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Database: UniProt
Entry: A0A249DDU2_LACRH
LinkDB: A0A249DDU2_LACRH
Original site: A0A249DDU2_LACRH 
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
//
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