ID A0A1H8EF86_9FIRM Unreviewed; 1435 AA.
AC A0A1H8EF86;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 23.
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=SAMN05216454_101101 {ECO:0000313|EMBL:SEN18199.1};
OS Peptostreptococcus russellii.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Peptostreptococcaceae;
OC Peptostreptococcus.
OX NCBI_TaxID=215200 {ECO:0000313|EMBL:SEN18199.1, ECO:0000313|Proteomes:UP000199512};
RN [1] {ECO:0000313|EMBL:SEN18199.1, ECO:0000313|Proteomes:UP000199512}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Calf135 {ECO:0000313|EMBL:SEN18199.1,
RC ECO:0000313|Proteomes:UP000199512};
RA de Groot N.N.;
RL Submitted (OCT-2016) 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}.
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DR EMBL; FODF01000001; SEN18199.1; -; Genomic_DNA.
DR STRING; 215200.SAMN05216454_101101; -.
DR OrthoDB; 9804290at2; -.
DR Proteomes; UP000199512; 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; 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; 2.
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; IPR024754; DNA_PolC-like_N_II.
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; PF11490; DNA_pol3_a_NII; 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 SMART; SM00479; EXOIII; 1.
DR SMART; SM00481; POLIIIAc; 1.
DR SUPFAM; SSF160975; AF1531-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:UP000199512};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_00356}.
FT DOMAIN 336..403
FT /note="Polymerase/histidinol phosphatase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00481"
FT DOMAIN 420..585
FT /note="Exonuclease"
FT /evidence="ECO:0000259|SMART:SM00479"
SQ SEQUENCE 1435 AA; 163279 MW; 928EC548E869CB00 CRC64;
MKNFIEFLES IEISKESLTK GFEELIIDRT ILKKKSGICV FYLSSKSVVL HERLENIRKE
MEKKLCPPID SIKVILKIEG YEKKPLKKVI KKYWPNIFYL IKQNCPSVLA YSNDLEHLCI
DDLLKIKAPN EFIFNRLKEK ELDEKIKTMI FEELGIEVNV ILEKAKENKH EEDEIKKIIR
AQEMETMKII SKLELENNKK EIVEDEKYVV EFEVDPDIIY GENVSAFYKD IEEIDENSRT
VAIIGEIFDI DTKELRNGKT LYSMFVTDYS SAISCKVYLD DRTREKVISE TKPGTYVKIK
GDILFNSYSD ELELNVTGIK REKRVVRKDE ADEKRVELHL HTQMSAMDSV VPVKKVINTA
IEWGHKAIAI TDHGVVQAFP DAMNASKGKD IKILYGVEAY LVDDDQEIIA DANDLDFNQK
FVVFDIETTG FSPINDNITE IGAVLVENGT IVENFSTFVN PEMDISYEIQ GLTRITNEMV
EDAPKIDEAL KKFMDFAEGA VLVAHNADFD TGFISEKCKL VGIDYNHAKI DTLMLARVLL
KNIKKFSLDK VCKELNINLS GHHRAVNDAA ATAEVFINFI ERFKKDGAEK LSDVNKIYGK
VDYTKLRPTH AIIFAKNQDG LKSLYEMISD SHIEHFYKTP RILKSILLKK RENLIIGSAC
SSGELYNAVQ RNKSEKEIEN ILKLYDYIEV QPLGNNEYMI KNGDVKDKDE LIKINMKLIE
LGEKYNKPVV ATGDVHTMEP YEYIYRDILK YSQGFSKLDS NSSLYFRTTS EMLDEFYYLP
EEKSREIVIE NPNKIVDMIG DVKPIPDETY PPVIEGSEEE LRNMCYKKAR RIYGDDLPEI
VEARLERELN SIIGNGYAVM YIIANKLVAK SLSDGYLVGS RGSVGSSFAA TMSDITEVNP
LPAHYICPNP DCKHSHFFAV GEWGSGIDLP AKKCEKCGSE MIRDGHDIPF EVFLGFEGDK
EPDIDLNFSG IYQPVIHKYT EELFGEGYTY RAGTIGTVKD KTAFGYVKKF SEENNLFFSK
TKMSWLSQGC TGVKKTSGQH PGGVMVIPDY KDVHDFTPIQ YPANDSTSGV KTTHFDYHSI
SGRILKLDIL GHDGPTIIRM LEDMIGIKIT DIPLDDKETM SIFTSTEALG VTEEEIGTPV
GSLAVPEFGT KFTRQMLIDT KPTTFAELVR ISGLSHGTDV WVNNAQDLVR GNVVGLKEVI
STRDDIMNYL IFSGLEAKMA FTIMENVRKG RGLKPEFEKA MRANNVPDWY INSCKKIKYM
FPKAHAVAYV MTSFRIAYCK VHHPEAFYAT YFTTKVEDFD ISLCTSGIDA VKKRMREIEE
LGNKATAKEH NQYTILEVVV EMYARKIEFL NVDLYKSHAY EFQIAEKGKI LPPMVSLQGM
GLNAAESIVE ERKNGEFLSK EDLLKRTKIS KTVVEKLTEH GTLANMSEKN QVSFF
//
