ID A0A167FM92_9BACL Unreviewed; 1438 AA.
AC A0A167FM92;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 24-JAN-2024, entry version 35.
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:OAB76704.1};
GN ORFNames=PNBC_04705 {ECO:0000313|EMBL:OAB76704.1};
OS Paenibacillus crassostreae.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX NCBI_TaxID=1763538 {ECO:0000313|EMBL:OAB76704.1, ECO:0000313|Proteomes:UP000077134};
RN [1] {ECO:0000313|EMBL:OAB76704.1, ECO:0000313|Proteomes:UP000077134}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LPB0068 {ECO:0000313|EMBL:OAB76704.1,
RC ECO:0000313|Proteomes:UP000077134};
RA Shin S.-K., Yi H.;
RT "Paenibacillus sp. LPB0068, isolated from Crassostrea gigas.";
RL Submitted (FEB-2016) 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:OAB76704.1}.
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DR EMBL; LSFN01000005; OAB76704.1; -; Genomic_DNA.
DR RefSeq; WP_068655668.1; NZ_LSFN01000005.1.
DR STRING; 1763538.LPB68_20035; -.
DR KEGG; pcx:LPB68_20035; -.
DR OrthoDB; 9804290at2; -.
DR Proteomes; UP000077134; 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; 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; 1.
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; 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:UP000077134};
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 1438 AA; 162324 MW; C10279C2CBA96BBB CRC64;
MSSVEDKRKR FELLMKQGAV PPGIMNPYFM DGYIDQVEIN RSSQEWIISI VKDTIVPGEI
YRAFCLKIQE KMQHIAKISF VFKYSNSVEV KDIIDAYWSL FVDWVHREIP SVNGWMNRAI
HSMDGEQLLL TLADATSLEL AKKKQIDQAI TRFFTTYFSL PFHVKFAVGD SAKEALKEFE
QKKIQEEREV VQNMISAIEF ESNSFEEDSD DVRLHVGYDI KEQPVAIQDI QDEEKKVTIQ
GTIFGLDSKE LRNGSTLYMF NLTDFGDSMQ MKMFAKTKDD VKVLSKLENG KWVKARGRVE
FDRFMQIPEL VMIPSDLNEV QAPPERKDKA PVKRVEFHLH TTMSTMDAIT PIDKYIKTAA
KWGHTAIGIS DHGGVQSFPE ASKAAKKNGL KMLYGVEANV LNDAIPVVLQ PQPIDLKSAT
YIVFDIETTG LSITHSNITE LAAVKIKEGK EIDRYATFVN PHEKIPFHIQ QLTNITDEMV
KDAPDLEPVL HEFVKFAADG ILVAHNARFD IGFIQASLKE YGLPEMPNPV LDTLELARLL
YPTMKNHRLN TMADKYKVLL ESHHRAIDDT IALAGILNGL LVDTEKMKGI TMLDRLNDYV
GKDLSNTRPF HCEIYALNLI GKKNLFKLIS LSHTQYFKRV ACIPRSKLVE LREGLLIISG
CEKGEFFEAV LNKSLEEAED IAQFYDVLEI QPLTMYMHLV DKGFVASALE IKAALKTICQ
IGEKLDKPVI ATGNAHYLEP REKLYRDIAI HGITGFSPLK DMRKPDAHFR TTDEMLEEFD
FLGKDKAYEV VVTNTVELAD QFEDFPLFPD KLYTPIIEGA DEEIRKTCYD TAKSLYGEDL
PEVVTKRLEK ELEPIIKYGF SANYLISERL VKKSNNDGYL VGSRGSVGSS VVATFLGISE
VNPLPAHYFC KNAECKYNEW FLDGSIPSGF DLPDKVCPQC GEKLKGEGQD IPFETFLGFK
GDKVPDIDLN FSGEYQPIAH NFTKEIFGDK CVFRAGTIGT IAEKTAFGYT KKYEEDHQKK
WRGAELSRLA AGFTGVKRGT GQHPGGIVVV PDYMDVEDVT PVQFPADDTK AEWMTTHFDY
HAFESNLLKL DILGHDDPTM MRMLQDLTGV DPTSIVMNDP KVMSLFHSTD ALGVSPQQIR
TPVATYGIPE MGTKFVRQML IESLPTSFAD LLQISGLSHG TGVWLGNAQE LIKNGTCNIK
TVIGCRDDIM LYLIYKAGMD AGMAFTITES VRKGKGLTPE WIEEMKKCKV PTWYIDSCLK
IQYMFPKAHA AAYVISAVRT AFFKLYYPIA YYATYFTVRA EDFDIELCCQ GYEAIYRQIE
VIEQKGFQAT TKEKSMLAIL EMALEMTARG FTFQSIDLYR SDATKFIVDE NSLIPPFSAM
PGIGDNAARN IAAARESGEY LSIEDFQQKS KASKTIIELL TQMGCFRGLP ESNQLSLF
//