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Database: UniProt
Entry: A0A2K4ZIH0_9FIRM
LinkDB: A0A2K4ZIH0_9FIRM
Original site: A0A2K4ZIH0_9FIRM 
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
//
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