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Database: UniProt
Entry: A0A2T7TG69_9ACTN
LinkDB: A0A2T7TG69_9ACTN
Original site: A0A2T7TG69_9ACTN 
ID   A0A2T7TG69_9ACTN        Unreviewed;      1179 AA.
AC   A0A2T7TG69;
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=Y717_19035 {ECO:0000313|EMBL:PVE14153.1};
OS   Streptomyces scopuliridis RB72.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=1440053 {ECO:0000313|EMBL:PVE14153.1, ECO:0000313|Proteomes:UP000245992};
RN   [1] {ECO:0000313|EMBL:PVE14153.1, ECO:0000313|Proteomes:UP000245992}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RB72 {ECO:0000313|EMBL:PVE14153.1,
RC   ECO:0000313|Proteomes:UP000245992};
RA   Olson J.B.;
RT   "Annotated genome of Streptomyces scopuliridis.";
RL   Submitted (DEC-2013) 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:PVE14153.1}.
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DR   EMBL; AZSP01000004; PVE14153.1; -; Genomic_DNA.
DR   RefSeq; WP_030353530.1; NZ_JOEI01000018.1.
DR   AlphaFoldDB; A0A2T7TG69; -.
DR   STRING; 1440053.GCA_000718095_04527; -.
DR   OrthoDB; 9803237at2; -.
DR   Proteomes; UP000245992; 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:UP000245992};
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   1179 AA;  131078 MW;  DB227C0EE00030E5 CRC64;
     MTKPPFTHLH VHTQYSLLDG AARLGDMFNA CKEMGMSHIA MTDHGNLHGA YDFFHQAKKA
     GVTPIIGIEA YVAPESRRLK RKVQWGQPHQ KRDDVSGSGG YTHKTIWAAN RTGLHNLFRL
     SSDAYKEGWL QKWPRMDKET IAKWSEGLIA STGCPSGELQ TRLRLGQFDE ALKAASEYQD
     IFGKDRYFLE LMDHGIEIER RVRDGLLEVG KKLGIPPLVT NDSHYTYANE ATAHDALLCI
     QTGKNLSDPD RFRFDGTGYY LKSTDEMYAV DLSDAWQEGC ANTRLVAEQI DTEGWFQERN
     LMPKFEVPEG FTEVSWFREE TMRGMARRFP NGIPEDRMRQ VEYEMGIIID MGFPGYFLVV
     ADFIMWAKNN GIAVGPGRGS AAGSIVSYAM GITDLDPIEH GLIFERFLNP ERISMPDVDI
     DFDERRRGEV IRYVTEKYGA DKVAMIGTYG KIKAKNAIKD SARVLGYPYA MGDRLTKAMP
     ADVLGKGIDL NGITDPKHPR YGEAGEIRGM YENEPDVKKV IDTAKGVEGL VRQMGVHAAG
     VIMSSETITD HVPVWVRHTD GVTITQWDYP QCESLGLLKM DFLGLRNLTI MDDAVKMVKS
     NKGVDLDLLS LPLDDPKTYE LLCRGDTLGV FQFDGGPMRS LLRQMQPDNF EDISAVSALY
     RPGPMGMNSH TNYAERKNAR QEITPIHPEL EEPLKEVLGL TYGLIVYQEQ VQKAAQIVAG
     YSLGEADILR RVMGKKKADE LAKNFVLFEA GAKKNGFSDE AIKALWDVLV PFAGYAFNKA
     HSSAYGLVTY WTAYLKANYP AEYMAALLTS VKDDKDKSAV YLNECRRMGI KVLPPNVNES
     LSNFAAQGDD VILFGLTAVR NVGQNVVDSI IRSRKAKGKY ATFPDFLDKV EAVVCNKRTV
     ESLIKAGAFD EMGHTRKGLV AHHEPMIDNV VQVKRKEAEG QFDLFGGMGE EETSEPGFGL
     DVEFSDIEWD KSYLLAQERE MLGLYVSDHP LFGIEHVLSD KSDAAISQLT GGEHADGAVV
     TIGGIISGLQ RKMTKQGNAW AIATVEDLAG SIECMFFPAT YQLVSTQLVE DTVVFVKGRL
     DKREDIPRLV AMELQVPDVS SAGTDAPVTI TIPTVKLTPP MVSRLGEILS HHRGNSEVRI
     KLQGARKTTV LRLDRHRVQP DPALFGDLKV LLGPSCLAG
//
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