ID A0A259U5S1_9FIRM Unreviewed; 1224 AA.
AC A0A259U5S1;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, 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 ECO:0000313|EMBL:OZC13491.1};
GN ORFNames=SPSIL_54190 {ECO:0000313|EMBL:OZC13491.1};
OS Sporomusa silvacetica DSM 10669.
OC Bacteria; Bacillota; Negativicutes; Selenomonadales; Sporomusaceae;
OC Sporomusa.
OX NCBI_TaxID=1123289 {ECO:0000313|EMBL:OZC13491.1, ECO:0000313|Proteomes:UP000216752};
RN [1] {ECO:0000313|EMBL:OZC13491.1, ECO:0000313|Proteomes:UP000216752}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 10669 {ECO:0000313|EMBL:OZC13491.1,
RC ECO:0000313|Proteomes:UP000216752};
RA Poehlein A., Daniel R.;
RT "Genome sequence of Sporomusa silvacetica DSM 10669.";
RL Submitted (FEB-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Required for replicative DNA synthesis. This DNA polymerase
CC also exhibits 3' to 5' exonuclease activity. {ECO:0000256|HAMAP-
CC 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:OZC13491.1}.
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DR EMBL; LSLK01000152; OZC13491.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A259U5S1; -.
DR OrthoDB; 9804290at2; -.
DR Proteomes; UP000216752; 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 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; IPR012340; NA-bd_OB-fold.
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 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; 2.
DR Pfam; PF17657; DNA_pol3_finger; 1.
DR Pfam; PF14579; HHH_6; 1.
DR Pfam; PF02811; PHP; 1.
DR SMART; SM00481; POLIIIAc; 1.
DR SUPFAM; SSF89550; PHP domain-like; 1.
PE 3: Inferred from homology;
KW Cytoplasm {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:UP000216752};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_00356}.
FT DOMAIN 326..393
FT /note="Polymerase/histidinol phosphatase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00481"
SQ SEQUENCE 1224 AA; 136725 MW; F73A439960017A8E CRC64;
MSSYCVIPEN CQSFFQFVEQ LPVDVVNREV LKAAQVNKVE VNPVAKTWII FITVAKPVSE
QTIGIIAEHL CQQCGLTTVR FTQQTKDLKQ YLVENWSQFV EQITEGHYAT KHLLLHAIWS
YEEETLTIET IGGLSTAILA ERGIEQVIKA FIIRNFGHSC EVKFLYSEME EVVNCDEALL
TPAFKEAVIS QDRPKANAND SPIIFGRNIR GAAAAVQPIN AIQEEARNVV LTGQILTHEV
KELKSGRFLL TFDLVDLTDG ISGKAFFDNK EQFDKATGLI KNGMQATVKG TVQYDKFANE
LILFTDSMCR AEKVEERQDN APIRRIELHA HTRMSAMDAV VSAKNLVKTA AKWGHSAIAI
TDHGVVQAFP EAYEEAASVG IKVIYGMEGY LFDDDINQAR HIIILAQNNI GLRNLYRLVS
ISHLRYLHRT PRIPRMILDD YREGLLLGSA CEAGELIHAM INGASQEELI TIAKYYDYLE
IQPTGNNEFL VRKGKIADEE GLRDINRKVC AIGAQLGKPV AATCDVHFLN PEDEVYRRIL
MAGRGYDDAD RQPPLFFRTT DEMLAEFSYL GVAKAHEVVI EVPKRINDSI ESIKPIPEEL
YSPQIPGAEE DIKFMSYQNA EQLYGTPLPE IVAKRLENEL DSIINHGFAV LYLIAHKLVK
KSMDDGYLVG SRGSVGSSFV ATMTGITEVN PLPPHWRCPS CKYSEFITDG SYGGGFDLPE
KVCPHCQTDM EKNGHDIPFA VFMGFHGDKV PDIDLNFSGD YQPVAHKYTE ELFGRDNVFR
AGTIATIADK TAYGYVKNYL NDKGSTARNA YINKLLGGCT GVKRTTGQHP GGIMVIPRDM
DVHHFTPIQY PADDKNSSTI TTHFDYHSIS SRLVKLDILG HDDPTVIKML EDLTNLDAKT
IPFDDAATMS LFSSTDALHL TPEALNSTVA TFGIPEFGTK FVRQMLEDTK PKTFSELIRI
SGFSHGTDVW LNNAQDLIRS GTAKLSEAIS TRDDIMVYLM QKGVEPLLAF KTMESVRKGK
GIKPDDVEKI RAKNVPEWFI ESCQKIKYMF PKAHAVAYVM MAFRIAYCKV HHPLAFYAAY
CTVRATDFDA DLIVKGAKVL KDELVILEEK GNTLSTKEKS IQTILEIAHE MYLRGYVFHR
VDLYKSDAEK FLIVDNGLLP PIGSLQGVGV SAAHNIVAAR QNKDFSSIED LRSRSRVSKT
VIDILKNHGC LAGLDDSDQI QLFA
//
