ID A0A2K4ZIH0_9FIRM Unreviewed; 1613 AA.
AC A0A2K4ZIH0;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 24-JAN-2024, entry version 24.
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_2 {ECO:0000313|EMBL:SOY30279.1};
GN Synonyms=polC {ECO:0000256|HAMAP-Rule:MF_00356};
GN ORFNames=AMURIS_03005 {ECO:0000313|EMBL:SOY30279.1};
OS Acetatifactor muris.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae;
OC Acetatifactor.
OX NCBI_TaxID=879566 {ECO:0000313|EMBL:SOY30279.1, ECO:0000313|Proteomes:UP000236311};
RN [1] {ECO:0000313|EMBL:SOY30279.1, ECO:0000313|Proteomes:UP000236311}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GP69 {ECO:0000313|EMBL:SOY30279.1};
RA Gaut B.S., Morton B.R., Clegg M.T., Duvall M.R.;
RL Submitted (JAN-2018) 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; OFSM01000015; SOY30279.1; -; Genomic_DNA.
DR Proteomes; UP000236311; 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; 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; 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; SSF160975; AF1531-like; 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:UP000236311};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_00356}.
FT DOMAIN 451..537
FT /note="Polymerase/histidinol phosphatase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00481"
FT DOMAIN 554..732
FT /note="Exonuclease"
FT /evidence="ECO:0000259|SMART:SM00479"
FT REGION 214..246
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 262..320
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 296..320
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1613 AA; 179822 MW; EC7DA49F39E03385 CRC64;
MMTKSKPFFE VFPTLEIKGK LYDKLEQTEV ERVSATKQKD RISVYLYSTR LLLKEDIWAA
EKEIKGQLFP HAMLKVRIFE RFELSSQYTP ENLMEVYRES ILAELLEYSH VEYNAFRTAD
IAYPETGEMR LTIEDTVLNR TKEEDLVRVL EKILVERCGL TAHVTVDYRE GRPGRFAEEN
ELKIQMRVSE ICRRAKTGGG YGDAVSEGTG ALQAEGNQDG RAEGGQAGGN SPGGALSRNG
GAGSGAGGKV GMAAGGNDVS RAGQNAAGAA QKSRSGFGAG QAGGNAGGVN GRADEAAQDG
ARKKGEFRRG EFRRNGDYGR TLKQSDNADV IYGRDFEEEA IPIEDIIGEM GEVTIRGKVL
KTDSRQIRNE RTIVMFDVTD FTDTMTVKLF TKNEFVKELT GSLKAGAFVK IKGVATLDKF
DHELTIGSLT GIKKISDFTT TRLDTALHKR VELHCHTKMS DFDGVSEAKD IVKRAYKWGH
AAIAITDHGV VQGFTDAFHV WQDLWKAEKE RCKEKGETPD RQNFFKIIYG VEAYLVDDLK
EIVTGDRGQN LGDDFVVFDI ETTGFSPVNN RIIEIGAVKV SGGKVTDRFS SFVNPQVPIP
FEIEKLTSIR DDMVADAPLI EEVLPQFLEF CRGCVPVAHN AGFDMSFIME NARRLGLSLS
GLTGRTGAGS GAECTYVDTV GIARVLLPDQ AKHTLDAVAK TLNISLENHH RAVDDAECTA
WIFLKLVQML EERQIHTLAE LNELGAASVE LVKRLPTYHA IILAKNDLGR INLYRLVTES
HLTYYNNRHP RIPKSLVMKY RDGLILGSAC EAGELYRALL DEQSEMQIAR IVNFYDYLEI
QPSGNNKFMI ASDRIRSVES MEDIQNINRR IVKLGEQFHK PVVGTCDVHF LDPEDEVYRR
IIMAGRGFED ADDQAPLFLH TTNEMLDEFS YLGSDKAYEI VVKNTNMIAD MIESIDPVRP
DKCAPVIEDS DKKLTKICYD RAHEIYGPDL PQIVEARLEK ELHSIITNGF AVMYIIAQKL
VWKSVEDGYL VGSRGSVGSS FVATMAGITE INPLSPHYYC SKCHYVDFEE EDVKAYAGKA
GVDMPDRNCP VCGEPLHKDG FDIPFETFLG FKGDKEPDID LNFSGEYQSK AHKYTEVIFG
AGQTYRAGTI ATLADKTAFG YVKNYFEERE KHKRKSEIER LAMGVAGVRR STGQHPGGIV
VLPIGQDINS FTPVQHPAND MTTDIVTTHF DYHSIDHNLL KLDILGHDDP TMIRMLQDMT
GRDPLTIPLD SSDVMSLFQN TQALGITPEQ IGGTKLGCLG IPEFGTDFAM NMVIEAKPES
FSDLVRISGL SHGTNVWVGN AQDLIRDGTA TISTCVCTRD DIMTYLINKG MEPEKSFKIM
EAVRKGMVAK GKTPAAQWKE WKEDMVAHNV PDWYIRSCEK IEYMFPKAHA AAYVMMAWRI
GYCKINYPLA YYGAYFSIRA KAFSYELMCQ GQARLEANMA EYRRRMEAAA DKEPGAQPLS
NREEGAYSDM RIVQEMYARG FEFMPIDIFT AQSRSFQIVG DKLMPSLNSI EGLGDKAADA
IVEAVKDGPF LSKDDFRERT KVSKTMVDLM SSLNLLGALP ESNQLSLFDF CGQ
//