ID A0A1F4FA45_9PROT Unreviewed; 1145 AA.
AC A0A1F4FA45;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE RecName: Full=DNA polymerase III subunit alpha {ECO:0000256|ARBA:ARBA00019114};
DE EC=2.7.7.7 {ECO:0000256|ARBA:ARBA00012417};
GN ORFNames=A3G83_06295 {ECO:0000313|EMBL:OGA70352.1};
OS Betaproteobacteria bacterium RIFCSPLOWO2_12_FULL_68_20.
OC Bacteria; Pseudomonadota; Betaproteobacteria.
OX NCBI_TaxID=1797505 {ECO:0000313|EMBL:OGA70352.1, ECO:0000313|Proteomes:UP000178578};
RN [1] {ECO:0000313|EMBL:OGA70352.1, ECO:0000313|Proteomes:UP000178578}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=27774985; DOI=10.1038/ncomms13219;
RA Anantharaman K., Brown C.T., Hug L.A., Sharon I., Castelle C.J.,
RA Probst A.J., Thomas B.C., Singh A., Wilkins M.J., Karaoz U., Brodie E.L.,
RA Williams K.H., Hubbard S.S., Banfield J.F.;
RT "Thousands of microbial genomes shed light on interconnected biogeochemical
RT processes in an aquifer system.";
RL Nat. Commun. 7:13219-13219(2016).
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}.
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:OGA70352.1}.
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DR EMBL; MERQ01000014; OGA70352.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1F4FA45; -.
DR STRING; 1797505.A3G83_06295; -.
DR Proteomes; UP000178578; 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 Gene3D; 2.40.50.140; Nucleic acid-binding proteins; 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; IPR012340; NA-bd_OB-fold.
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 4: Predicted;
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 7..74
FT /note="Polymerase/histidinol phosphatase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00481"
SQ SEQUENCE 1145 AA; 126819 MW; DBF9FD6D7FBB61E5 CRC64;
MAAPRFVHLR MRSEYSVIDG IVRIEDAVKR AASDGMPALA LTDAANLFGM VKFYQAARAG
GVKPLLGADC WLQNESDRDK PFRVLLLCAS RAGYLRLCEL LSRAWLRNQH RDRAEIARGW
LAEGGTEGLI ALSGAASGDV GQALAARNPA AERIARGWAE LFPGRYYLEL QRAGFAHGDA
LVAHTVALAA RLGLPVVATH PVQFLGADDF RAHEARVCIA QGYILADQRR PKAFTPEQYF
KSQEEMARLF ADIPQALENS VAIARRCNLE IELGKSRLPA FPTPSGVPLE VFLRQQTETG
LEARLAKLYP DAEERASRSA SYRERLDFEI RIIIKMGFAG YFLIVADFIN WARSNGVPVG
PGRGSGAGSL VAYSLGITDL DPIRYDLLFE RFLNPERVSM PDFDIDFCQD GRDRVIEYVR
RKYGEENVSQ IATFGTMAAR AVVRDVGRVL DLGYNFCDQL AKLIPVQPGR LITLEMARGM
EPLLAERERK EDEVRELLAL AGKLEGLVRN VGMHAGGVLI APGKLTDYCP LYAAEGTAHV
ISQLDKDDVE AVGLVKFDFL GLTTLTILDW AERHVRALGE AEFSLERIPL DDPRTYALLS
AGNTTAVFQL ESRGMRDLIR RARPDRFEDV IALVALFRPG PMELIPEFVE RKHGKRVDYL
DPRLEPILAP TYGIMVYQEQ VMQIARVIGG YTLGAADLLR RAMGKKLPEE MAQQRDVFVT
GARHNGLSRA KATQLFDLME KFAGYGFNRS HAAAYAVLAY QTAYMKAHHA AAFMAANLSA
VMDDTDKVRQ FHEDAAANGL RILPPDVNAS EHRFVPVDRV TIRYGLGAVR GTGESAVNAV
IEARRQAPFT GLFDFCLRVD KRLVNRRAVE ALVRAGAFDP IDANRARLLA SVGRALEAAE
QAGRQASQSS LFGEAEAPRG GERAHVEAQP WDLKRQLTEE KVALGFYLSG HLFSVYEREL
QGFPRTQLVR LAPAEHRVWM AGVVASARTQ MTRRGRMMVV MLDDGTAQLE LSVFSELFEK
HRDRLKEDAL LVVQGKVQRD EYSGGLRVTA EDLLDLDALR GRYAAGLRIA VNGQGDAKRL
REVLMPYRTT GDAGCQVLVR YENGAATCEV ALGDAWRVRP DGRLIDELSA WLAPDRVQVI
YANGS
//
