ID E3I1C7_RHOVT Unreviewed; 1151 AA.
AC E3I1C7;
DT 11-JAN-2011, integrated into UniProtKB/TrEMBL.
DT 11-JAN-2011, sequence version 1.
DT 27-MAR-2024, entry version 66.
DE RecName: Full=DNA polymerase III subunit alpha {ECO:0000256|ARBA:ARBA00019114};
DE EC=2.7.7.7 {ECO:0000256|ARBA:ARBA00012417};
GN OrderedLocusNames=Rvan_1983 {ECO:0000313|EMBL:ADP71218.1};
OS Rhodomicrobium vannielii (strain ATCC 17100 / ATH 3.1.1 / DSM 162 / LMG
OS 4299).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Hyphomicrobiaceae; Rhodomicrobium.
OX NCBI_TaxID=648757 {ECO:0000313|EMBL:ADP71218.1, ECO:0000313|Proteomes:UP000001399};
RN [1] {ECO:0000313|Proteomes:UP000001399}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 17100 / ATH 3.1.1 / DSM 162 / LMG 4299
RC {ECO:0000313|Proteomes:UP000001399};
RX PubMed=21705585; DOI=10.1128/JB.05453-11;
RG US DOE Joint Genome Institute;
RA Brown P.J., Kysela D.T., Buechlein A., Hemmerich C., Brun Y.V.;
RT "Genome sequences of eight morphologically diverse alphaproteobacteria.";
RL J. Bacteriol. 193:4567-4568(2011).
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 -!- 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};
CC -!- SUBUNIT: DNA polymerase III contains a core (composed of alpha, epsilon
CC and theta chains) that associates with a tau subunit. This core
CC dimerizes to form the POLIII' complex. PolIII' associates with the
CC gamma complex (composed of gamma, delta, delta', psi and chi chains)
CC and with the beta chain to form the complete DNA polymerase III
CC complex. {ECO:0000256|ARBA:ARBA00026073}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC -!- SIMILARITY: Belongs to the DNA polymerase type-C family. DnaE
CC subfamily. {ECO:0000256|ARBA:ARBA00009496}.
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DR EMBL; CP002292; ADP71218.1; -; Genomic_DNA.
DR RefSeq; WP_013419604.1; NC_014664.1.
DR AlphaFoldDB; E3I1C7; -.
DR STRING; 648757.Rvan_1983; -.
DR KEGG; rva:Rvan_1983; -.
DR eggNOG; COG0587; Bacteria.
DR HOGENOM; CLU_001600_0_0_5; -.
DR OrthoDB; 9803237at2; -.
DR Proteomes; UP000001399; Chromosome.
DR GO; GO:0008408; F:3'-5' exonuclease activity; IEA:InterPro.
DR GO; GO:0003887; F:DNA-directed DNA polymerase activity; IEA:UniProtKB-KW.
DR GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
DR CDD; cd04485; DnaE_OBF; 1.
DR CDD; cd07433; PHP_PolIIIA_DnaE1; 1.
DR Gene3D; 1.10.150.870; -; 1.
DR Gene3D; 1.10.10.1600; Bacterial DNA polymerase III alpha subunit, thumb domain; 1.
DR Gene3D; 3.20.20.140; Metal-dependent hydrolases; 1.
DR InterPro; IPR011708; DNA_pol3_alpha_NTPase_dom.
DR InterPro; IPR041931; DNA_pol3_alpha_thumb_dom.
DR InterPro; IPR040982; DNA_pol3_finger.
DR InterPro; IPR004805; DnaE2/DnaE/PolC.
DR InterPro; IPR029460; DNAPol_HHH.
DR InterPro; IPR004013; PHP_dom.
DR InterPro; IPR003141; Pol/His_phosphatase_N.
DR InterPro; IPR016195; Pol/histidinol_Pase-like.
DR InterPro; IPR049821; PolIIIA_DnaE1_PHP.
DR NCBIfam; TIGR00594; polc; 1.
DR PANTHER; PTHR32294; DNA POLYMERASE III SUBUNIT ALPHA; 1.
DR PANTHER; PTHR32294:SF0; DNA POLYMERASE III SUBUNIT ALPHA; 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 SMART; SM00481; POLIIIAc; 1.
DR SUPFAM; SSF160975; AF1531-like; 1.
DR SUPFAM; SSF89550; PHP domain-like; 1.
PE 3: Inferred from homology;
KW DNA replication {ECO:0000256|ARBA:ARBA00022705};
KW DNA-directed DNA polymerase {ECO:0000256|ARBA:ARBA00022932};
KW Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695,
KW ECO:0000313|EMBL:ADP71218.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000001399};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:ADP71218.1}.
FT DOMAIN 7..74
FT /note="Polymerase/histidinol phosphatase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00481"
SQ SEQUENCE 1151 AA; 126291 MW; 566B2B65549A51EC CRC64;
MTKPGFIHLH VHSAYSLLEG ALPVKALIKA AAADGQPALA ITDRNNLFGA LEFSEYLSGE
GIQPIIGCAL TLAFPAPADE TPRPGQRPDA HSGTIVLLAK DAEGYGNLMR LSSRAFLDSG
DGSNPHVEVE FLVEHAGGLI ALSGGPDGPA DRAFAAGNAA IAEARLATLA EAFGNRFYVE
IQRHGLARER AVEPQLLRWA YDNGVPLVAT NEAYFPKRAV FEAHDALLCI AEGRYVAEDD
RRRLSPDHWL KPQADMVKLF ADLPEAVANT IEIAQRCAFR PRPRKPILPQ FVAGSEDTHE
AEAAELRRQA IAGLEHRLAT IPAHFHAASK DEYFKRLEFE LDVITRMKFP GYFLIVSDFI
KWAKAQGIPV GPGRGSGAGS VVAWSLTITD LDPIRFGLLF ERFLNPERVS MPDFDIDFCQ
DRRDEVIQYV RAKYGSNRVA QIITYGKLQA RAVLRDVGRV LQMPYGQVDR LCKLVPNNPA
NPVTLAEAIE GEPQLQEARD REEIVAQLLD TAQKLEGLYR HASTHAAGVV IGDRDLVELV
PLYRDPKSDM LVTQFNMKWV EQAGLVKFDF LGLKTLTVLQ KACALLEKAG RPIDLGHLPL
DDRPTYEMLA KGDTGGVFQL ESTGMREALR KLKPDRFGDI IAMVALYRPG PMDNIETYVN
RKHGIEVPDY LHPLAKPILE ETYGVIIYQE QVMQLAQVLS GYSLGEADLL RRAMGKKIKA
EMDAQGARFV KGALEKDIPE ARARYIFELV AKFAGYGFNK SHAAAYALIA YQTAYLKANH
AQEFIAASMT LDMANTDKLY AFTREAKRNG LAILPPSVNK SAVEFEPEGD NAIRYALAAL
KNMGHAAAAH IVEARGDKPY RDLADFMLRI NPKALNKRGI ETLNAAGAFE DMETNRAKVA
KNLDRLVEFG SKAAEDRARG QEDMFGGGIA GSPAPRLDLA DAPEWSLVET LENELGAAGF
YLSGHPLDDF TDQLARMNVL KWSDFSARVQ AHGRAESRLA ATVTYRQDRK AKSGNRFAFA
GFSDPTGQFE AVIFSDTLNV AGDKLEAGKN VLVHVEGEAD GEAIKVRVQA VQALDEVLGK
ITKQVSITAT ERLQVAELVK HLGREGGIQV NLVVQIPEAQ KAVEFKLGDN FSITARQLAT
LKTLPGVLQV G
//
