ID W3Y5T3_9FIRM Unreviewed; 1271 AA.
AC W3Y5T3;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 24-JAN-2024, entry version 43.
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=HMPREF1521_0339 {ECO:0000313|EMBL:ETS93548.1};
OS Veillonella sp. AS16.
OC Bacteria; Bacillota; Negativicutes; Veillonellales; Veillonellaceae;
OC Veillonella.
OX NCBI_TaxID=936589 {ECO:0000313|EMBL:ETS93548.1, ECO:0000313|Proteomes:UP000019042};
RN [1] {ECO:0000313|EMBL:ETS93548.1, ECO:0000313|Proteomes:UP000019042}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AS16 {ECO:0000313|EMBL:ETS93548.1,
RC ECO:0000313|Proteomes:UP000019042};
RA Durkin A.S., McCorrison J., Torralba M., Gillis M., Haft D.H., Methe B.,
RA Sutton G., Nelson K.E.;
RL Submitted (JAN-2014) to the EMBL/GenBank/DDBJ databases.
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}.
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:ETS93548.1}.
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DR EMBL; AZYX01000007; ETS93548.1; -; Genomic_DNA.
DR RefSeq; WP_038115112.1; NZ_AZYX01000007.1.
DR AlphaFoldDB; W3Y5T3; -.
DR PATRIC; fig|936589.3.peg.354; -.
DR eggNOG; COG2176; Bacteria.
DR Proteomes; UP000019042; 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 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; SSF160975; AF1531-like; 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};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_00356}.
FT DOMAIN 345..412
FT /note="Polymerase/histidinol phosphatase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00481"
FT REGION 177..225
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 177..192
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1271 AA; 142698 MW; FC2E8CE0B311E61D CRC64;
MKVRYRVVPK QNKKSSFYVN CHSQQVTIQA ADSAFTTLLS LRERLTRWYE EKNISFDAIP
TNTDTSCCFV WKVDTETGEG LDTYYYGGGC GAGEWIEEAE ARREEKEAAL RPKYGQSFAG
IQDSEAESHR DCYDGYDEED DFAPFVEAVE LGYFDNSPIV MPAQTAAAST QCNTVASISS
GQKKSGTKSL SPKGGNLKGA VKAGNGDGKY PHRAPKEIPP EEGMIVGPRF DGDPVSIMSV
QSNENGVIFE GVFVGLEKRD TRTGKSIVSG SICDKTNSMK FIKFTDSPED GDKLLKQLKG
LKTVMVQGNV AYEDRFDKDF VLSIRSIKEV DRTVERSEDR PDSRVELHLH TKMSDKDALV
SVKDLFKTVK KWGHPAVAIT DHGVVQAFPE AQALGKELGV KVIYGVEGYL IDDATVERDE
EPVLDKKKPK VKDKRYHIIL LAKNMVGLRN LYKMISISHL EHYKVRPRIP RSVIEEHREG
IIIGSACEAG ELMQSIVRGA TKEELLEVAS FYDYLEIQPH TNNTFLVRKG LMPDEQALID
MNKTVIELGE ALNKPVCATC DVHYLHPEEK IYREIMLTAC GYPDADEQPD LHLRTTDEML
ASFPYLTPEK AYEVVVTNTR AINDSIEEIK PVPDGTYSPK IEGADEAFTE MCYRNAKAIY
GDPLPRVVQE RLDYELDCII TNGYGVLYYI AHKLVKKSLD DGYLVGSRGS VGSSFAATMS
EITEVNPLPP HYICPHCKWS QFFENGEYAG GFDLPRKQCP ECGHDLETNG HDIPFAIFLG
FEGDKVPDID LNFSGDYQAK AHKYTEELFG RDNVFKAGTI GTIADKTAFG YVKKYAEVRG
IQARNGFFEN LAKGFTNVKN TTGQHPGGIM VCPRDMDVHH FTPIQYPANK KDSGVITTHF
DYHSIEGRMT KLDILGHDDP TIIRMLEDLT GIDAKTIPFD DPKTLSLFSS TEGIGLKPEQ
LQGDQVASLA VPECGTKFVR GMLEDSRPQT FSDLVRISGF SHGTNVWLDN AQDLIKNGTC
KLNEAISTRD DVMNFLIHRG MDRKHSFFVM ENVRKGKGIE KRNKQGEATT EFEAEMRDNN
IPEWFIESCK KISYLFPRAH AVAYVMMAFR IAWFKVYHPL AFYAAYFSIR AKAFDLRIMT
GDLKTQLAEF NRIKALDKAA GPREKDLMSA LEVSMEMYQR GYRFSNVDIQ HSEARRFSIK
DGALLPPFLA IDSLGEKVAD AIVEEREKKP FTSLKDLQRR CKVSNTIIDL MKDLKCCGEL
PEDEQMSLFG A
//
