ID A0A3N9UFL9_9BACI Unreviewed; 1441 AA.
AC A0A3N9UFL9;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 24-JAN-2024, entry version 17.
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=EBB45_08080 {ECO:0000313|EMBL:RQW74928.1};
OS Lysinibacillus composti.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Lysinibacillus.
OX NCBI_TaxID=720633 {ECO:0000313|EMBL:RQW74928.1, ECO:0000313|Proteomes:UP000274033};
RN [1] {ECO:0000313|EMBL:RQW74928.1, ECO:0000313|Proteomes:UP000274033}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MCCC 1A12701 {ECO:0000313|EMBL:RQW74928.1,
RC ECO:0000313|Proteomes:UP000274033};
RX PubMed=23812821; DOI=10.1007/s12275-013-2664-1;
RA Kim S.J., Jang Y.H., Hamada M., Ahn J.H., Weon H.Y., Suzuki K., Whang K.S.,
RA Kwon S.W.;
RT "Lysinibacillus chungkukjangi sp. nov., isolated from Chungkukjang, Korean
RT fermented soybean food.";
RL J. Microbiol. 51:400-404(2013).
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:RQW74928.1}.
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DR EMBL; RRCT01000006; RQW74928.1; -; Genomic_DNA.
DR OrthoDB; 9804290at2; -.
DR Proteomes; UP000274033; 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 Coiled coil {ECO:0000256|SAM:Coils};
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:UP000274033};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_00356}.
FT DOMAIN 340..407
FT /note="Polymerase/histidinol phosphatase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00481"
FT DOMAIN 425..591
FT /note="Exonuclease"
FT /evidence="ECO:0000259|SMART:SM00479"
FT COILED 167..210
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 1441 AA; 162749 MW; 7A48E003DA33CA2B CRC64;
MSEIQEAKER FRTLLQQLQL TEDVYMSFFE DGELTRLTVH KKKRIWEFAM KLQNILPFQL
YQLMRTRMAQ QFANIAQTNI SIEASQPEVT EQLITDYWLL AIEQIDDMSP PLRNRLISQI
PKWTGHKIIA SCMIELEQLT LKSKYTTKIA EAYSQFGFPT IPVEFQLVEA NEELIEAQKT
YMEQRQLEEA AMAKQALEDL QTQEKAKKDN PSVEISGPFQ LGNHIKDTEV MDIKSIIEEE
RRVVIEGFVF AADIKELRSG RSLLEIKITD YTDSILVKMF SRDKEDAEMM THLKKGMWVK
VRGSVQNDTF VRDLVVMAQD INEIFKETRR DTAPEGEKRV ELHLHSPMSQ MDAVTPIDRL
VAQAAKWGHP AIAITDHAVA QGFPDAYAAG KKHGIKIIYG IEANLVDDGA PIAYAEQHIA
LDDATFVVFD VETTGLSTAY DTIIELAAVK IKEGKVIDKF ERFSNPHRPL SAKIIELTHI
TDDMLQDAPE VDQVVTEFRD FIGDSIVVAH NASFDIGFLY TAYEKAGIQG VIHPVIDTLE
LSRFLNPTLK SHRLNTLCKK YGIELTQHHR AIYDTEATGE LMLHLLKDAK EKGIDYHDDF
NKNVGGNESY KNSRPYHCTI LAKDDDGLKN LFKLITIAHT QTYYRVPRIR RSDLMKLRQG
LLIGSGCNNG ELFETMMNKS PDEAEKVAKF YDYIEVQPKP VYSPLIEGGI IHDQWNLEDI
LRKLVKLGKK LDIPVVATGN VHYLDKNDAV FRQILVGSQG GANPLNRYRL PQVHFRTTNE
MLEEFDFLGP DLAKEIVVTN SQKVANMISD VKPIKDKLYT PKIEGSDEEI TKMTYEMAKQ
IYGENLPEIV QKRIEKELAS ILGHGFGVIY LISAKLVKKS LSDGYLVGSR GSVGSSLVAT
FMEITEVNPL PPHYVCPNCK NVEFFDDGSV GSGFDLPNKD CPECGTAYKK DGQDIPFETF
LGFKGDKVPD IDLNFSGEYQ PQAHNYTKVL FGEDYVFRAG TIGTVAEKTA YGYVRGYQND
HNLTYRGAEV DRLVQGCTGV KRTTGQHPGG IIVVPDYMDI YDFTPVQFPA DAQDAEWKTT
HFDFHSIHDN VLKLDILGHD DPTVIRMLQD LSGIDPKTIP TDDPEVMKIF SSPESLGVTE
EQIYCKTGTY GIPEFGTRFV RQMLEDTKPS TFSELVQISG LSHGTDVWLG NAQELIHNGT
CVLSEVIGCR DDIMVYLIYQ GLEPGFAFKI MESVRKGKGL TDEMEEEMRA QKVPEWYIDS
CKKIKYMFPK AHAAAYVLMA VRIAWFKVHH PILYYAAYFT VRASDFDLLA MTKGSPMIRA
RIDEINAKGL DASKKEKDLL TVLELALEMS ERGMTMKNID LYRSQASEFV IDGNSLIPPF
DAIPGLGTNV AKAIVQARGD GEFLSKEDLQ QRGRVSKSLI EYMDQLGCLE GLPDANQLSL
F
//
