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
//