ID R6XRE4_9FIRM Unreviewed; 1509 AA.
AC R6XRE4;
DT 24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2013, sequence version 1.
DT 24-JAN-2024, entry version 49.
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=BN602_00624 {ECO:0000313|EMBL:CDD21619.1};
OS Firmicutes bacterium CAG:313.
OC Bacteria; Bacillota.
OX NCBI_TaxID=1263017 {ECO:0000313|EMBL:CDD21619.1, ECO:0000313|Proteomes:UP000018373};
RN [1] {ECO:0000313|EMBL:CDD21619.1, ECO:0000313|Proteomes:UP000018373}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MGS:313 {ECO:0000313|Proteomes:UP000018373};
RA Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., Sunagawa S.,
RA Plichta D., Gautier L., Le Chatelier E., Peletier E., Bonde I., Nielsen T.,
RA Manichanh C., Arumugam M., Batto J., Santos M.B.Q.D., Blom N., Borruel N.,
RA Burgdorf K.S., Boumezbeur F., Casellas F., Dore J., Guarner F., Hansen T.,
RA Hildebrand F., Kaas R.S., Kennedy S., Kristiansen K., Kultima J.R.,
RA Leonard P., Levenez F., Lund O., Moumen B., Le Paslier D., Pons N.,
RA Pedersen O., Prifti E., Qin J., Raes J., Tap J., Tims S., Ussery D.W.,
RA Yamada T., MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P.,
RA Wang J., Brunak S., Ehrlich S.D.;
RT "Dependencies among metagenomic species, viruses, plasmids and units of
RT genetic variation.";
RL Submitted (NOV-2012) 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|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:CDD21619.1}.
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DR EMBL; CBGQ010000020; CDD21619.1; -; Genomic_DNA.
DR STRING; 1263017.BN602_00624; -.
DR Proteomes; UP000018373; 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 Gene3D; 1.10.150.870; -; 1.
DR Gene3D; 3.30.1900.20; -; 1.
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; 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; 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; PF07733; DNA_pol3_alpha; 2.
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 SMART; SM00479; EXOIII; 1.
DR SMART; SM00481; POLIIIAc; 1.
DR SUPFAM; SSF53098; Ribonuclease H-like; 1.
PE 3: Inferred from homology;
KW Coiled coil {ECO:0000256|SAM:Coils};
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:UP000018373};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_00356}.
FT DOMAIN 348..415
FT /note="Polymerase/histidinol phosphatase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00481"
FT DOMAIN 434..603
FT /note="Exonuclease"
FT /evidence="ECO:0000259|SMART:SM00479"
FT COILED 165..192
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 1509 AA; 172020 MW; 3B3EF16518C40584 CRC64;
MSLDKIQEIF VNSGVEINDA LATGKLTNVK VNDKTSTWRL CLQFSEIVEP DDLYNMQEKV
AKYIRENFGI KNVKFTVDYD DSTKSTYYAK SSFVKKYLLE AIEVCKEVKK GVIILNEYSL
NLNDNQIEFI VATDEESKTV EENLIVIKKF FLNYGLDFIK FKITIDENAK NIKELSEEKQ
KIKEDLDETK SAEEYKMRKQ LQQENKIQGS YQYKNSGQYI NVKIDDIPYT SMEVSEFKQM
NGTDKVIVFG SIVSAEIRPI RSKQGKDFIL FVGSITNNTD TVMIKRFIYN NQVDEYKENM
KVGKRVEVKG EIRWDDFAKD VVIMCNEIIL LGSDLSRVRF DEAIVKRVEL HAHTKMSVLD
SIMSVEDYVD QASNYGHKAI AVTDHANCHV LPDLFKLCAK KGIKPIAGVE GYYIDEKSLN
IAFTDEDIEL KDATYVVFDI ETTGLYIPFN EIIEIGAVKI KNGLIIDEFA SLIKPKNRVH
KKIMDITHIT NDMLEDQLPI EEVLPKFKEF IKGCILVAHN AHFDSDFIYA ELAKLGIFDG
PMPCLDTMMM ARGLYGGAFK QNNLRAVGKY LKVEVEPNEQ HRAVYDAKTT GNVFLKMLGD
ATDQGITNYN QFNALVTKNE LFRYKIPNHI NILVKNKQGL KNFYKIISES HTTYFQKDAR
ILRSLIEKNR EGILVGSGCA NGEIFRLALE KTYDQLVNAM DFYDYIEVQP PCCYLHLFDM
WSEEEGLEMA KSLINEIIAA ARQKNKMVVA TGDVHELIEE DAQYRKVYLS VARPNGGGPH
ELSHYEGTLD MHYRNTAEML EEFSFLDTDL AYEIVVTNTN KINDMIEEYE LFPKKLYVPR
DDFMTDKNGV ASMKAAVYDI SYQTAYKMYG QPLPKYVQER LDRELDAVIG HGYFSVYYIS
HLLVKNSNDA GYIVGSRGSV GSSFVATMMG ITEVNPLRPH YVCPHCYFSA FKFNEEEKAQ
YNQNISEEME NELNKAGVGV DLKPMKCPVC GHELNRGGLD IAFETFLGFT GEKVPDIDLN
FSGEYQAQAH LFCQKTFGID NAFRAGTVST VQSKTAFAYA RDYYQKIGVF KRQVELERLA
VMLSESKRTT GQHPGGIVVV PDDIEYTDLI PVQYPPISDN DIEGQNWRTS HYDYHKFEDN
LLKLDILGHD DPTVMKFLMD NVHANPDDFP FSTVDGIPYY DEKVISLFAS KDALELKGED
VDTLSSGTIG IPEFGTQFVR GMLETIKPNS ISQIIKVSGL SHGTDVWMKN AEDLVKGTNP
DYPKIKFNEV IGCRDDIMIY LIAIGVSAAN AFKIMEGVRK GKGLTAEQEE LMIKHNVPAW
FIDSCKKIKY LFPKAHAAAY VIMALRIAWF KVYRPIYYYA AYFSKRAKEF DPEAFALGKN
ALTNRINEIE RKIRDHQEVT NKEVDLLDEL KIALEMVLRG YKFRQIDVNI SDATNLVIAP
DKKSLYLPFI AVDSLGETVA QSIVEARKKR AFSSKKDFEM RTSINKKQYA NLVKLEAFGD
LVDDDTTLL
//
