ID A0A1F4F642_9PROT Unreviewed; 1147 AA.
AC A0A1F4F642;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE RecName: Full=DNA polymerase III subunit alpha {ECO:0000256|ARBA:ARBA00019114};
DE EC=2.7.7.7 {ECO:0000256|ARBA:ARBA00012417};
GN ORFNames=A3F77_03940 {ECO:0000313|EMBL:OGA68902.1};
OS Betaproteobacteria bacterium RIFCSPLOWO2_12_FULL_67_28.
OC Bacteria; Pseudomonadota; Betaproteobacteria.
OX NCBI_TaxID=1797503 {ECO:0000313|EMBL:OGA68902.1};
RN [1] {ECO:0000313|EMBL:OGA68902.1}
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:OGA68902.1}.
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DR EMBL; MERO01000082; OGA68902.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1F4F642; -.
DR STRING; 1797503.A3F77_03940; -.
DR Proteomes; UP000177406; 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; IPR048472; DNA_pol_IIIA_C.
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; PF20914; DNA_pol_IIIA_C; 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 1147 AA; 126381 MW; 0546F96E66C7FA1D CRC64;
MSDPRFVHLR LHSEYSVTDG IVRIEDVVAR AAADGMPALA LTDNANVFGM IKFYKAARAA
GVKPVLGADC WIQNETDRDK PSRLLLLCAS HAGYLRLSAL LSRAWLSNQH RARAEIAPAW
FSELGSDGLI ALSGAAAGDV GQALLAGNAA AAERLAAAWA ALFPGRYYLE LQRAGFANSE
SLVVHSLALA VKSGIPVVAT HPVQFLARED FRAHEARVCI AEGYLLGDQR RPRRFTPEQY
WKSQDEMAQL FADVPQALAN AVEIARRCNL VMELGKSRLP AFPVPAGFTI DQFLRAEAEK
GLAHRLHQLF PDAARRAEET PRYRERLDFE IRMIVQMGFA GYFLIVADFI NWARINGVPV
GPGRGSGTGS LVAYSLGITD LDPIHYELLF ERFLNPERVS MPDFDIDFCQ DGRDRVIDYV
RNKYGAESVS QIATFGTMAA RAVVRDTGRV LDLGYNFCDQ VAKLIPAQPG QSVTLAEARK
LEPLLAERER NEDDVRELLA LGEKLEGLTR NVGMHAGGVL IAPGRLTDFC PLYAAEGTAN
VISQLDKDDV EAIGLVKFDF LGLTTLTILD WAERYARELG ERDFALDRVP LDDAATYRLI
AAGNTSAVFQ LESRGMRDMV KRAQPDRLED VIALVALFRP GPMDLIPDFI ARKHGKQRVE
YLDRRLEPIL GPTYGIMVYQ EQVMQIAQVI GGYTLGGADL LRRAMGKKNQ EEMDAQRDIF
VAGAERNGLA RGRAMQLFDL MAKFAGYGFN KSHAAAYALL AYQTAYLKAH QLAAFMAANL
SAVMDDTDKV RQLHDDALGN GLRILPPDIN ASGYRFTPVD RQTVRYGLGA VRGTGAAAVA
AMVEARKAGA FSGLFEFCRR VDKRFLNRRA VEALVRAGAF DALQADRARL LASVGRAIEA
AEQAERRKSQ SSLFGEADAA QTEREALLEA VPWDLKQRLV EEKTALGFNI SGHLFSVYEQ
ELAGLPRQLL GQLAPAEHPV LVAGIVVEAR PQMTRRGRMM VVKLEDGSAQ IDVNVYSELL
DRQRERLKAD ALLLVRGRVQ RDMLTGGIRM VAEELLDLAA VRARYAARLR IAMNGQADAQ
RLGELLTPYR ASDGPACPVV VHYENGSASC DVVLGPSWRV RPEERLISEL QAWLAPENVQ
VIYDTPA
//
