ID U7UBL5_9FIRM Unreviewed; 1409 AA.
AC U7UBL5;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 24-JAN-2024, entry version 54.
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:ERT56750.1};
GN ORFNames=HMPREF1253_1563 {ECO:0000313|EMBL:ERT56750.1};
OS Peptoniphilus sp. BV3C26.
OC Bacteria; Bacillota; Tissierellia; Tissierellales; Peptoniphilaceae;
OC Peptoniphilus.
OX NCBI_TaxID=1111134 {ECO:0000313|EMBL:ERT56750.1, ECO:0000313|Proteomes:UP000017105};
RN [1] {ECO:0000313|EMBL:ERT56750.1, ECO:0000313|Proteomes:UP000017105}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BV3C26 {ECO:0000313|EMBL:ERT56750.1,
RC ECO:0000313|Proteomes:UP000017105};
RA Durkin A.S., Haft D.R., McCorrison J., Torralba M., Gillis M., Haft D.H.,
RA Methe B., Sutton G., Nelson K.E.;
RL Submitted (SEP-2013) 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}.
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:ERT56750.1}.
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DR EMBL; AWXB01000065; ERT56750.1; -; Genomic_DNA.
DR RefSeq; WP_023056387.1; NZ_AWXB01000065.1.
DR STRING; 1111134.HMPREF1253_1563; -.
DR PATRIC; fig|1111134.3.peg.1762; -.
DR eggNOG; COG2176; Bacteria.
DR OrthoDB; 9804290at2; -.
DR Proteomes; UP000017105; 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; 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; 1.20.5.140; -; 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; 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; 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; SSF81585; PsbU/PolX domain-like; 1.
DR SUPFAM; SSF53098; Ribonuclease H-like; 1.
PE 3: Inferred from homology;
KW Coiled coil {ECO:0000256|SAM:Coils};
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:UP000017105};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_00356}.
FT DOMAIN 314..381
FT /note="Polymerase/histidinol phosphatase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00481"
FT DOMAIN 398..563
FT /note="Exonuclease"
FT /evidence="ECO:0000259|SMART:SM00479"
FT COILED 153..184
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 1409 AA; 160991 MW; 07A67271F5735D43 CRC64;
MVNLKNILNK LNLKLNIDAE EIKLGSIKFN EEKMDLNLVF FTGYELDEKI KNEIREALKD
YLKEILVNVY FEVKEIKEIE DKVFSFLIKN CPSIQSWLKK EDLKIDEDLK TINLEAPDKI
TYKAILNNDA LKRLNDEVLK DNYKFQLTFN EEFKEAEDLL NDYYKELENM EKEACKSVQA
ANQNLSFKKT DKEIINTYGK KTSGEEVSIN DLSSEFTNVK IKGYIFKLDS KETKSGKILA
MIYLTDYSNS IECKVFISNK KAQSFFNSFK VNDYVEVCGK FTFDSFSKTD VIMVNYIKKL
EKIEKEDKYN KKRVELRLHS KMTTMSGVTE FSKFAKKAQE WGHPAIAITD LTDVQAFPEA
SEFAEKNNIK ILYGLDGRMI EDEGNIVDYY ENHDFNNSYV VFDIETTGLS PYRDKITEIG
AVKVVDGEIV DRFSQLINPE REIPLTVQNL TGLSNAMLAD EPTIDKVIYD FKNFIEGSTL
VAHNAQFDIS FIRREMNDKN LNFDYPVLDT LFLSRALLKG QKRFNLSAIS KVLGVSLIGA
HRAVNDAEAT AHVFIKLLSL AGNPKSFEEI NLLFKDIKKG VLFPTSMTIL IKDKVGLKNL
YKLVSQSHLN YFSKEAKIPK SLLKSMRQGL LYGSGNSESD LWQAIYFKKP QEEILKIAEF
YDYLEIQPID NNINYIVQDK LTKDDLININ KEIVRIGKKL NKIVVADSDS YYLDQHEDLI
RRIVLNGKQG PTREEEKIPQ KLYFRTSDEM MEEFNYLGEE KEKIVIDNTI EIANMCQEIK
PLPDGKFPPY IEGSEHDLRE MTYKKAHEIY GDNLPKIVEE RLEKELSSII GNGYAVLYII
AQKLVTKSNK DGYLVGSRGS VGSSFAATMA GITEVNPLPP HYVCPKCKHS EFVDEKSVGS
GIDLPVKNCP LCGEEMRRDG HNIPFEVFLG FEGDKEPDID LNFAGEYQPV AHKYTEELFG
EGYVFRAGTI GTIAEKTAYG YINDFYENKM IRQAEKDRLA GSIVGIKRTT GQHPGGVMIV
PKTSDIFDFS PIQHPADKAS TNVITTHFDY NFLHGKILKL DILGHDGPTI IKMLEDLTKV
NSSTIELNDE RTMKLFSSTE GLGIDEKICS TPTGTLGIPE FGTDFVKRML IKTKPKTFSE
LVRISGLSHG TDVWTNNAEI LVDEKRAELS QVISTREDIM IYLIQAGAEN KMAFFTMEKV
RKGKGLTEEQ MEIMKKLPLP DWYIDACLKI KYMFPKAHAV AYVMLSFRVA WYKLNYPLAF
YTTYFTNKLS DFSLEYILAG QKSIKERIQE ISNDPKPTQK DKDQKTVLEL ALEMISRGYN
FLGVDIYKSD AKKFKIEGNN IRVPLMSLPG LGENIANEIV KSSENYKYIS VEDFIEKTKA
TKSIVEMLKN QGCFDNMDTT NQISIFNFL
//
