ID C4GBI7_9FIRM Unreviewed; 1532 AA.
AC C4GBI7;
DT 07-JUL-2009, integrated into UniProtKB/TrEMBL.
DT 07-JUL-2009, sequence version 1.
DT 24-JAN-2024, entry version 86.
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:EEP28480.1};
GN ORFNames=GCWU000342_01290 {ECO:0000313|EMBL:EEP28480.1};
OS Shuttleworthia satelles DSM 14600.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae;
OC Shuttleworthia.
OX NCBI_TaxID=626523 {ECO:0000313|EMBL:EEP28480.1, ECO:0000313|Proteomes:UP000003494};
RN [1] {ECO:0000313|EMBL:EEP28480.1, ECO:0000313|Proteomes:UP000003494}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 14600 {ECO:0000313|EMBL:EEP28480.1,
RC ECO:0000313|Proteomes:UP000003494};
RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., Courtney L.,
RA Fronick C., Harrison M., Strong C., Farmer C., Delahaunty K., Markovic C.,
RA Hall O., Minx P., Tomlinson C., Mitreva M., Nelson J., Hou S., Wollam A.,
RA Pepin K.H., Johnson M., Bhonagiri V., Nash W.E., Warren W., Chinwalla A.,
RA Mardis E.R., Wilson R.K.;
RL Submitted (APR-2009) 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|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:EEP28480.1}.
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DR EMBL; ACIP02000002; EEP28480.1; -; Genomic_DNA.
DR RefSeq; WP_006906298.1; NZ_GG665866.1.
DR STRING; 626523.GCWU000342_01290; -.
DR eggNOG; COG2176; Bacteria.
DR HOGENOM; CLU_003297_2_0_9; -.
DR Proteomes; UP000003494; 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; cd07432; PHP_HisPPase; 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; 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; 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; PF07733; DNA_pol3_alpha; 1.
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 SMART; SM00479; EXOIII; 1.
DR SMART; SM00481; POLIIIAc; 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:UP000003494};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_00356}.
FT DOMAIN 413..481
FT /note="Polymerase/histidinol phosphatase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00481"
FT DOMAIN 499..664
FT /note="Exonuclease"
FT /evidence="ECO:0000259|SMART:SM00479"
FT REGION 208..281
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1532 AA; 172649 MW; 3FD5B00369958C6E CRC64;
MAKAFQELFS NLKLSAGLTG LLENAQIERV TTNRQHDVMR IYLSFQDLIP KRRIWKLEKA
IASQYFKEQQ VDVRIIERFY LSEAYNAKNL FASYRDSIYE EIEHYSSILY GIIKKADFTF
DRDDHLELTL EDTVLARGRE EEIHDILDKI FCQRCGQTLL IDIAYKQAKK SKYRADTDAV
IANRVTEIVE RQKQMLEKEA AAEAAQGLPS EDLGLGHRPH LQKQMGKKGQ SPDFAKRQGE
TGKRQEGGRT SVYFAAGGSS ADRGKPSWKQ GERGSASFRG PRPLKYSSHA DLIYGRDFDD
EVTPISEIQG AVGEVCIRGQ IISFETREIR NERTLVSFAL TDFTDSIVTK LFVANAHMEE
LEKGLHKGAF VKIKGTPSLD TFDHDLTMGY VKGIMAIPSF QTIRADNAAT KRVELHCHTK
MSDMDGVSAV EDIVRQARHF GHKALAITDH GVVQAFPDAD HEIGKDPDFK VIYGMEAYLV
DDTKTVVTDG LPGQSLDDSF VVFDIETTGF SAEKDRIIEI GAVRMEGGRI TDRFSSFVNP
GRPIPFRITE LTSIRDDMVI GSAGIEEVLP DFLAFSQGAI MVAHNADFDM GFIRQNCLRL
HLEAPATYMD TVAMGRYLMP SLHNQKLNTL AKALKIDPGH HHRAVDDAEA TAHIFEKFIQ
MFRDRGMNEL SDINANARMS DEVIRKMHAN HCILIARNDI GRINLYKLTS LSHLRFFQRQ
AKIPKSLVEK YREGLIIGSA CEAGELFQAL EGGRPPQEIS RIVSFYDYLE IQPIGNNRFL
LEADNDNIQT EEDLRDFNRR IVRLGEDFHK PVCATGDVHF LNPEDEIYRR IIQVGKGFKD
ADHQPPLFLH TTEEMLEEFS YLGMDKAREV VITNTNRIAD MCERIHPTRP DKCPPVIANS
DQMLRTICHN RAHELYGKKL PAIVEERMER ELNSIIGNGY AVMYIIAQKL VWKSNEDGYL
VGSRGSVGSS FAAYLAGITE VNSLQAHYLC PDCKFVDFDS DQVKAFAGRS GCDMPDRKCP
RCGADLMKLG FDIPFETFLG FKGNKEPDID LNFSGEYQAK AHKYTEVIFG EGQTFKAGTI
GTLADKTAYG YIKNYYEERG IHKRSCEIDR IVQGCVGIRR TTGQHPGGIV VLPVGEEINS
FTPVQHPADD MTSDIITTHF DYHKIDGNLL KLDILGHDDP TMIRKLEDLT GLRATDIPLD
DKAVMGLFMG TDSLGIPEGD QLWGGTSMGT LGIPEFGTDF AMGMLRDAKP KEFSDLIRIS
GLSHGTDVWL GNAKDLIQQG IATISTAICC RDDIMVYLIN QGMDSEESFT IMERVRKGLV
AKGKVADDWA KWTADMKEHG VPDWYIGSCE KIKYMFPKAH AAAYVMMAWR VAYCKVYYPL
AYYAAFFSIR ATAFSYEIMC RGRNYLETIL AEYDKRRDQL SNKEQDTYRD MRIVQEMYVR
GYEFLPLDLY QSDARYFKIV DGKLLPPFAS IDGMGDKAAE TLAIAAAQGK FLSMDDLKER
GKLSQTIADK LNELGLTGDM PKSNQLSIFD FA
//
