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Database: UniProt
Entry: A0A238ZST9_9ACTN
LinkDB: A0A238ZST9_9ACTN
Original site: A0A238ZST9_9ACTN 
ID   A0A238ZST9_9ACTN        Unreviewed;      1185 AA.
AC   A0A238ZST9;
DT   25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT   25-OCT-2017, sequence version 1.
DT   24-JAN-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=SAMN05216252_101538 {ECO:0000313|EMBL:SNR86487.1};
OS   Actinacidiphila glaucinigra.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Actinacidiphila.
OX   NCBI_TaxID=235986 {ECO:0000313|EMBL:SNR86487.1, ECO:0000313|Proteomes:UP000198280};
RN   [1] {ECO:0000313|EMBL:SNR86487.1, ECO:0000313|Proteomes:UP000198280}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CGMCC 4.1858 {ECO:0000313|EMBL:SNR86487.1,
RC   ECO:0000313|Proteomes:UP000198280};
RA   Kim H.J., Triplett B.A.;
RL   Submitted (JUN-2017) 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; FZOF01000001; SNR86487.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A238ZST9; -.
DR   Proteomes; UP000198280; 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; 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:UP000198280};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          6..73
FT                   /note="Polymerase/histidinol phosphatase N-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00481"
SQ   SEQUENCE   1185 AA;  131039 MW;  E69AEECD4925DCB2 CRC64;
     MTTPFTHLHV HTQYSLLDGA ARLKDMFKAC GEMGMTHIAM TDHGNLHGAY DFFHQAKGAG
     ITPIIGIEAY VAPESRRNKR KVTWGQPHQK RDDVSASGSY LHKTIWAANA TGLHNLFRLS
     SDAYAEGWLT KYPRMDKETI AQWSEGLMAS TGCPSGEVQT RLRLGQFDEA VKAAAEYQDI
     FGKERYFLEL MDHGIEIERR VRDGLLEIGK KLGIPPVVTN DSHYTYASEA DAHDALLCIQ
     TGKNVSDPDR FRFDGTGYYL KTTDEMLGID SSDAWQEGCR NTTLLVAQQV DTDGMFQARN
     LMPRFEVPEG YTEVTWFREE TMSGMRRRYP AGIPDDRMKQ VEYEMDTIIQ MGFPGYFLVV
     ADFIMWAKNN GIAVGPGRGS AAGSIVAYAM GITDLDPIDH GLIFERFLNP ERISMPDVDI
     DFDERRRAEV IRYVTEKYGA DKVAMIGTYG TIKAKNAIKD SARVLGYPYA VGDRLTKAMP
     ADVLGKGIPL SGITDSAHPR YSEAGEIRSM YENEPDAKKV IDLARGVEGL VRQMGVHAAG
     VIMSSEPIVD HAPVWVRHSD GVTITQWDYP SCESLGLLKM DFLGLRNLTI MDDAVKLVKA
     NKGVDIELLA LPFDDPKTFE LLGRGDTLGV FQFDGGPMRS LLRMMKPDNF EDISAVSALY
     RPGPMGMNSH INYALRKNKQ QEITPIHPAL EAPLKEVLDV TYGLIVYQEQ VQKAAQIIAG
     YSLGEADILR RVMGKKKPEE LAKNFTIFQE GARKNGYSDE SIQALWDVLV PFAGYAFNKA
     HSAAYGLVSY WTAYLKANYP AEYMAALLTS VRDDKDKSAI YLNECRRMGI RVLPPNVNES
     DANFTAQGDD VILFGLTAVR NVGQNVVDSI IRCRKSKGKY TSFPDFLDKV EAVVCNKRTV
     ESLIKAGAYD EMGHTRKGLT EHYEPMIDNV VAVKRKEAEG QFDLFGGMGD ETAGDEPGFG
     LDVTFSDVEW DKTYLLAQER EMLGLYVSDH PLFGIEHVLN DKADASVSAL AGDYSDGSIV
     TIGGIISGLQ RKMTKQGNAW AIATVEDLGG SIDCMFFPAT YQLISTQLVE DAVVFVKGRL
     DKREDIPRLV AMELMVPDLT DAGTNAPVTI SIPTVKVTPP LVARLGEVLA SHKGSTEVRV
     RLQGARKTTV LRLDRHRVTA DPALFGDLKA LLGPSCLATA QQQAG
//
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