ID F4QQL4_9CAUL Unreviewed; 1133 AA.
AC F4QQL4;
DT 28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT 28-JUN-2011, sequence version 1.
DT 27-MAR-2024, entry version 47.
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:EGF90501.1};
GN ORFNames=ABI_35240 {ECO:0000313|EMBL:EGF90501.1};
OS Asticcacaulis biprosthecium C19.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Caulobacterales;
OC Caulobacteraceae; Asticcacaulis.
OX NCBI_TaxID=715226 {ECO:0000313|EMBL:EGF90501.1, ECO:0000313|Proteomes:UP000006512};
RN [1] {ECO:0000313|Proteomes:UP000006512}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C19 {ECO:0000313|Proteomes:UP000006512};
RA Brown P.J.B., Buechlein A., Hemmerich C., Brun Y.V.;
RT "Draft genome sequence of Brevundimonas diminuta.";
RL Submitted (MAR-2011) to the EMBL/GenBank/DDBJ databases.
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; GL883079; EGF90501.1; -; Genomic_DNA.
DR AlphaFoldDB; F4QQL4; -.
DR STRING; 715226.ABI_35240; -.
DR eggNOG; COG0587; Bacteria.
DR HOGENOM; CLU_001600_0_0_5; -.
DR Proteomes; UP000006512; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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:0003676; F:nucleic acid binding; IEA:InterPro.
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; IPR004365; NA-bd_OB_tRNA.
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 Pfam; PF01336; tRNA_anti-codon; 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 Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 1..66
FT /note="Polymerase/histidinol phosphatase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00481"
SQ SEQUENCE 1133 AA; 126139 MW; 72B2FF3EC8ACC251 CRC64;
MRVRSAYSLL EGAIKAYDMG KLAHKNGMPA VAITDRCNLY GGLEFSQSCK DSGVQPIVGC
ALPVKGIGGT PTEKWARIPT FVVLCQNEQG WLNLTKLSSI AYVDSDNMDE PHVTWDQVTA
HNEGLLLLSG SYDGPVDVLF RQNRPDEGKA ALKSMLDVFG DRFYIELQRH EGRPKGSATE
AGLVEFAYQN DVPLVATNDA YFAGADMYRA HEALLCISDS TFMGIEDRRR VTKDHWFKPA
AAMRELFADL TEACDNTIEI ARRCAFLVNK RDPILPRFDT GAGRNEDEEL AWQAREGLKM
RLKQVKLACP EEDYWARLER EIGVIQKMGF PGYFLIVSDF IKWGKSHGVP VGPGRGSGAG
SLVAWALTIT DLDPLRFGLL FERFLNPERV SMPDFDIDFC QERREEVISY VQHKYGRDRV
AQIITFGTLQ ARAVLRDVGR VMQLPLGQVD RLCKMVPNNP ANPTTLAQAI EIEPRLREAR
DDDEQVKNLL DTALKLEGLY RNASTHAAGI VIGDRPLTEL VPLYRDPRSD IPATQFNMKW
VESAGLVKFD FLGLKTLTVL DRAERYLKKR GVDINFSILP LDDTATYELL ASGQSIGVFQ
LESQGMRDTL RKLRCSSLEE ITALISLYRP GPIDNIDTYV DRKFGRMEID MLHPSLEPVL
KETYGVIIYQ EQVMQIAQVL SGYSLGEADL LRRAMGKKKK EEMDLQKVRF MTGAKEKGVP
EAQSDFIFEL VNKFAGYGFN KSHAAAYAFI SYQTGYLKAN HPVEFFAASF SLDIANTDKL
AVFYQDARRF GVPIVPPDIN RSMADFDVEN GELLYALGAI RNVGFEAMQS VVQAREEGGK
FTDLFDFLER IDPKAVNRRA IENLAKAGAF DSIHPNRAQI VAAADMLIAY AQSVAAERAS
SQVSLFGSTD ASRPRLPKVA ASAGPERLDE ELAAIGFYLS GHPLQDMLDV FKRRKITLYA
EAMSLALEGH DAFRMAGIVR RRQERAAAGS GEKFAFVTLS DPSGEYEVLF PPESLRRCRD
QLEPGASIVL KVRAKGKEGE VRFFGDEAGP MATSIKTDDL GLKLHVSAQV IDLAVLRAQL
EASKLPNGGK ISLLSDLAGQ GQIEFDLPHR YSLDAHMRGR LKAMPGVLYF EDV
//
