ID A0A1W6L6B6_9BURK Unreviewed; 1167 AA.
AC A0A1W6L6B6;
DT 05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2017, sequence version 1.
DT 27-MAR-2024, entry version 27.
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:ARN19871.1};
GN ORFNames=A4W93_08065 {ECO:0000313|EMBL:ARN19871.1}, GCM10007918_23370
GN {ECO:0000313|EMBL:GLS95045.1};
OS Piscinibacter gummiphilus.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Sphaerotilaceae; Piscinibacter.
OX NCBI_TaxID=946333 {ECO:0000313|EMBL:ARN19871.1, ECO:0000313|Proteomes:UP000193427};
RN [1] {ECO:0000313|EMBL:ARN19871.1, ECO:0000313|Proteomes:UP000193427}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NS21 {ECO:0000313|EMBL:ARN19871.1,
RC ECO:0000313|Proteomes:UP000193427};
RA Tabata M., Kasai D., Fukuda M.;
RT "Complete genome sequence of natural rubber-degrading, novel Gram-negative
RT bacterium, Rhizobacter gummiphilus strain NS21.";
RL Submitted (APR-2016) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:GLS95045.1, ECO:0000313|Proteomes:UP001157201}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NBRC 109400 {ECO:0000313|EMBL:GLS95045.1,
RC ECO:0000313|Proteomes:UP001157201};
RX PubMed=30832757;
RA Wu L., Ma J.;
RT "The Global Catalogue of Microorganisms (GCM) 10K type strain sequencing
RT project: providing services to taxonomists for standard genome sequencing
RT and annotation.";
RL Int. J. Syst. Evol. Microbiol. 69:895-898(2019).
RN [3] {ECO:0000313|EMBL:GLS95045.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=NBRC 109400 {ECO:0000313|EMBL:GLS95045.1};
RA Sun Q., Mori K.;
RT "Draft genome sequence of Rhizobacter gummiphilus strain NBRC 109400.";
RL Submitted (JAN-2023) to the EMBL/GenBank/DDBJ databases.
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 -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
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DR EMBL; CP015118; ARN19871.1; -; Genomic_DNA.
DR EMBL; BSPR01000008; GLS95045.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1W6L6B6; -.
DR STRING; 946333.A4W93_08065; -.
DR KEGG; rgu:A4W93_08065; -.
DR OrthoDB; 9803237at2; -.
DR Proteomes; UP000193427; Chromosome.
DR Proteomes; UP001157201; Unassembled WGS sequence.
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 4: Predicted;
KW DNA replication {ECO:0000256|ARBA:ARBA00022705};
KW DNA-directed DNA polymerase {ECO:0000256|ARBA:ARBA00022932,
KW ECO:0000313|EMBL:GLS95045.1};
KW Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695};
KW Reference proteome {ECO:0000313|Proteomes:UP000193427};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 4..71
FT /note="Polymerase/histidinol phosphatase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00481"
SQ SEQUENCE 1167 AA; 129035 MW; F54E5B45792DF0FE CRC64;
MAFVHLRSHT EFSVVDGTLR IDELVDAAAG DGQAALAITD LSNLFGGVKF YKEARKAGVK
PVLGADVWLE PDTAAGEKLP SRLLLLAQNR NGYLNLCEIL SRAWIQDVQQ GRAWVRWESL
AALGSDLIVL SGADLGAVGQ ALLANDTERA KAIATRLSDL FPQRFYIELQ RAGLPGHEPH
VRAAVPLAAE LGLPVVATHP LQFQTPEDFE AHEARTCIAE GETLTNPRRV KKFTRDQHFK
TQAEMEALFA DVPTAIRNTV EIAKRCSLTL VLGKPRLPDF PVPEVEGRLM EPEEYFRYVS
HEGLKERMIH LFPDPAKREA ENPRYVERLD FEINTILKMG FPGYFLIVAD FIIWAKGHGC
PVGPGRGSGA GSLVAYALKI TDLDPLRYNL LFERFLNPER VSMPDFDIDF CQGNRDRVID
YVKDKYGREA VSQIATFGTM AAKAALRDVG RVLGMGYGHV DGVAKLVPAP PGKTVTLKRP
GDKPDPGIIY ARTEAPEIEQ REKNEEEVAE LLALAERVEG MVRNIGMHAG GVLIAPGKIT
DFCPLYMQPG SDSAVSQYDK DDVEAIGLVK FDFLGLATLT ILELAKDYIR ARRPKQENFA
FENIPLNDRA SYQLMSEGKT VAVFQLESSG MQRMLKDAKP SVFEDIIALV ALYRPGPMDL
IPSFCARKHG REEVEYPHPL MKSVLEETYG IMVYQEQVMQ VAQIVGGYSL GGADLLRRAM
GKKKLEEMVA HRATFAEGAG KQGIEEPKAN EIFDLMEKFA GYGFNKSHAA AYALLAYHTA
YLKAHYLAEF TAANMSVALD DTDKLKIFHD DAVKLGLTFE PPNINTCNYR FEPVADKVVR
YGLGAVKGTG QSAVEAIIEA RAEGGPFKSI FDFAARVDRS RINKRTVEAL IKAGAFDLLH
PERSQVVASI GLAFEYADTQ AAHADQGGLF DFDDSHGAST TEPDLVEAKP WSIKERLSLE
KIALGFYLSG HLFDQSGSEV RKFARREIAD LIDTREPQVL AGIVGDLRVI NGQRGRVAIF
KLDDKSEMIE AVANEELLNA NKDLLKDDEL IIVLGKAQPD RFSGGMRLNV QQVWDLPTAR
CRFGKYLRVE VNGSVPPVTE VLRDHPSRRV ETEEGTVTQG LPVRLVLHRE GASGELDLGD
EGRFYPSDAA LERWLEGSHG KSTVVYD
//
