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
//