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Entry: A0A167FM92_9BACL
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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
//
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