ID A0A1Q8Q601_9BACI Unreviewed; 975 AA.
AC A0A1Q8Q601;
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 ORFNames=BTO30_07450 {ECO:0000313|EMBL:OLN22757.1};
OS Domibacillus antri.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Domibacillus.
OX NCBI_TaxID=1714264 {ECO:0000313|EMBL:OLN22757.1, ECO:0000313|Proteomes:UP000185568};
RN [1] {ECO:0000313|EMBL:OLN22757.1, ECO:0000313|Proteomes:UP000185568}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=XD80 {ECO:0000313|EMBL:OLN22757.1,
RC ECO:0000313|Proteomes:UP000185568};
RA Verma A., Krishnamurthi S.;
RT "Domibacillus antri genome sequencing.";
RL Submitted (DEC-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; Evidence={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:OLN22757.1}.
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DR EMBL; MSDU01000014; OLN22757.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Q8Q601; -.
DR STRING; 1714264.BTO30_07450; -.
DR OrthoDB; 9804290at2; -.
DR Proteomes; UP000185568; 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; 3.20.20.140; Metal-dependent hydrolases; 2.
DR Gene3D; 2.40.50.140; Nucleic acid-binding proteins; 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; IPR024754; DNA_PolC-like_N_II.
DR InterPro; IPR028112; DNA_PolC-type_N_I.
DR InterPro; IPR004805; DnaE2/DnaE/PolC.
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; 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; 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 Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_00356};
KW DNA replication {ECO:0000256|HAMAP-Rule:MF_00356};
KW DNA-directed DNA polymerase {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|HAMAP-Rule:MF_00356};
KW Transferase {ECO:0000256|HAMAP-Rule:MF_00356}.
FT DOMAIN 337..404
FT /note="Polymerase/histidinol phosphatase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00481"
FT DOMAIN 422..588
FT /note="Exonuclease"
FT /evidence="ECO:0000259|SMART:SM00479"
SQ SEQUENCE 975 AA; 110092 MW; 257F27659F517BCE CRC64;
MNGDSSSGRS RFLILLEQLR LTEDAVVRHF DETEIKKLTV LKQERKWHFV FSAPALIPCG
ILMRFADALT NTFSSFAAVT FSIDINERSC TPEHITDYWP YCIRQLDGIA PPLLAALNNQ
KPVVSGTKLI FRTQNEMEGM ALKNKYGRRL CDIYESLGFP PLTFDVQVTE NAQNEEYEKF
LEEKRKEDAE RARQAVIDMQ NRVKEQEDGA AEDSGPVTIG YTIKPDSEFK RLEEIIDEER
RIASEGYIFD AETKELRSGR TLLTFKITDY TDSLMVKMFS RDKEDAAMFN RIKKGMWVRV
RGSVQNDTFV RDLVMIANDI NEIRPPSRED TAEKKRVELH LHSPMSQMDA VTSVSTLVSQ
AKKWGHSAIA ITDHAVAQSF PEAYSAGKKN GIKILYGMEA NLVDDGVPIA YGDADRELAS
DTFVVFDVET TGLSAVYDTI IELAAVKIKD GDIIDRFERF ANPHHPLSAT TIELTGITDE
MVKDAPDVDV ALRDFKEWCG DAILVAHNAS FDMGFIQTGY QKYGLGRTDN PVIDTLELAR
LLYPDMKNHR LNTLAKKFDV ELTQHHRAIY DAEATGYILF KLLKEADEKG IKKHNEFNNY
MGEGGAYKRA RPYHCTILAQ NAEGLKNLFK LVSLSHINYF YRVPRIPRSV LQKHRNGLLI
GSGCNKGEVF EAMMQKGMEE ARQAAQFYDY LEVQPKQVNA PLIEMDLVKD EAGLEDIIQN
IIQLGREQEK LVVATGNVHY LNKEDKVYRH ILISSMGGAN PLNRQTLPDV HFRTTDEMLD
AFSFLGEETA HEIVVENSNK IADMIEEVKP IKDDLYTPKI EGADEEMREM SYSMARSIYG
ENLPEIVEAR LEKELKSIIG HGFAVIYLIS HKLVKKSLDD GYLVGSRGSV GSSFVATMTE
ITEVNPLPPH YVCPKCKKSE FFDDGSVGSG FDLEDKDCPD CGIPYKKDGH DIPFETFLGF
KGDKVPDIDL SATRS
//
