ID A0A1G8KMJ1_9LACT Unreviewed; 1438 AA.
AC A0A1G8KMJ1;
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 ECO:0000313|EMBL:PMC58165.1};
GN ORFNames=CJ205_05610 {ECO:0000313|EMBL:PMC58165.1};
OS Dolosicoccus paucivorans.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Aerococcaceae; Dolosicoccus.
OX NCBI_TaxID=84521 {ECO:0000313|EMBL:PMC58165.1, ECO:0000313|Proteomes:UP000235682};
RN [1] {ECO:0000313|EMBL:PMC58165.1, ECO:0000313|Proteomes:UP000235682}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UMB0852 {ECO:0000313|EMBL:PMC58165.1,
RC ECO:0000313|Proteomes:UP000235682};
RA Thomas-White K., Kumar N., Forster S., Putonti C., Lawley T., Wolfe A.J.;
RT "Bacterial strain isolated from the female urinary microbiota.";
RL Submitted (SEP-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:PMC58165.1}.
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DR EMBL; PNHE01000022; PMC58165.1; -; Genomic_DNA.
DR STRING; 84521.SAMN04487994_101227; -.
DR OrthoDB; 9804290at2; -.
DR Proteomes; UP000235682; 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; 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; 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; 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; 2.
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}; Reference proteome {ECO:0000313|Proteomes:UP000235682};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_00356}.
FT DOMAIN 332..399
FT /note="Polymerase/histidinol phosphatase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00481"
FT DOMAIN 417..583
FT /note="Exonuclease"
FT /evidence="ECO:0000259|SMART:SM00479"
SQ SEQUENCE 1438 AA; 164137 MW; 41A891A66AF7EE9F CRC64;
MKENQELFNI LLQQLQIKDE DILNELEAVE MIKVDVHPNK KEWHFYLSAP KRLHPHVYEM
FQHALESAFT EIATPNAWWQ FPTEQATKET LIDYWPTLYR LMIRHYPLLE GLLRSANIEI
LDEEIRIGLA SQDQIQTFKT QFHQLIADQL QKASFTQVPL TCYVDETVSQ KDHEAFVNRQ
NQEEEASIQA ALQALEQQKN RPKVQEGDAD LTIGKDIPEG QTITILDVYD NPRRQVIEGH
IFAIEYRTFQ SGTELMTMKI TDYTSSVQVK MFSGRRASKE ALHQFNKGEW IRLEGDLEMD
NYTHEMVFQP RSIRKIKKAS RQDTAPENEK RIEFHMHSNM SQMDATNSAS DLIKQAAAWG
HPAVALTDHA AVQAFPEAYH AGKANDIKVI FGMEAYVVND GEPVAYNPEH IELEDATYVV
FDVETTGLSA IYDSIIEIAG VKMHQGNIID TYEAFINPGH PLSAFTTELT GITDAMLEDA
PPEKQVMEEF QAFCEGTILV AHNASFDIGF INKTYERLGM KPSTLPVIDT LELSRLVNPD
LRTHRLNTLA RHYGVHLEQH HRAIYDSETT GFILYKLLEQ ALEDYQMTHH DQLNNEMGKG
DSYKQSRPFH VTLLAKNQAG LKDLFKLVSI SNIEYFHRTP RIPRSVLNRY REHLLVGTAC
SEGEVFTAMM QKGYDEAVEL AKYYDYIEIQ PPSVYEPLVE QELVRSHAAL QDIMKEMVRL
GEELDKLVIA TGNVHYLDEK DHIYREILLR SMKINANRTL YLPKAHFRTT QEMLDEFDFL
PQDVAHNIVV ENTHLLNEQI EEVEVIKSDL YTPVIEGSDQ EITDYTYEQA YKMYGNPLPE
IVEARIKKEL DSIISNGFSV IYLISQKLVL KSMDDGYLVG SRGSVGSSLV ATLTGITEVN
PLVPHYYCPN CQYNEFFTDG TIGSGYDLPE KTCPNCGEDV PLVREGQDIP FETFLGFYGD
KVPDIDLNFS GVYQPTAHAY TKELFGEDYV YRAGTISTVA ERTAFGYVRG YLEHTQEELP
QAEKERLAKG IEGVKRTTGQ HPGGIIVIPD NMDVFDFTPI QFPADDMGAE WRTTHFDFHS
IDENVLKLDI LGHDDPTVIR MLQDLSGIDP STINPTDEEV MTIFTSPKAL GVEPEQIFSS
TGTLGIPEFG TEFVRNMLEE ARPKTFAELI QISGLSHGTD VWLNNARDLI NNNIAPLSEV
IGLRDDIMTT LIYYGLDDGL AFTIMEAVRK GRGLTPEWED QMREHNVPEW YIDSCKKIKY
MFPKAHAVAY VLMALRVAYF KVHYPMYYYA AYFSVRAKEF DIVAMHQGKE MVKRRIREIN
DKGFDATVTD KNLLVSLELA NEMLERGYKF QMIDINKSDA ENFLIEGDTL IPPFRSIPGL
GLSVAQQIVA ARKEAPFLSK EDIQKRGRVS KTIIEYLTDH GVIQDLPDEN QLSLFDMM
//
