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Database: UniProt
Entry: A0A1Y4WFW4_9FIRM
LinkDB: A0A1Y4WFW4_9FIRM
Original site: A0A1Y4WFW4_9FIRM 
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}.
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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
//
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