ID A0A1R1BXV4_9BACL Unreviewed; 1435 AA.
AC A0A1R1BXV4;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 24-JAN-2024, entry version 25.
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 ECO:0000313|EMBL:OMF14645.1};
GN ORFNames=BK127_18175 {ECO:0000313|EMBL:OMF14645.1};
OS Paenibacillus sp. FSL H7-0331.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX NCBI_TaxID=1920421 {ECO:0000313|EMBL:OMF14645.1, ECO:0000313|Proteomes:UP000187480};
RN [1] {ECO:0000313|EMBL:OMF14645.1, ECO:0000313|Proteomes:UP000187480}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FSL H7-0331 {ECO:0000313|EMBL:OMF14645.1,
RC ECO:0000313|Proteomes:UP000187480};
RA Beno S.M.;
RT "Paenibacillus species isolates.";
RL Submitted (NOV-2016) 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:OMF14645.1}.
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DR EMBL; MRTH01000011; OMF14645.1; -; Genomic_DNA.
DR RefSeq; WP_076232847.1; NZ_MRTH01000011.1.
DR STRING; 1920421.BK127_18175; -.
DR OrthoDB; 9804290at2; -.
DR Proteomes; UP000187480; 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; 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; 1.
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:UP000187480};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_00356}.
FT DOMAIN 335..402
FT /note="Polymerase/histidinol phosphatase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00481"
FT DOMAIN 420..586
FT /note="Exonuclease"
FT /evidence="ECO:0000259|SMART:SM00479"
SQ SEQUENCE 1435 AA; 162096 MW; C2581AEE896E02D2 CRC64;
MSETAEKRQR FEMLMEQARV PQDVVGSFFV DGYIDKVETS HKNKEWTLYI GKSSIVPREV
YVSFCKLIRD KFAHIAAIRF ILRYTDQVTA ESIAHEYWSM FVEWVQREET SVNGWMNKAH
IEVQGNVLTL VMLDSMGLEM AKKKNIGQWV QTYYHTYFGA EFQVRYSKNE KPEEEIKKFE
QQIKEENKMV TEEMMTSIEA EQEADSLNAA EIKLMVGYDI KDAPVPIQMV QDEEKKVTLQ
GAVFGLDSKE LKNGMTLFTF NITDFTDSMM VKAFAKNKED VKIYSLIQNG TWLKLRGKVE
YDRFMQTPEL VLMPNDINEV MAPPDRKDDA AEKRVEFHLH TTMSTMDGIT SVDQYIKTAA
KWGHKAIAIT DHAGIQCFPE ADKAAKKNGI KVIFGLEANV VDDAVPIVVN PRNEDLREIE
YVIFDIETTG LSIINNKIIE LAGVKMKDGK EFDRFASFVN PHEKIPYNIQ QLTNITDDMV
VDAPELEEVL PKFIDFIGDC VLVAHNARFD MGFIHANCKR LGLAPVTNPS LDTLELARLL
FPTMKNHRLN TLSDKFKVGL DNHHRAIDDS IALGYILFHL IKEAVERGLI NMPQLNDNVG
KSLKNQRPFH CCIYAQNAVG KKNLFTLVSL SHTEYFQRVA SIPRSKLVEL REGLIIASGC
EKGEFFEAVL NKSMEEAERV AEFYDVLEIQ PIGVNMHLVD KGLVGSKEHL EDANQRVLQI
GRKLDKLVIA TGNVHYLHPR LKICRDIAIN GITGFSPLKD MKKPEVHFRT TKEMLAEFQY
LGAETAHEVV VKNTAELADR FEEIELFPSK LFTPIIEGAD EEIRQKCYDT AKRIYGDDLH
EVITARLEKE LIPIIKYGFS ANYLISERLV KKSNEDGYLV GSRGSVGSSV VATFLGISEV
NPLPPHYICG SCKHSEWILD GSLMSGFDLP DKSCPTCGER LKGEGQDIPF ETFLGFKGDK
VPDIDLNFSG EYQSVAHNYT KELFGEKCVF RAGTIGTIAE KTAFGYVKKF EEEQGKKWRG
AEINRLASGF TGVKRSTGQH PGGIVVVPDY MDVNDVTPVQ FPADDTNAEW KTTHFDYHAF
ENNLLKLDIL GHDDPTMMRM LQDLTGVDPT TIPMNDPKVM SIFNSTKSLE VSPEQIRTPV
ATYGVPEMGT KFVRQMLQET QPSTFADLLQ ISGLSHGTGV WLGNAQELIR KDTCTIKTVI
GCRDDIMLYL IYKAGMDAGL AFKITESVRK GKGLTAEWKE DMKKHKVPGW YIESCERIEY
MFPKAHAAAY VISAVRTAFF KLYYPIAYYA TYFTVRAEDF EVELLCQGYD AILRRLIEIE
DKGFQALPKE KAMISILEMA LEMTARGFSF KGIDLFKSDA TKFLVDGDSL IVPFSALGGI
GENAAKNIAA SKNDGPFLSI EDFQNRSKAS KTIIELLNSM GCFRGLPETN QLSLF
//
