ID A0A1Y4WFW4_9FIRM Unreviewed; 1380 AA.
AC A0A1Y4WFW4;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-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 ECO:0000313|EMBL:OUQ80618.1};
GN ORFNames=B5E43_03720 {ECO:0000313|EMBL:OUQ80618.1};
OS Flavonifractor sp. An100.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Oscillospiraceae;
OC Flavonifractor.
OX NCBI_TaxID=1965538 {ECO:0000313|EMBL:OUQ80618.1, ECO:0000313|Proteomes:UP000196191};
RN [1] {ECO:0000313|Proteomes:UP000196191}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=An100 {ECO:0000313|Proteomes:UP000196191};
RA Medvecky M., Cejkova D., Polansky O., Karasova D., Kubasova T., Cizek A.,
RA Rychlik I.;
RT "Function of individual gut microbiota members based on whole genome
RT sequencing of pure cultures obtained from chicken caecum.";
RL Submitted (APR-2017) 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:OUQ80618.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; NFMA01000004; OUQ80618.1; -; Genomic_DNA.
DR OrthoDB; 9804290at2; -.
DR Proteomes; UP000196191; 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; 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; 2.
DR Pfam; PF00929; RNase_T; 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|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:UP000196191};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_00356}.
FT DOMAIN 264..336
FT /note="Polymerase/histidinol phosphatase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00481"
FT DOMAIN 355..523
FT /note="Exonuclease"
FT /evidence="ECO:0000259|SMART:SM00479"
SQ SEQUENCE 1380 AA; 152837 MW; DA942FC92C5E3C89 CRC64;
MSKKIPFLQM FAALRRWTEL AQAVEGWLIV TAAIDKASRS ATITVEGAGG AGPNLVREAE
ETLARCYGLN SVKLNCLPNI AAQSQTVKEE SAGAVEDLHK EEPGGVETEQ PQDAFARAEA
IRRAAMKSVS RPAAPKGEKK PAGKAIFGKP ISKAATPIGE LELDMGTVVV EGDVFAIDNR
ELKKRGAWVV AFDLTDYTGS IRINKFFPGD EGKPLVDGIK KGMHLKVQGR LNMDRFYGDM
VLEPVAVMAA EKKMKEDKAP EKRVELHLHT TMSSMDALTA VGPKLGPDKN VVKRAEAWGH
PAIAITDHGV AQSFPDAWHS AKKIKLLYGV EAYFINDVDD RVVVHGDTNA SFSDEIVCFD
IETTGLNKKY EVIIEIGAVV LKNGEITDRF NTFVSPGRIL SPEIIGLTGI TDEMLVGAPS
QEEALRAFLD FAGDRPLAAH NAEFDMGFIA AGCRKYGIPF ENPSVDSLIL AQNLLPDLGK
YKLDIVAEHL HLPAFNHHRA SDDAATVAYM LPPFFRMMEE LGLHHLGEIN GYMPRLRKGG
KAKRQPKHLI VLAKNQTGLR NLYKLISLAH LEHFKRVPTM PKSLINENRE GLIIGSACEA
GELFRAVVDG KDWGELKRIA SWYDYLEIQP ICNNMFMLRK GMVRSEEELR DFNRTIVRLG
EELGKPVCAT GDVHFLDPED EIYRHILLAS KGFEDADEPL PIYFKTTDEM LEEFDYLGKE
KAYEVVVKNT NLIANWCDPI EPLPKGLFAP KLEDSDGELK RLVWGKAHEL YGDEPPQIVV
DRIEAELGDI IRCKYDVIYM SAQKLVQNSL EHGYLVGSRG SVGSSLVAFM SGITEVNSLP
AHYRCPKCKH SDFEFGPANG YGCGADMPDA NCPICGTKYV KDGFNIPFET FLGFGGDKVP
DIDLNFSGEY QSSAHRYTFE LFGQTHVFRA GTIGTVAEKT AFGYVKKYLD EKGKIASKAE
ENRLAIGCTG VKRTTGQHPG GMVVIPQDKE IYDFCPVQHP ADDPNSDIIT THFEYHSMES
NLLKLDMLGH DDPTMIRMLE DLTGVNARTD IPLDDKDTMS IFQSSKVLGY ENDKILGPTG
GTAIPEFGTT FVRGMLEDTQ PSQFDILVRL SGFSHGTDVW LGNAKDLITS GTAKVSEAIG
CRDDIMLFLI SKGMPPKRSF KIMEAVRKGR GLPEGAEEEM KAAGVPDWYI GSCKKIAYLF
PKAHAVAYVM MAFRIAWFKV HRPLAFYAAY FSIRAKAFDE AYMCRGMETC QRKMREIIAK
DKEASAVEQD MLTTLEVCYE FYLRGFTFDR MDLYQSEAIR FTVDEEHNAL RPPFVSVAGL
GETAAVSLAE ARKGKRFISI EEVSAACPKV SKTHIELLKQ AGAFGDLPET SQLDLFALLG
//