ID A0A1A5YMG4_9BACL Unreviewed; 1438 AA.
AC A0A1A5YMG4;
DT 05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2016, sequence version 1.
DT 24-JAN-2024, entry version 29.
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:OBR66814.1};
GN ORFNames=A7K91_16395 {ECO:0000313|EMBL:OBR66814.1};
OS Paenibacillus oryzae.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX NCBI_TaxID=1844972 {ECO:0000313|EMBL:OBR66814.1, ECO:0000313|Proteomes:UP000092024};
RN [1] {ECO:0000313|EMBL:OBR66814.1, ECO:0000313|Proteomes:UP000092024}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1DrF-4 {ECO:0000313|EMBL:OBR66814.1,
RC ECO:0000313|Proteomes:UP000092024};
RA Zhang J., Zhang X.;
RT "Paenibacillus oryzae. sp. nov., isolated from the rice root.";
RL Submitted (MAY-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:OBR66814.1}.
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DR EMBL; LYPA01000043; OBR66814.1; -; Genomic_DNA.
DR STRING; 1844972.A7K91_16395; -.
DR OrthoDB; 9804290at2; -.
DR Proteomes; UP000092024; 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; 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; 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:UP000092024};
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 1438 AA; 161439 MW; 0B7842EC06B08ECB CRC64;
MALKLSKRES FELLLQQAGL PLELVQSYFQ DGEIDQVIVG KSNQEWTFCI SKTSMVPLQA
FNGFCQAVRN KFQHIAAVSF VLKYDDVVET ENILLQYWPL FLEWAQREMS SVNGWLTKAS
MEAQGNAITL SLLDATGLEL AKRKSVDQAI ISFYKRHFER DCRVSLTAGE ARQEVYDQFM
QKIEQEEREA VQQLMAESAA EAPEPGPEGE DAVPLAVGYD IREEPVPLMN IQDEEKKITV
QGMVFGLDVK ELRNGSTLFI FNVTDFTDSV AMKMFAKTKD DVKVLSQLSN GKWVKARGRI
EYDRFMQEPE LVMMPNDLHE VRAPKDRMDN AEEKRVEFHL HTTMSTMDAV TPIGEYVKTA
AKWGHKAIAV SDHSNIQCFP DAVKAAKKHG MKLLFGVEAN VVNDAVPMVL NPRSAVLADA
TYIVFDIETT GLSVVNNKII ELAGVRMRNG KEVDRFSTFI NPHEKIPYHI QQLTNINDDM
VKDAPELEPK LREFVDYIGD DILVAHNARF DIGFIQANCK AIGLPEVQNP VLDTLELARF
LHPTMKNHRL NTLSDKYKIS LENHHRAVDD SVALGGVLFG LIGDAAERNI RNLEQLNDYV
GLDLSNARPF HCNIYALNAA GKKNLFKLIS LSHTDYFKKV ATIPKSKLKE LREGLLVISG
CEKGEFFETV LNKSQEEATE VAEFYDVLEI QPLDFYMHLV EKGLVGSRAE LEGAMRRICE
IGDSLGKPVI ATGNVHYLNP RDKMYRDITI HGITGFSPLK AMRKPEAHFR TTEEMLQEFS
FLGEARAYQV VVTNTSELAE RFETYDMFPK ELFTPNIEGA DEEIRSTCYG TAKAMYGEDL
PQVVIDRLEK ELVPIIKYRF SANYLISEKL VKKSNRDGYL VGSRGSVGSS VVATFLGISE
VNPLPAHYLC KNPECKHSEW FLDGSVPSGF DLPDKLCPHC GKPMKGEGQD IPFETFLGFK
GDKVPDIDLN FSGEYQPIAH NFTKEMFGEK NVYRAGTIGT VAEKTAYGFA KKYEEEHQKK
WRGAELARLA SGCTGVKRST GQHPGGIVVV PDYIEVEDVT PVQYPADDTS AEWKTTHFDY
HAFDENLLKL DILGHDDPTM MRMLQDLTGV DPTTIPMNDP KVMSMFNSTT ALEVAPEKIR
SAVATYGVPE MGTKFVRQML QETQPSSFAD LLQISGLSHG TGVWLGNAQE LIKNGTCNIK
TVIGCRDDIM LYLIYKAGMD AGLAFKITES VRKGKGLTPE WIEEMKNCKV PAWYIDSCLR
IEYMFPKAHA AAYVISAVRT AFFKLYYPIE YYATYFTVRA DDFDLELLCQ GYDAILRKLI
EIEGKGFSAT PKEKAMTSQL EMSLEMTARG FSFKPIDLYR SHATKFQVDG DSLIPPFAAI
AGIGDNAARN IAAAREEGEF LSIEDFQMKS KATKTIIEVL SGMGCFRGLP ESNQLSLF
//
