ID A0A1M5QWC9_9CLOT Unreviewed; 1451 AA.
AC A0A1M5QWC9;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, 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 ORFNames=SAMN02745207_00336 {ECO:0000313|EMBL:SHH18435.1};
OS Clostridium grantii DSM 8605.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=1121316 {ECO:0000313|EMBL:SHH18435.1, ECO:0000313|Proteomes:UP000184447};
RN [1] {ECO:0000313|EMBL:SHH18435.1, ECO:0000313|Proteomes:UP000184447}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 8605 {ECO:0000313|EMBL:SHH18435.1,
RC ECO:0000313|Proteomes:UP000184447};
RA Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL Submitted (NOV-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}.
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DR EMBL; FQXM01000002; SHH18435.1; -; Genomic_DNA.
DR RefSeq; WP_073336323.1; NZ_FQXM01000002.1.
DR STRING; 1121316.SAMN02745207_00336; -.
DR OrthoDB; 9804290at2; -.
DR Proteomes; UP000184447; 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; 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; 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; 2.
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; 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; 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:UP000184447};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_00356}.
FT DOMAIN 353..420
FT /note="Polymerase/histidinol phosphatase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00481"
FT DOMAIN 437..602
FT /note="Exonuclease"
FT /evidence="ECO:0000259|SMART:SM00479"
FT REGION 193..236
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 194..225
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1451 AA; 163641 MW; B4235B71A93B1EC5 CRC64;
MNQNFVNSLL EDFNKNEILM NDKLRIEKVQ FLSKSCKMKV YIKSHNSLNG EKISVLKSII
ASKLNGFENI ELIIAKDISN VDISEIVNKY WVDIVAKISE ETPLCKECLI AAEKKLDNNV
LSLHLGEEFI YTFLKGKKIN NHIENSILEM FGAKIKVNIS YNNSIQTMGA DFFKERENKE
REIITNIIKN KGTNESKSSD KKDSQKTFQK DFKGKSKDKQ FYNKEGKSSE NNPNVIVGRD
FNGDTIEIST ITQTSGVVAI CGDIIKSEII ETKSGRKIFV FDVTDYTSSM TIKCFPRPKD
TEKMEEEIKK GIRVKLRGEA TFDTFSREVV IMGRDIIKTT KIEKMDIYEE KRVELHLHTQ
MSSMDAIAPA SKLIERAAKW GHKAIGITDH GVVQAFPEAM DAAKKYNIKV LYGVEAYFVD
DGEPIAINCD EKTIKDSFTV FDIETTGFSS AYDKIIEIGA VKIINGEIVD RFSYFVNPET
NIPFKIIELT GINNEMVKNS ETIEKILPKF VEFAKGTVLV AHNASFDVSF IRKNMSDLNM
KFDFPVLDTI PLSKFLYPEL KRYKLNTVCK YLGISLENHH RAVDDAEATA LIVQESFKRL
KEKAIVTIEE LNKEYLATID IKKMNTYHLI IYAKTQAGLK NLYKLISTSN LDYFFKRPRL
SKSIINQYRD GLIIGSACEA GQVFSSVLQG KSSEEMQEIV KFYDFLEIQP TGNNEFMIKK
GIVKNEDQLK ELNIKVVELG EKFNLPVVAT GDVHFLDEKD SIFREILMAG KGFSDAKDQP
PLYFKTTNEM IKEFEYLGEE KAKEVVIYNT NMIANQIEDI LPIPKETFPP KIEGADDDIR
NMTMQKAKSI YGDPLPDIVQ KRLDKELNSI ISNGYAVLYL IAHKLVAKSL EDGYLVGSRG
SVGSSLVATM TDITEVNGLP AHYVCEKCKY SQFITDGSVS SGVDLPDKDC PNCGENLYKE
GFDIPFETFL GFEGDKEPDI DLNFSGDNQA DIHRYTEVLF GKGHTFKAGT IGTIAEKTAY
GFVKKYLDEN NSKVTTAEIN RLTAGCTGVK RTSGQHPGGI MVVPADNEIY NFCPIQHPAD
DPNSDIITTH FDYHSISGRL LKLDILGHDD PTMLRMLKDI TGIDPTTVPI GDEKVLSLFT
GTDALGITPE ELGCPVATYG LPEFGTKFVR GMLLDTMPQT FSDLVRISGL SHGTDVWLNN
AQYFIKEGLT TLKDCISTRD DIMVYLIYKG LPPQDAFTIM EKVRKGKGLG EKDEELMRQN
SVPDWYIESC KRIKYMFPKG HAVAYVMMAM RIAYYKVYYP EAYYSAFFTV RGLDDFDAEL
ICKGEDAINL KINEINEMGN NISQKEKGLL TVLELSYEMY KRKINLLRVD LYKSEATRFV
IEEKGIRPPL SALAGVGVNA AKAMVEARIH GEFISKEDLR LRTKVTKSVI ETLSIHGCIN
GLPDTNQLCL F
//