ID A0A371SMY8_9BACI Unreviewed; 1437 AA.
AC A0A371SMY8;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 24-JAN-2024, entry version 20.
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=DZB84_01890 {ECO:0000313|EMBL:RFB19027.1};
OS Bacillus sp. HNG.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=2293325 {ECO:0000313|EMBL:RFB19027.1, ECO:0000313|Proteomes:UP000263943};
RN [1] {ECO:0000313|EMBL:RFB19027.1, ECO:0000313|Proteomes:UP000263943}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HNG {ECO:0000313|EMBL:RFB19027.1,
RC ECO:0000313|Proteomes:UP000263943};
RA Gagnon H.N., Maines B.A., Sevigny J.L.;
RT "Genome Assembly of Bacillus sp. HNG.";
RL Submitted (AUG-2018) to the EMBL/GenBank/DDBJ databases.
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. 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:RFB19027.1}.
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DR EMBL; QUQV01000001; RFB19027.1; -; Genomic_DNA.
DR OrthoDB; 9804290at2; -.
DR Proteomes; UP000263943; 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; cd06127; DEDDh; 1.
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 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; 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; 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:UP000263943};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_00356}.
FT DOMAIN 336..403
FT /note="Polymerase/histidinol phosphatase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00481"
FT DOMAIN 421..587
FT /note="Exonuclease"
FT /evidence="ECO:0000259|SMART:SM00479"
SQ SEQUENCE 1437 AA; 162430 MW; C1F9BB5ACC1EAFD0 CRC64;
MELSPQQKER FKVLLQQLEL TDDALVTHFE NAGIVKLMID KENKAWHFVF SFENVIPADV
MRIFSTQLQT KFAHIASVTF SLHVGSQHVT EEMVQAYWPL CLQELDGIAP PILSLLHNQL
PTQQGLKLHI KTRNDTESIA IKKKYGQLIG NVYQSYGFPM FTLETEVELS NKEYEQFLEK
KQQEDQERAL LAVADMQKKE KDKEQANAVT GPITIGYTIK EDEDFKEISS ILDEERRIAV
QGYIFFAETR ELRSGRTLLT FKITDYTDSI LVKVFSRDKE DVQLLQSIKK GMWVRVRGSI
QNDTFVRDLV MIANDINEIQ PMNERKDTAP EGEKRVELHL HTPMSQMDAV TSISQLVGQA
KKWGHTAIAL TDHAGAQSFP EAYSAAKKNG IKMIYGVEAN LVDDGVPIAY NSQHRNLEED
TYVVFDVETT GLSAVYNTII ELAAVKVKNG EIIDRFESFA NPHHRLSATT IDLTGITDDM
VSSAPEVSEV LVKFKEWTGD AILVAHNASF DMGFLNVGYK KAGLEQATNP VIDTLELARF
LYPDLKNHRL NTLCKKFDIE LTQHHRAIYD AEATGFLAVK LLKDAAEKEI MYHDQLNDYM
GQGKSYQRSR PYHATLLAQN DVGLKNLFKL ISLSHIHYYY RVPRIPRSQL QKYREGILVG
SACDKGEVFE GMMQKSPEEV ESIAQFYDYL EVQPPSNYKH LLELDLIQNE RELKDILKNI
VSLGEKLNVP VVATGNVHYL NPEDHIYRKI LVRSQGGANP LNRHSLPEVH FRTTNEMLDC
FSFLDKEKAK EIVVTNTQKV ADMVGDVKPI KDDLYTPKIE GAEDEIRDMS YSMARSIYGE
ELPEIVEKRL EKELKSIIGH GFAVIYLISH KLVKKSLDDG YLVGSRGSVG SSLVATMTEI
TEVNPLPPHY VCPDCKHLEF FNDGSVGSGF DLPDKECPNC GANYKKDGHD IPFETFLGFK
GDKVPDIDLN FSGEYQPRAH NYTKVLFGEE YVYRAGTIGT VAEKTAYGYV KGYANDHNLT
MRGAETDRLV AGCTGVKRTT GQHPGGIIVV PDYMDIYDFS PIQFPADDIN SEWRTTHFDF
HSIHDNVLKL DILGHDDPTV IRMLQDLSGI DPKTIPTDDP EVMKIFSGTE SLGVTEEQIM
CKTGTLGIPE FGTRFVRQML EDTKPTTFSE LVQISGLSHG TDVWLGNAQE LIQNNICTLS
EVIGCRDDIM VYLIYKGLDP SMAFKIMESV RKGKGLTDEF IEEMKKNDVP DWYIDSCLKI
KYMFPKAHAA AYVLMAVRIA YFKVHLPLLY YAAYFTVRAD DFDVEAMVRG SSTIRARMEE
INAKGLDASP KEKNLLTVLE LALEMCERGF AFNKIDLYRS SATEFIIDGD ALIPPFNSIP
GLGTNAAINI VKAREQGEFL SKEDLQKRGK VSKTIMEYLE NHGCLEDMPE QNQLSLF
//
