ID A0A2T4ZAT0_9BACL Unreviewed; 1431 AA.
AC A0A2T4ZAT0;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 24-JAN-2024, entry version 21.
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 ORFNames=C8J48_1566 {ECO:0000313|EMBL:PTM58967.1};
OS Desmospora activa DSM 45169.
OC Bacteria; Bacillota; Bacilli; Bacillales; Thermoactinomycetaceae;
OC Desmospora.
OX NCBI_TaxID=1121389 {ECO:0000313|EMBL:PTM58967.1, ECO:0000313|Proteomes:UP000241639};
RN [1] {ECO:0000313|EMBL:PTM58967.1, ECO:0000313|Proteomes:UP000241639}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 45169 {ECO:0000313|EMBL:PTM58967.1,
RC ECO:0000313|Proteomes:UP000241639};
RA Goeker M.;
RT "Genomic Encyclopedia of Archaeal and Bacterial Type Strains, Phase II
RT (KMG-II): from individual species to whole genera.";
RL Submitted (APR-2018) 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:PTM58967.1}.
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DR EMBL; PZZP01000001; PTM58967.1; -; Genomic_DNA.
DR OrthoDB; 9804290at2; -.
DR Proteomes; UP000241639; 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; 3.30.300.180; -; 1.
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; IPR038454; DnaA_N_sf.
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; 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; SSF89550; PHP domain-like; 1.
DR SUPFAM; SSF81585; PsbU/PolX 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:UP000241639};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_00356}.
FT DOMAIN 332..399
FT /note="Polymerase/histidinol phosphatase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00481"
FT DOMAIN 417..583
FT /note="Exonuclease"
FT /evidence="ECO:0000259|SMART:SM00479"
SQ SEQUENCE 1431 AA; 161718 MW; 09FD8A02D6FB8A73 CRC64;
MSVTEARRER WEAVMKRAQL PTEMATYFTE ASIEKVKVSR KQKMWTFYLR LETPVPPNVM
FAMQKQVAEA FHPVVQVQFV VRYQQADLEQ LIEMYWHWIR KKVAQNLSPS AAGWLSRAEW
TMVDSTLTLS FPSRMMTQMA VAKQLDQVVS SLFQEVSGTR IQVKLQVDAN SQAQEQFREQ
REQEEKKLIQ EAMVSLEEAA SAPDEGGAEE EGPVTIGYDF NDEPILIKEI TDEERRVCIK
GKVFKVEMRE LRSGRTLLTF NVTDYSDSIA VKVFARDKED AATLTRIKDG MWVALRGSVQ
YDTFARDLVV MANDIREVKP YKRMDTADEK RVELHLHTAM SAMDGVYDPG EMVKRAAEWG
HPAVAITDHG VLQAYPDAFS AGKKHGIKIL YGLEAFVVDD GVSVVMNEEK RLLKEDTYVV
FDVETTGLSA MHDEIIELAA VKVENGAIVD RFESFVNPHR PLSATITELT SITDDMVKDA
PDLDAVLPDY LNFIEGTVLV AHNARFDMGF LQAGAKKIGR EPVKNPVIDT LELGRLLYPR
LKNHRLNTLC KQFDIDLTQH HRAIYDAEAT GYLLWKMLED CVERELPRLD QLNQLTGERD
VSRLRPFHGI VLVENLTGLK NLYKMVSESH LNYFHRTPRI PRSLLQKYRE GLIVGSGCEK
GELYEAALTK SPEEVEAIAE FYDYLEIQPI EVNRHLVEKE LVENEERLRD ANRLLVEIGE
KLGKPVVATS NAHYLDAWDS PFRDILAFNQ TGGFRNSGPL SPVHFRTTDE MLAEFSYLGE
EKAIEVVVTN PRAIADRIEE MKPFPDDLHT PIIEGAEEEL RQICYDTARE MYGEPLPTIV
EERLEKELGS IIKHGFAVIY LISQKLVVKS LQDGYLVGSR GSVGSSFVAT MSHITEVNPL
PPHYVCPSCK HSQFIADGTV ASGFDLPDKD CPECGSNMKK DGHDIPFETF LGFKGDKVPD
IDLNFSGEYQ PQAHKYTEEL FGKDYVYRAG TISTVAQKTA FGYVKKFEEE KGQQWRSAEI
DRMVEGCSGV KRTTGQHPGG QMVIPQNLEV FDFTPIQRPA DDVKSETITT HFDYHAISGR
LLKLDILGHD DPTVIRMLQD LTGVDPQSIP VDDPEVMKLF SGTESLGITP EELGTVTGTL
GIPEFGTRFV RQMLEDTKPT TFSELVRISG LSHGTDVWLN NAQDLVRNGT AVLSEVISTR
DDIMIYLIYK GMDPSIAFKL MEKVRKGKGL TEEEGELMRQ HDVPQWYIDS CRKIKYMFPK
AHAVAYVLMA VRIAWFKVYH PIEYYATYFT VRADDFDVEL VLKGKDAVKK AIVEIEEKGV
SASPKEKGLL TILESVREML ARGLTFQRVD LYRSDATHFK VEGDSLIPPF SSVSGIGTNA
AKNIVVARQD GEFLSIEDLT KRARVTSAVV EVLKRLGCLD EMPESNQLTL F
//
