ID H8K3B0_RICAG Unreviewed; 1181 AA.
AC H8K3B0;
DT 16-MAY-2012, integrated into UniProtKB/TrEMBL.
DT 16-MAY-2012, sequence version 1.
DT 27-MAR-2024, entry version 64.
DE RecName: Full=DNA polymerase III subunit alpha {ECO:0000256|ARBA:ARBA00019114};
DE EC=2.7.7.7 {ECO:0000256|ARBA:ARBA00012417};
GN Name=dnaE {ECO:0000313|EMBL:AFC70302.1};
GN OrderedLocusNames=MCE_07640 {ECO:0000313|EMBL:AFC70302.1};
OS Rickettsia amblyommatis (strain GAT-30V) (Rickettsia amblyommii).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rickettsiales;
OC Rickettsiaceae; Rickettsieae; Rickettsia; spotted fever group.
OX NCBI_TaxID=1105111 {ECO:0000313|EMBL:AFC70302.1, ECO:0000313|Proteomes:UP000008005};
RN [1] {ECO:0000313|Proteomes:UP000008005}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GAT-30V {ECO:0000313|Proteomes:UP000008005};
RA Johnson S.L., Munk A.C., Han S., Bruce D.C., Dasch G.A.;
RT "Complete genome sequence of Candidatus Rickettsia amblyommii strain GAT-
RT 30V.";
RL Submitted (FEB-2012) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:AFC70302.1, ECO:0000313|Proteomes:UP000008005}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GAT-30V {ECO:0000313|EMBL:AFC70302.1,
RC ECO:0000313|Proteomes:UP000008005};
RX PubMed=27638476; DOI=10.1099/ijsem.0.001502;
RA Karpathy S.E., Slater K.S., Goldsmith C.S., Nicholson W.L., Paddock C.D.;
RT "Rickettsia amblyommatis sp. nov., a spotted fever group Rickettsia
RT associated with multiple species of Amblyomma ticks in North, Central and
RT South America.";
RL Int. J. Syst. Evol. Microbiol. 66:5236-5243(2016).
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; CP003334; AFC70302.1; -; Genomic_DNA.
DR RefSeq; WP_014392795.1; NC_017028.1.
DR AlphaFoldDB; H8K3B0; -.
DR STRING; 1105111.MCE_07640; -.
DR KEGG; ram:MCE_07640; -.
DR HOGENOM; CLU_001600_0_0_5; -.
DR Proteomes; UP000008005; 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; 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:AFC70302.1};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:AFC70302.1}.
FT DOMAIN 6..73
FT /note="Polymerase/histidinol phosphatase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00481"
SQ SEQUENCE 1181 AA; 132998 MW; 0374191C4DE7B56B CRC64;
MRPEFIHLRT QSSYSFLESA LTIEKVVELA SSNKMPAICL ADKGNLFGSL EFALYALKKG
LQPIHGVILN IKYDIDIFAQ ILLIAKDETG YKNLLKLSSL TFTKNDRKIC DHIDFEDLIK
YQEGLIGLCC YTDGIVGKCL LARNEEQAML FARKLQEILG DRFYFEIMRH ELPEEQFIED
SYIRIAAELA IPLVATNKVL FSEKSMHDAH DVLLCISAGV TKEYPDRKTV SENCYFRSPH
EMIELFSDLP SAIQNTVNLR ERCYFAAHAN PPMLPNFATK DISETDLIRK DAKEGLLARL
ATKFKSENIS LENQEELKTE YFARLNYELD IICNMNFAGY FLIVSDFIKW SKKEGILVGP
GRGSGAGSVV AWSLLITDLD PIKFGLLFER FLNPERISMP DFDIDFCQER REEVINYVRS
KYGNNRVGQI ITFGKMQAKA VIKDVARVLS LPYKFADYLT ELVPFSAVNP VSLEQAMREV
PELANAAKGN GLYNLDGEAE LIKLVLDTSL ILEGLHRHAS THAAGIVIAG TDLVDIVPVY
KDANSDMLVV GYSMKYSEIA GLIKFDFLGL QTLTVITDCK KLLKEQGIEV EFNNMTFDDN
KTYQMLCKGK GVGVFQFESI GMKDALRRLK PDSIHDLIAL GALYRPGPME NIPTYIACKH
KLQQPDYLHE LLKPILEETY GVVIYQEQVQ RIAQVLAGYT LGAADLLRRA MGKKIKKEME
EQEEMFVKGA IANNISESQA KSIFATVAKF AGYGFNKAHA ASYGVISYQT AYLKANYPAE
FLVACLNLEL NNHDKINLFL QEAKDNGIKI TAPNINISEG YFSVKFSDTV IPHSVRPVIP
RLDRGIQEIS KDTVVKPRYD IAGAIIFALG AIKGVTPNFG KLVTDERKAR GAFKSITDFI
ERLPPKSINS KLLENLIKSG CFDELHDNRL QLLLSIPKLL SYSISYHEEQ ESNQFSLIKV
SSLSPTILVS SDYADKNTLA FYEFEAMGLF ISNHPLTEYQ EIFSRLNILN TADLYNNLPD
GTNRVNLAGV IQKKDSRMSA RGRFVTLVLS DPENIFELSI FSEEVLKDYV HLLDVKSLVV
VNCDIVKDEG GIKLTAKSFS SIEDAINNKQ FELQFYPQNH EELRQIVTLL AARINNEDQS
NAKATIYLQS ADVKNFVAKI TLPEKFLLQG QDFEILKGYS K
//
