ID G0VQD7_MEGEL Unreviewed; 1212 AA.
AC G0VQD7;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 24-JAN-2024, entry version 70.
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=MELS_1444 {ECO:0000313|EMBL:CCC73665.1};
OS Megasphaera elsdenii DSM 20460.
OC Bacteria; Bacillota; Negativicutes; Veillonellales; Veillonellaceae;
OC Megasphaera.
OX NCBI_TaxID=1064535 {ECO:0000313|EMBL:CCC73665.1, ECO:0000313|Proteomes:UP000010111};
RN [1] {ECO:0000313|EMBL:CCC73665.1, ECO:0000313|Proteomes:UP000010111}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 20460 {ECO:0000313|EMBL:CCC73665.1,
RC ECO:0000313|Proteomes:UP000010111};
RX PubMed=21914887; DOI=10.1128/JB.05861-11;
RA Marx H., Graf A.B., Tatto N., Thallinger G.G., Mattanovich D., Sauer M.;
RT "Genome Sequence of the Ruminal Bacterium Megasphaera elsdenii.";
RL J. Bacteriol. 193:5578-5579(2011).
CC -!- FUNCTION: Required for replicative DNA synthesis. This DNA polymerase
CC also exhibits 3' to 5' exonuclease activity. {ECO:0000256|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;
CC Evidence={ECO:0000256|ARBA:ARBA00024632, ECO:0000256|HAMAP-
CC Rule:MF_00356};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00356}.
CC -!- SIMILARITY: Belongs to the DNA polymerase type-C family. PolC
CC subfamily. {ECO:0000256|HAMAP-Rule:MF_00356}.
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DR EMBL; HE576794; CCC73665.1; -; Genomic_DNA.
DR RefSeq; WP_014016395.1; NZ_CP027570.1.
DR AlphaFoldDB; G0VQD7; -.
DR STRING; 1064535.MELS_1444; -.
DR KEGG; med:MELS_1444; -.
DR eggNOG; COG0613; Bacteria.
DR eggNOG; COG2176; Bacteria.
DR HOGENOM; CLU_003297_2_1_9; -.
DR Proteomes; UP000010111; 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 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; -; 2.
DR Gene3D; 6.10.140.1510; -; 1.
DR Gene3D; 3.20.20.140; Metal-dependent hydrolases; 1.
DR Gene3D; 2.40.50.140; Nucleic acid-binding proteins; 1.
DR Gene3D; 1.10.150.700; PolC, middle finger domain; 1.
DR HAMAP; MF_00356; DNApol_PolC; 1.
DR InterPro; IPR011708; DNA_pol3_alpha_NTPase_dom.
DR InterPro; IPR040982; DNA_pol3_finger.
DR InterPro; IPR004805; DnaE2/DnaE/PolC.
DR InterPro; IPR029460; DNAPol_HHH.
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; Pol_III_a_PolC-type_gram_pos.
DR InterPro; IPR044923; PolC_middle_finger_sf.
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; PF07733; DNA_pol3_alpha; 2.
DR Pfam; PF17657; DNA_pol3_finger; 1.
DR Pfam; PF14579; HHH_6; 1.
DR Pfam; PF02811; PHP; 1.
DR SMART; SM00481; POLIIIAc; 1.
DR SUPFAM; SSF50249; Nucleic acid-binding proteins; 1.
DR SUPFAM; SSF89550; PHP domain-like; 1.
PE 3: Inferred from homology;
KW Cytoplasm {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:UP000010111};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_00356}.
FT DOMAIN 299..368
FT /note="Polymerase/histidinol phosphatase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00481"
FT REGION 135..157
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1212 AA; 134650 MW; 3B4FC6DB4865D03D CRC64;
MKVWHIVPKN DILIPADGGR SVTIASIAAD LAGHAWHVKT ESPYAIGDMD LLRDRVCRKL
GLDGTVSVEH RVTSVFHGGD MSLAVPDNDP LRQVADISTD DMEGYGIPHE DCYDAIYDVD
DELYDDADYK KACQSASQSG DSSAKKGSKG SGTKTGSDSR VWMGRAFGGD AVSINDVLGE
EQNDVILKGK VVKVEFRELK SKRTLLTFQM ADSTNGISAK KFLDVSNQGG GGKYRRKNTL
TPEEYDNLVK KLKPGVYVRV HGNIQYDNYQ NDYVLMAYDM MEADGGTVER EDHNPTPRVE
LHLHTVMSDM DALITVKQLI KTIKKWGHPA VAVTDHGVVQ SFPLLQEIST DKTNNVKVIY
GMEGYLFDDK IDQSYHIIIL AKNQIGIRNL YKLVSISHLK YIYRGRPRIP RAVLSEYREG
LILGSACEAG ELVRSMVQKK LPYEELKKIA SFYDYLEIQP LTNNGFLVRE GFVADEEGLR
DINRTILKLG DDLGKLTVAT CDAHFMNPED KIYREILMTG KGFKDAEFQP DLYLRTTDEM
LAEFAYLGEE RAREVVITNP NKINDMIADC RPVPKETLYF PQIAGSSEAL KNMCYKKAHE
IYGDPLPKIV EDRLEEEFTS ILGHGFGVLY YIAHKLVKHS NDDGYLVGSR GSVGSSFVAT
MSDITEVNPL PPHYVCPKCQ WSEFFTHGEV GGGFDLPDKV CPQCGTPLHK NGHNIPFAIF
LGFDGDKVPD IDLNFSGEYH PKAHKYTEEL FGKDNVFRAG TIGAVKDKTA YGYVMKWAEA
KGIKVNDAYV NSLVAGCTGI KNTTGQHPGG VMVIPRDMDV HHFTPVQYPA NKKDSGIITT
HFDYHSIEGR LVKLDILGHD DPTVIRMLED MTGIKATTIP FDDPATLSLF SSTKALGVTP
EELGSKVGSL GIPEFGTSFV RQMLVDTKPK TFSELVRISG FSHGTDVWLN NAQDLITSGT
VPLKEAVSTR DDIMNYLIQH GIKPKTSFKV MENVRKGKGI DKLNKLGQKT TDYEGELKAG
HIPQWFIDSC HKIGYLFPRA HAVAYVMMAF RIAWYKINQP LAYYCAFFTI RAKAFKLSAM
IHGLEGQERA MKEIAAKGKS ASKIEQDLYS ALELAKEMSL RGFSFMNVDI NRSAATKFTI
CDGKILPPFT AIDGLGANVA EQIVSAREQA PFSSKADLKM RGKVSQSLVD VMSQEGCLGD
LPEDEQIDLF AM
//
