ID A0A1S9CQ76_9FIRM Unreviewed; 1460 AA.
AC A0A1S9CQ76;
DT 10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT 10-MAY-2017, sequence version 1.
DT 24-JAN-2024, entry version 27.
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=ATN35_00275 {ECO:0000313|EMBL:OON99067.1};
OS Epulopiscium sp. Nele67-Bin004.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae;
OC Candidatus Epulonipiscium.
OX NCBI_TaxID=1764962 {ECO:0000313|EMBL:OON99067.1, ECO:0000313|Proteomes:UP000190174};
RN [1] {ECO:0000313|Proteomes:UP000190174}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Ngugi D.K., Miyake S., Stingl U.;
RL Submitted (AUG-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:OON99067.1}.
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DR EMBL; LNZQ01000164; OON99067.1; -; Genomic_DNA.
DR Proteomes; UP000190174; 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; 1.20.5.140; -; 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; 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; 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 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:UP000190174};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_00356}.
FT DOMAIN 349..417
FT /note="Polymerase/histidinol phosphatase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00481"
FT DOMAIN 434..599
FT /note="Exonuclease"
FT /evidence="ECO:0000259|SMART:SM00479"
FT REGION 189..224
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 189..212
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1460 AA; 165662 MW; F40038CD7D8765CD CRC64;
MSTKAFFEVL PDLVVEKNLH KLFAPSTINE VEFQKASNKL VFNIESPNLL PYYSKKKMRE
QIKTKLFNTA EVKIDFNISY ALDEDYSVER ITTEYKESIV DELQDNELMY YLLLKNSDWE
ISNDTLIIKN ANNPLLEKSF GDIKLYISKL YKQRFNKQIN CTLQLSDITD ENFDETQKLK
VYMAKSQAQQ ASQTAKPKQK PMDQLDNFNS RPQQPERKPR QKVNTEGLIY GRNCEGDVIE
IYHIVDEIGE VCVQGQIIAM ETREIRSEKT IIICDITDFT DTITFKLFVE NADLAEILSQ
LQKGKFYKVK GVATLDKFDK EIALNSIRGI RIIPDFRSVR EDTAEEKRVE LHLHTKMSDM
DSVVDIKEMI SRAKAWGMPA VAITDHGCLQ AFPIANHCIK KDDPFKIIYG VEAYFVDDLK
HAVENDKGQS LDDEFVVFDI ETTGFSPTTN KIIEIGAVKI VGGKVVDAYS TFVNPHCEIP
KNIVELTKIT DDYVKNAPSI ETVLPEFLQF CEGVVMVAHN AEFDMSFIYS NAKAIGLDVQ
KTVVDTVAIA RTLLPDLGNA KLGNIAKKLG VSLENHHRAV DDAKATSDIF LKFCERLKQQ
EIYTLTDLNK LCDASPDYIK KLPTYHGIIL VKNEVGRINL NRLVSISHLD YFNRRPRMPK
SLIQKYREGL ILGSACEAGE IFQGIMREKD EVEMQKLVSF YDYLEIQPEL NNEFMIRSEK
HKATSREDLR EYNRQIISLG EKYNKRVVAT CDVHFMNPED EVYRRIIMSY KGFKDADFQP
PLYFRTTNEM LEEFAYLGQD KAYEVVVTNT RAIADEIEKI SPVLPDKCPP EIENSDVELR
QICYDKAHEI YGPNLHEVVV ERLERELNSI INNGFAVMYI ISQKLVWDSN DHGYLVGSRG
SVGSSFAATM SGITEVNPLA PHYICPSCFY TDFDSEVVKS FAGSSGCDMP DADCPKCGTP
LNKEGHDIPF ETFLGFKGDK EPDIDLNFSG EYQAASHKYV EVLFGEGKAY RAGTIGTVAD
KTAFVYVLKY CETRALSKRK AEMKRLAAGC TGVKRTTGQH PGGIIVVPHD REIYEFCAIQ
RPANDVHTPI ITTHYEYHSI DHNLLKLDIL GHDDPTIIRR LEDITGISSD TIRLDDKDVM
KLFHGTEVLG ITPDDIGGIR LGSLGVPEFG TDFVIQMLVD AKPQNFSDLV RISGLSHGTD
VWIGNAQTLI EEGKGTISTV ICTRDDIMTY LIGKGLEKGL AFTIMESVRK GKGLTPEWEE
EMIANDVPDW YVWSCKKIKY MFPKAHAAAY VMMAWRIAWY KVFWPLAYYT AFFSIRASSF
SYDTMCFGKR QLEDNMKAIS SKPKDMQTAK EQDTLKDMRI VQEMYARGFE FLPIDLTVVH
DKNFQIIDNK IMPSLGVIEG LGEKAAESVV SAVKDGPFLS KDDFRKRTKV SQTITDKMSE
FGLLGDIPES NQISIMDLLG
//
