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Database: UniProt
Entry: A0A0U2VL32_9ENTE
LinkDB: A0A0U2VL32_9ENTE
Original site: A0A0U2VL32_9ENTE 
ID   A0A0U2VL32_9ENTE        Unreviewed;      1450 AA.
AC   A0A0U2VL32;
DT   16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT   16-MAR-2016, sequence version 1.
DT   24-JAN-2024, entry version 34.
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:ALS38188.1};
GN   ORFNames=ATZ35_13835 {ECO:0000313|EMBL:ALS38188.1};
OS   Enterococcus rotai.
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Enterococcaceae;
OC   Enterococcus.
OX   NCBI_TaxID=118060 {ECO:0000313|EMBL:ALS38188.1, ECO:0000313|Proteomes:UP000067523};
RN   [1] {ECO:0000313|EMBL:ALS38188.1, ECO:0000313|Proteomes:UP000067523}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LMG 26678 {ECO:0000313|EMBL:ALS38188.1,
RC   ECO:0000313|Proteomes:UP000067523};
RA   Shamseldin A., Moawad H., Abd El-Rahim W.M., Sadowsky M.J.;
RL   Submitted (DEC-2015) 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; CP013655; ALS38188.1; -; Genomic_DNA.
DR   STRING; 118060.ATZ35_13835; -.
DR   Proteomes; UP000067523; 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; 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; 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; 1.
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; 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          340..407
FT                   /note="Polymerase/histidinol phosphatase N-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00481"
FT   DOMAIN          425..591
FT                   /note="Exonuclease"
FT                   /evidence="ECO:0000259|SMART:SM00479"
FT   REGION          198..225
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1450 AA;  164201 MW;  2CF0FA8DD64C4A80 CRC64;
     MAEKAQELFA KLIDQIQLNE QERQHPLIQQ GRIHKVVVHQ QSRLWEFHLG FAEILPVMLY
     QSFMQQLELA FQQIAGVTVK ISADKSEFTE EQLTDYWQLA LLNSQCDTPL VQRVIKTQTP
     IIEDKKIILP VDNDAVIPYL KQQYLPIIEE LYINYGFQKF HIEPKMDEQQ AKRVLALFEE
     RKQEQDAAFQ QQAAESLVKH EQKKKQQQQQ GPALEGPIRL GRNIPNDEPI MPMGNILEEE
     RRVTIEGFVF DVEVRELRSK RKILILKITD YTSSFIVKKF SNGEKDEQVF DAIQKHSWVR
     VRGSIQEDTF MRDLVMNCQD LMEVKHAPRK DYAPEGDKRV ELHLHSNMST MDATNNVADY
     VAQAGKWGHK AIAITDHGGA QGFPDAHSAG KKAGVKILYG VEANVVDDGV PIAYNEAHIE
     LTDATYVVFD VETTGLSAVY DTIIELAAVK MHKGNIIDTF EEFIDPGHPL SQTTINLTGI
     TDEMVRGSKS EEEVLRLFRE FSEDTILVAH NASFDMGFLN TSYGKYDIPE AENPVIDTLE
     LSRYLNPTFK SHRLNTLSKK FGVNLEQHHR AIYDSESTGH LCWIFLKDAK ENHNMNYHDE
     LNMHIGEGDS YKRARPFHAT ILATTQAGLK NLFKLISMSN IDYFFRIPRI PRSQLSKLRE
     GLIIGSACSS GEIFEAMMQK GVEEAKNRAK FYDYIEVMPK AVYAPLLEQE LVKSEADLEE
     IIANLVKIGD ELDKPVVATG NVHYLNEEDS IYRKILVGSM GGANPLNRHS LPDVHFRTTD
     EMLTAFQFLG EETAHRLVVE NPNAIADMCD EITPVKDDLY TPKIPGSEDE IRNLSYTRAK
     ELYGDPLPDI VEKRLKKELD SIIGNGFSVI YLISQKLVHK SMEDGYLVGS RGSVGSSFVA
     TMTGITEVNP LAPHYHCVNC KHSEFFEDGS YGSGFDMPEK NCPNCGQRLF KDGHDIPFET
     FLGFHGDKVP DIDLNFSGDY QAEAHNYTKV LFGEEYVYRA GTIGTVADKT AYGFVKGYER
     DHNLHFRGAE VDRLAKGSTG VKRTTGQHPG GIIVIPDYMD VYDFTPIQYP ADDQNSEWKT
     THFDFHSIHD NILKLDILGH DDPTVIRMLQ DLSGIDPKTI PTDDPEMMRI FAGPEVLGVT
     PEQIYSKTGT LGIPEFGTRF VRGMLEETHP STFAELLQIS GLSHGTDVWL GNAEELIRRG
     EATLAEVIGC RDDIMVYLIH AGLDSGMAFK IMETVRKGLW NKIPDELREE YLTAMKENNV
     PDWYIDSCSK IKYMFPKAHA AAYVLMALRV AYFKVYFPIL YYCAYFSVRA DDFDLVAMSQ
     GKEAVKARMK EIQDKGLEAS TKEKNLLTVL ELANEMIERG FKFGMIDLYK SDAENFVIDG
     DTLIAPFRAV PSLGLNVAKS IVEAREEPFL SKEDLASRGK VSKTLIEYMT ENGVLKDLPD
     ENQLSLFDML
//
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