..594
FT /note="Exonuclease"
FT /evidence="ECO:0000259|SMART:SM00479"
SQ SEQUENCE 1467 AA; 165652 MW; 91DECDE75F572890 CRC64;
MSDKFQLLLE QIGMPPELRE SGAFSAGKIE NVLLHKISKV WEFTFRLPQV LDISHYQLLK
ARLHNEFAKT GNQARFQIVT DNQEISAQLL QAYYRQAFEE ELCQSAGFKS LFQDLKVTYE
DGQVWIEGPQ SVDTLHFRKN HLPNLIQQFE RFGFGQLRVD IRVCQEMTQQ QEQVFHAQNE
QIYQKANQEN LEALEQLAQM TPPPVSEAQP VGGNFQDFKK KKVARPSLDK EPITPMVEVE
TEENRLVFEG LVFEVEQKTT RTGRVIINFK MTDYTSSFKL QKWAKDEEDA QKFDMIKKGN
WLRVRGNIET NMYTRDLTMN VQDVQEVKKE IRKDLMPEGQ KRIEFHAHTN MSTMDALPPV
EDLIARAAAW GHKAIAITDH ANVQSFPHGY HAARKAGIQA IFGLEANLVE DSIPITFNEV
SMDLKEATYV VFDVETTGLS AEHNSLIQIA ASKMEKGNII EQFDEFIDPG HPLSAFTTEL
TGITDNHVKG SKPLLQVLQE FQAFCQDAVL VAHNASFDVG FMNANYERHG LPLISQPVID
TLEFARNLYP EYKRHGLGPL TKRFQVSLEH HHMANYDAEA TGRLLFIFIN DVRDRHGITN
LVDLNTRLVR EDSYKKARVK HATIYVTNQV GLKNIFKLVS LSNVKYFEGV ARIPKTVLEQ
HREGLILGTA CADGEVFDTL LSQGFEAALS VVDEYDFIEV MPPALYAPLI ARDLIKDEEA
IRQIIRDLIE LGRRSGKPVI ATGNVHYLDP EEEIYREIIV RALGQSSMMN WTIGSGEDAQ
PAPLPKAHFR TTNEMLDEFN FLGENLAREI VITNPNQLLE RFEDIEVVKK DLYTPYIERA
EEQVAEMTYE KAFATYGNPL PDIVDLRIEK ELSSILGNGF AVIYLASQML VQRSNERGYL
VGSRGSVGSS FVATMIGITE VNPMPPHYVC PNCQHSEFIT DGSYGSGFDM PDKNCEKCGH
PYNKDGQDIP FETFLGFDGD KVPDIDLNFS GDDQPDAHLD VRAIFGEEYA FRAGTVGTVA
AKTAYGFVRG YERDYGKFYK DVEVERLAAG AAGVKRTTGQ HPGGIVVIPD YMDVYDFTPV
QYPADDNTAT WQTTHFNFHD IDENILKLDV LGHDDPTMVR KLQQLSGIDP NTIPFDDKGV
MALFTGTEIL GVSPEQIGTP TGMLGIPEFG TNFVRGMVEE THPTTFSELL QLSGLSHGTD
VWLGNAQDLI KSGIANLSTV IGCRDDIMVY LMHAGLPPKM AFNIMERVRK GLWLKISEEE
RNSYIQAMKD NHVPDWYIES CGKIKYMFPK AHAAAYVMMA LRVAYFKVHH PIFYYCAYFS
IRAKAFDLAV MSGGLDKVKA KMEEISLKKK NNEASNVEND LYTTLEIVNE MLERGFKFGK
LDLYKSDAIE FLIEGDTLIP PFVAMDGLGE NVAKQVVAAR AQGEFLSKTE LRKRGGLSST
LVEKMDDMGI LGRMPEDNQL SLFDELF
//
