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Database: UniProt
Entry: A0A1G2SBN4_9BACT
LinkDB: A0A1G2SBN4_9BACT
Original site: A0A1G2SBN4_9BACT 
ID   A0A1G2SBN4_9BACT        Unreviewed;      1067 AA.
AC   A0A1G2SBN4;
DT   15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT   15-FEB-2017, sequence version 1.
DT   13-SEP-2023, entry version 16.
DE   RecName: Full=DNA polymerase III subunit alpha {ECO:0000256|ARBA:ARBA00019114};
DE            EC=2.7.7.7 {ECO:0000256|ARBA:ARBA00012417};
GN   ORFNames=A3B07_02355 {ECO:0000313|EMBL:OHA82443.1};
OS   Candidatus Yonathbacteria bacterium RIFCSPLOWO2_01_FULL_43_27.
OC   Bacteria; Candidatus Yonathbacteria.
OX   NCBI_TaxID=1802726 {ECO:0000313|EMBL:OHA82443.1, ECO:0000313|Proteomes:UP000178817};
RN   [1] {ECO:0000313|EMBL:OHA82443.1, ECO:0000313|Proteomes:UP000178817}
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:OHA82443.1}.
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DR   EMBL; MHUV01000006; OHA82443.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1G2SBN4; -.
DR   STRING; 1802726.A3B07_02355; -.
DR   Proteomes; UP000178817; 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; cd12113; PHP_PolIIIA_DnaE3; 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   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          11..78
FT                   /note="Polymerase/histidinol phosphatase N-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00481"
SQ   SEQUENCE   1067 AA;  119869 MW;  EF81DB0FF552FFCF CRC64;
     MSTPSEQKSF IHLHTHSHYS LLDGLSKVEE MVALAKEYGM NAVGLTDHGN MYGAIDFYKT
     CKKKGIKPII GVEAYMTPGS RHDKRPGIDT ERFHLTLLAK NEAGYKNLIR LVTISNLEGF
     YYKPRIDKEV LRKYSNDLIC LSGCFGSEFS RAVRREDLEE AEKIAREHQE IFGAENYFLE
     IMHHPGIEDF DKTRDHIIAL SKKLDIPLVA TQDSHYLHHE DQRAHETLLA IQTNGDLKDE
     NRFSMAVDDF SFINTETALE YFKETPEAVW NTQKIADMCN IELTLGSWVF PDLKIPEGTD
     YNSELKRLVY EGITTRGLDA NDSNVIDRIE YELKVIRDKG YAPYFLVVGD LLRFSRENNI
     LTNIRGSVAG SITTYLLGIT NVNPLEYNLP FERFLNPERP SAPDIDMDYA DNRRDEVISY
     ARQKYGSENV AQIGTFGTMM ARGAVRDVAR ALGHPYGIGD KISRLIPEGS QGFPMTIDTA
     LSTVPELADL YKNDASTTEI IDLAKKLEGC VRHISVHAAG VVIGPKPLYE FTPTQLDPKG
     GKIITQYDMH AVEDAGLLKF DFLGIRNLSI LGDAIRLVKE RHDVHIDLDH IPLDDPRTFA
     MLARGETMGL FQLNGAGMTR YLKELRPTTI HDINAMVALY RPGPMESIPE YIKRKYNPST
     ITYLDPRLKD ILAMSYGVIT YQDDVMMIAI HLAGYSWLDA DKLRKAMGKK IPAEMQAQKE
     KLLKGFTEYG KLSKKVTEEL WALIEPFAAY GFNKAHAASY GRLAYQTAFM KANYPVEYMT
     AILTAESGDT EKIAEIISES KRMSIPILPP DVNASFGGFT IVTKDDKEEI RFGLYTIKNL
     GTDISDAVIA EREANGHYST LANFLERIRH KNLNKKSYEA LVMSGAMDGL GERGVMLANT
     EEALAYNRAQ GEEMSGQASL FGQMTDTSTV PSLRLKSAPP AAKKEMLTWE KELLGLFVSG
     HPLDAHREKL EAIGTTVEKV KTLRDGNVAV AGGIVEDIRS ILTKKGDKMA FVKLTDYSGT
     LELVLFPEVF FTHKEFFETP DRCIKVKGKV SERNGEKSLI VERVKEL
//
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