ID A0A0L0QNJ9_VIRPA Unreviewed; 1428 AA.
AC A0A0L0QNJ9;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, 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:KNE20205.1};
GN ORFNames=AFK71_17595 {ECO:0000313|EMBL:KNE20205.1};
OS Virgibacillus pantothenticus.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Virgibacillus.
OX NCBI_TaxID=1473 {ECO:0000313|EMBL:KNE20205.1, ECO:0000313|Proteomes:UP000036780};
RN [1] {ECO:0000313|Proteomes:UP000036780}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 26 {ECO:0000313|Proteomes:UP000036780};
RA Liu B., Wang J., Zhu Y., Liu G., Chen Q., Chen Z., Lan J., Che J., Ge C.,
RA Shi H., Pan Z., Liu X.;
RT "Fjat-10053 dsm26.";
RL Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: DNA polymerase III is a complex, multichain enzyme
CC responsible for most of the replicative synthesis in bacteria. This DNA
CC polymerase also exhibits 3' to 5' exonuclease activity. The alpha chain
CC is the DNA polymerase. {ECO:0000256|ARBA:ARBA00025611}.
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. DnaE
CC subfamily. {ECO:0000256|ARBA:ARBA00009496}.
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:KNE20205.1}.
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DR EMBL; LGTO01000007; KNE20205.1; -; Genomic_DNA.
DR RefSeq; WP_050352774.1; NZ_LGTO01000007.1.
DR GeneID; 66870661; -.
DR PATRIC; fig|1473.5.peg.2242; -.
DR OrthoDB; 9804290at2; -.
DR Proteomes; UP000036780; 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; 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; 1.
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; IPR016195; Pol/histidinol_Pase-like.
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; 1.
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; SSF50249; Nucleic acid-binding proteins; 1.
DR SUPFAM; SSF89550; PHP domain-like; 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:UP000036780};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_00356}.
FT DOMAIN 328..395
FT /note="Polymerase/histidinol phosphatase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00481"
FT DOMAIN 413..579
FT /note="Exonuclease"
FT /evidence="ECO:0000259|SMART:SM00479"
SQ SEQUENCE 1428 AA; 161489 MW; 4B6626E78BA75488 CRC64;
MDISKKEKMD VLLRQLQISE DHLAYFADSY LNKLEIFKQT KTWHFHISTN QVLPCEVYQL
FKHQLQTCFA QIANVELTIE TANRSCSEQT TLNYWENFIQ SFTHLSPAYK DMVQSQTPKV
NGNNIMLTAR NEAEGKAVKK RLEEPFKAYC SKSGLPNFHL QIEVKPELEA IQQFKEQKAA
EDQQLVQRTI QEKTKRDQAK LQPENKPLMF GYKIQDEPVQ MEEILEEERR VTVQGYIFAV
DIRKLRSGRS LLIIKATDYT DSLQIKMFSK GEEDAEKFDV VKEGMWIKAR GSIQTDMYSN
ELAMMANDIH EIKVEPRKDV APDEEKRVEL HAHTTMSQMD AVVSPANLIA QAAKWGHKAI
AITDHAGVQG FPEAYNAGKK HNIKVLYGVE ANLVDDGVPI AYNDKDLDLA TGTYVVFDVE
TTGLSAVYDT IIELAAVKIH QGEIVDRFES FANPHHPLSQ TTTDLTGITD EMVQNAPEVE
EVLTDFRNWM ADDILVAHNA SFDMGFLNQG FKKLGFDKAA NAVIDTLELA RFLFPHLKNH
RLNTLCKHLD IELTQHHRAI YDAEATGYLL WKLVQALLEK EITNHNQLNN HMGEGNAYQR
SRPFHCILIA QTEEGLKNLY KLVSYAHIDY FYRVPRLPRS VLQKYRKGIL VGSACDQGEV
FETMMQKSAE EAEAVARFYD YIEVQPPANY AHLIEKDLVQ NEAQLLDIIK NLVQLGERMD
KKVVATGNVH YLDEQDQIYR QILIASQAGN PLNRVTLPQT PFRTTNEMLE AFYFLGEKKA
TEIVITNTQA IADEIEEIAP VKDGLFTPTI EGADQEIRDL CYTRAKKIYG EPIPEIVTDR
LEKELKSIIG HGFSVIYLIS QKLVKKSLDD GYLVGSRGSV GSSFVATMTE ITEVNPLPPH
YVCPSCHYNE FITDGSVGSG FDLPDKNCPT CATPLTKDGQ DIPFETFLGF KGDKVPDIDL
NFSGSYQPRA HNYTKELFGI DNVYRAGTIG TIAEKTAYGY VKGYASDKQL VYKNAEVDRL
VKGCTGVKRT TGQHPGGIIV VPDDKEIFDF TPIQYPADDR NSEWRTTHFD FHSIHDNLLK
LDILGHDDPT VIRMLQDLSG IDPKTIPTDD PDVMTIFSGP EALGVKAEQI NCKTGTLGVP
EFGTKFVRQM LEDTKPNTFA ELVIISGLSH GTDVWLGNAQ ELINDGICEL PDVIGCRDDI
MVYLMHKGLD ASLAFQIMEF VRKGKGLKDE WITEMKKHDV PDWYIESCKK IKYMFPKAHA
AAYVLMAVRI AYFKVHHPIF FYAAYFTVRA DDFELDTMIK GSNAIRKRIE MITAKGNDAS
PKEKSLLTVL ELSLEMCERG FSFKKVDLYR SSATEFIVEG DALIPPFNAV DGLGTNAALN
IVKAREEGEF LSKEDLRERS KISKTVLEYL DNHGCLEGMA EQNQLSLF
//
