ID A0A249DDU2_LACRH Unreviewed; 1444 AA.
AC A0A249DDU2;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 24-JAN-2024, entry version 35.
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:ASX17223.1};
GN ORFNames=BGK71_07295 {ECO:0000313|EMBL:ASX17223.1};
OS Lacticaseibacillus rhamnosus (Lactobacillus rhamnosus).
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC Lacticaseibacillus.
OX NCBI_TaxID=47715 {ECO:0000313|EMBL:ASX17223.1, ECO:0000313|Proteomes:UP000215843};
RN [1] {ECO:0000313|EMBL:ASX17223.1, ECO:0000313|Proteomes:UP000215843}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LR5 {ECO:0000313|EMBL:ASX17223.1,
RC ECO:0000313|Proteomes:UP000215843};
RA Nam Y.-D., Kang J., Chung W.-H.;
RT "Complete genome sequence of Lactobacillus rhamnosus LR5.";
RL Submitted (AUG-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|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; CP017063; ASX17223.1; -; Genomic_DNA.
DR RefSeq; WP_047676493.1; NZ_VRTQ01000005.1.
DR GeneID; 69832047; -.
DR Proteomes; UP000215843; Chromosome.
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; 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; 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; 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; 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 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};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_00356}.
FT DOMAIN 334..401
FT /note="Polymerase/histidinol phosphatase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00481"
FT DOMAIN 420..586
FT /note="Exonuclease"
FT /evidence="ECO:0000259|SMART:SM00479"
FT REGION 201..224
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 203..224
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1444 AA; 161404 MW; 66014AD338E9B530 CRC64;
MALSQHEMFE KLMDQLDLPA DVRHDPSLAD GSVQAVTIHE QSQRYDFTLA FPTILPFQIF
NTVVTQLPIA FKQIAATRLT IAVAQPTITD KLLAQYWPYV VQNSEIGTGI VRELCEKQVP
TLVNNRAVIT AENEQIRQYL INQGLGKLEA TYQQVGFSGL RMQAQVDEEQ AAQSVAAFEA
QKAAQTAKMA QAAAEVVKRQ AAKQKQEPTN GPVQMGRQLK MSDPPQQMVT ITQEERSVTV
EGYVFDVEVR ELRSKRQLLI FKITDYSSSF IAKKFSNGAD DEAMFARIKK GQWLRVRGSV
QEDNYSRELT INAQDIQTVS HPDPTDDVEG EKRVELHLHT NMSQMDATNS ITDFVNRAKA
WGHKAIAVTD HAGLQAYPEA HTAAAKAGLK MLYGVEINLV DDGTPVAYRA DEPRVLADAE
YVVFDVETTG LSAVYDKVIE LAAVKMKDGQ VIDQFEEMID PGFPLSELTI NLTHITDDMV
HGSKSEEEVF RLFQQFCDGA IMVGHNVTFD VGFLDNGYER HGLADIDNPV IDTLELSRML
HPERKNHKLD TLAKLYKVSL EHHHRANADA EATGYLLYAL EKEAAKMYNM TKLNQLNDRV
GAGEAYKAAR PSHAIVFAKT QAGLKNLFKL VSLSNVKYFY RVPRVPRSQL QKLREGLLVG
SACSSGEVFT AMMQKGEAEA RAKAAFYDYL EIQPPAVYQP LLEADLIKGE SHLKDILQKM
VKIGDDLEKP VVVTGDVHYL DQHDAIYRKI LIHSQGGANP LNRHSLPDVH FRSTREMLDD
FSWLGEEKAQ QLVVTNSNLI ADWIDDDITP VKDKLYTPEV PGVEEKLKHD VMATAYELYG
DPLPEIVAQR LDKELKSIIG NGFSVIYNIA QRLVLKSNKD GYLVGSRGSV GSSLAATMAG
ITEVNPLPPH YRCPKCQYSE FFTHGEVGSG FDLPDKTCPK CGTELHKDGH DIPFETFLGF
HGDKVPDIDL NFSGDYQPVA HNYIKVMFGE DHSFRAGTIG TVADKTAYGY VKAYERDTGQ
QLRGAEIDRL AQGDTGVKRT TGQHPAGILI VPADMDIYDF TPIQYPADDQ NAAWMTTHFD
FHSIHDNILK MDVLGHDDPT MIRMLQDLSG VEPKSIPTDD PGVMALFSGT ESLGVTPEQI
NSKMGTLGIP EFGTRFVRGM LEETKPTTFS ELLQISGLSH GTDVWLGNAE ELIKQGIVTL
KEVIGCRDNI MMDLIHWGMD DSMAFNIMEH VRKGRGIPDD WQKAMRENEN VPDWYIDSCL
KIKYMFPKAH ATAYILMALR IAWFKVHYPL VYYTAYFSVR AEDFDLAAMS HGKEAVKAAM
KEITDKGMDA SAKEKQLLTV LEIANECLER GFKIKMIDVT KSDSHDFLIQ DDHTILAPFR
AVPGLGDNVA KQIVAAREEK PFLSKEDLAN RGKVSKTLID YMTTNHVLDD LPDENQLSLF
DGLF
//