ID B0PB10_9FIRM Unreviewed; 1445 AA.
AC B0PB10;
DT 08-APR-2008, integrated into UniProtKB/TrEMBL.
DT 08-APR-2008, sequence version 1.
DT 24-JAN-2024, entry version 84.
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:EDS11340.1};
GN ORFNames=ANACOL_01961 {ECO:0000313|EMBL:EDS11340.1};
OS Anaerotruncus colihominis DSM 17241.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Oscillospiraceae;
OC Anaerotruncus.
OX NCBI_TaxID=445972 {ECO:0000313|EMBL:EDS11340.1, ECO:0000313|Proteomes:UP000003803};
RN [1] {ECO:0000313|EMBL:EDS11340.1, ECO:0000313|Proteomes:UP000003803}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 17241 {ECO:0000313|EMBL:EDS11340.1,
RC ECO:0000313|Proteomes:UP000003803};
RA Sudarsanam P., Ley R., Guruge J., Turnbaugh P.J., Mahowald M., Liep D.,
RA Gordon J.;
RT "Draft genome sequence of Anaerotruncus colihominis(DSM 17241).";
RL Submitted (NOV-2007) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:EDS11340.1, ECO:0000313|Proteomes:UP000003803}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 17241 {ECO:0000313|EMBL:EDS11340.1,
RC ECO:0000313|Proteomes:UP000003803};
RA Fulton L., Clifton S., Fulton B., Xu J., Minx P., Pepin K.H., Johnson M.,
RA Thiruvilangam P., Bhonagiri V., Nash W.E., Mardis E.R., Wilson R.K.;
RL Submitted (NOV-2007) 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:EDS11340.1}.
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DR EMBL; ABGD02000014; EDS11340.1; -; Genomic_DNA.
DR RefSeq; WP_006875256.1; NZ_DS544183.1.
DR STRING; 169435.ERS852551_01459; -.
DR eggNOG; COG2176; Bacteria.
DR HOGENOM; CLU_003297_2_0_9; -.
DR Proteomes; UP000003803; 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; 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 SMART; SM00479; EXOIII; 1.
DR SMART; SM00481; POLIIIAc; 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};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_00356}.
FT DOMAIN 336..408
FT /note="Polymerase/histidinol phosphatase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00481"
FT DOMAIN 425..592
FT /note="Exonuclease"
FT /evidence="ECO:0000259|SMART:SM00479"
SQ SEQUENCE 1445 AA; 160637 MW; 9C31CDE6052562DF CRC64;
MASLIELFGE YIELPPGALA RGTVLGMQID QQKRSMCVSL GLDELTPYAA LSELGRRLAA
AFSLNDAVVH PRYDGGMLSS EHLPELIARL GSEGVPVNGF FTGCRCDLID ETLRIYLTHG
GQEFLESIHC PQKLSAVIRE EFGREVRIVF DGVLEVAPDS ALYQETVEKV RPKPIRYTPP
TPQQAEKKPE NGAVIPAAAR LSFDAHDLPF EPGSMVTLYG NPPKGRPIEM AQVNIESGNV
TVWGDVFKID RRTSRDEKTL ILSIYFTDYT GSYCAKVIGR FDKKMKALDE LHEGDTVAMH
GLIEYDRFDR ENVMRPDSIA TVKKIPRRDL CEEKRVELHM HSNMSAMDGI TPAAKLIKRA
YEFGHKAVAI TDHGVVQAFP DCMNAVAKIR KSGGDIKVIY GVEAYFVDDV VQAVSGNAHG
RFDSEMIVFD LETTGLSAAT ERITEIGAVK LRNGEIVDRF NTFVNPERSI PPKITELTGI
TDDDVRGAPL EGEALRQFYA FCGGSSAVLI AHNAPFDTSF LRQCARRCGM EYNFTAIDTV
VLSRSLFPEL KKHKLDIVAK HLGLGEFNHH RACDDAEMLA RIYIRMMELM QSERACSDIG
QINTSLAAVD VKKSPTYHQI ILVKNLTGLK NLYRLISISH LDYYAKRPRI PKSKLIEHRE
GLLIGSACEA GQLYRAIVEG KSWGDLCDIA RFYDYLEIQP VANNEYMVRS NMVADEQAIR
EFNETVVRLG ERLNIPVVAT CDVHFMDPGD AKFRAILMAG MGFADADQQA PLYFRTTDEM
LKEFEYLGAQ KAHEVVIENP NLIADMVENI KPIPDGTFTP TIPGSDEDLQ RITRAKAMEL
YGYQGQVPEL VSKRLERELG SIIKHGFAVL YMIAQKLVAK SEEGGYHVGS RGSVGSSFVA
TMAGISEVNP LPPHYYCPDC HYSEFITDGS VGSGFDLPEK ACPMCGATYK QDGHDIPFET
FLGFDGDKAP DIDLNFSGEY QAQIHKYTEE LFGPTHVFKA GTISTVAEKT AYGFVKKYAQ
ERGLIMTRAE EERLAIGCTG VKRTTGQHPG GMVVVPSDHE VFDFSAVQRP ADDPNSDITT
THFDFHSLHD TILKLDELGH DVPTMYKYLK DMTGIDANDV PMNDQKVMSL FLSPEALGVT
EEEIDCNTGT LGIPEFGTNF VRGMLIEAQP KNFSDLLQIS GLSHGTDVWL GNAQELIKNK
VCTISNVIGT RDSIMTYLLH KGLEPKMAFK IMEITRKGNA PKLLTEEHMT AMREHGVPQW
YIDSCLKIKY MFPKAHAAAY DIASIRLCWF KVYHPLAFYA VIFTVRGGDF DAEAAVQGKS
ATKRKIQNLL QMGNERTAKD EGVLTMLQII HECQARGYSF LPVDLYKSHY SIYEVEDGKI
RLPFMALKGV GEAAARSLWE TAKTEQFISA DDISNRAGVS KSVIEMLRGA GALGDLPETS
QVSFF
//
