GenomeNet

Database: UniProt
Entry: A0A2U1F9S6_9PSEU
LinkDB: A0A2U1F9S6_9PSEU
Original site: A0A2U1F9S6_9PSEU 
ID   A0A2U1F9S6_9PSEU        Unreviewed;      1176 AA.
AC   A0A2U1F9S6;
DT   18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT   18-JUL-2018, sequence version 1.
DT   24-JAN-2024, entry version 19.
DE   RecName: Full=DNA polymerase III subunit alpha {ECO:0000256|ARBA:ARBA00019114};
DE            EC=2.7.7.7 {ECO:0000256|ARBA:ARBA00012417};
GN   ORFNames=C8D89_10761 {ECO:0000313|EMBL:PVZ08899.1};
OS   Actinomycetospora cinnamomea.
OC   Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC   Pseudonocardiaceae; Actinomycetospora.
OX   NCBI_TaxID=663609 {ECO:0000313|EMBL:PVZ08899.1, ECO:0000313|Proteomes:UP000245639};
RN   [1] {ECO:0000313|EMBL:PVZ08899.1, ECO:0000313|Proteomes:UP000245639}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 45771 {ECO:0000313|EMBL:PVZ08899.1,
RC   ECO:0000313|Proteomes:UP000245639};
RA   Goeker M.;
RT   "Genomic Encyclopedia of Type Strains, Phase IV (KMG-IV): sequencing the
RT   most valuable type-strain genomes for metagenomic binning, comparative
RT   biology and taxonomic classification.";
RL   Submitted (APR-2018) 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}.
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:PVZ08899.1}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; QEKW01000007; PVZ08899.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2U1F9S6; -.
DR   OrthoDB; 9803237at2; -.
DR   Proteomes; UP000245639; 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   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   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   Reference proteome {ECO:0000313|Proteomes:UP000245639};
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   1176 AA;  129168 MW;  82ABE5A1BD975976 CRC64;
     MTGDSFVHLH THTEFSMLDG AARLDDLFAE AARMGMPALA MTDHGNTFGA YEFWKKSQAH
     GVKPIIGMEG YLAPGSRHER KRATLGGQVV SDDNPGEMYT HMTLLAENTE GMHNLFRLSS
     LASLEGYYYK PRMDRELLET YGKGIIATTG CPSGEVQRLL QRGDFDGACQ AASDYRDIFG
     EDNFFCELMD HGIEIERRVR DDLYDLKKKL DLPGLATNDL HYTYAKDAKP HEVLLCVQTG
     KTMNDPNRFR FDAQDFYLKS AQEMRAQWDG VFPEACDNTL AVAERVDVEF VEGRDLMPRA
     PVPEGETEAS WLVKEVERGL NQRFGGQVPD GHRKQAAYEI DVICQKGYPG YFLVTADLVQ
     HAKSVGIRVG PGRGSAAGCL IAYALGITDL DPVKHNLIFE RFLNPERKSM PDIDLDFDER
     RRGEMIRYVT EKYGEDRIAQ IITYSTIKAK AAIKDSARVL YGQPGYAVAD RISKAMPPAV
     MGKDIPLSGI FDPGHKRYSE ATEVRALYEA DPQVKEIVDT ARDLEGLKRQ WGVHAAGVIM
     SSTPLIDVIP IQRREADGAI ITQFDMGVCE TLGLLKMDFL GLRNLTVIDD ALHNIELNGK
     PPLDLDHLGL DDTLAYELLA RGDTLGVFQL DGGPMRDLLR RMVPTTFEDI SAVLALYRPG
     PMGANAHNDY ADRKNGRQEI KPIHPELAEP LAEILGETFG LIVYQEQVMA IAQQLAGYSL
     GAADLLRRAM GKKKKEILDK EFVPFSEGMK ANGYSQQAIQ TLWDILVPFS DYAFNRAHTA
     GYGLVSYWTA YLKANYPAEY MAALLTSVRD DKDKAAVYLA ECRKIGITVL PPDVNDSVRD
     FAPVGADIRF GLGAIRNVGT NVVDAIVEAR REKGAYTDFS DFLRKVPQQV CNKKTVESLI
     KAGAFDSLGH PRKGLALVHA EAVDAVMTTK KAEADGQFDL FGSFDGPDEA DTTGMFDVKV
     PEGEWEPKHR LALEREMLGL YVSGHPLNGI EQVLASRADT PITKILEGDV AEGATVTVGG
     ILATVTRRVN KKGEPWASAQ IEDLAGGIEV LFFPRTYAAV SIDVAEDAIV LVKGKVNKRD
     DRVSLFVEDL AVPDLSGGVG GAPVKVVIES ARCTPERVGK LKEVLVAHPG PSEVHLTLLA
     ANGASHVLRL DDGLKVTNSG ALMGDLKALL GPRCLG
//
DBGET integrated database retrieval system