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Database: UniProt
Entry: A0A0N0TV74_9ACTN
LinkDB: A0A0N0TV74_9ACTN
Original site: A0A0N0TV74_9ACTN 
ID   A0A0N0TV74_9ACTN        Unreviewed;      1163 AA.
AC   A0A0N0TV74;
DT   09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT   09-DEC-2015, sequence version 1.
DT   24-JAN-2024, entry version 26.
DE   RecName: Full=DNA polymerase III subunit alpha {ECO:0000256|ARBA:ARBA00019114};
DE            EC=2.7.7.7 {ECO:0000256|ARBA:ARBA00012417};
GN   ORFNames=ADL06_04310 {ECO:0000313|EMBL:KOX36769.1};
OS   Streptomyces sp. NRRL F-6491.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=1519495 {ECO:0000313|EMBL:KOX36769.1, ECO:0000313|Proteomes:UP000037743};
RN   [1] {ECO:0000313|EMBL:KOX36769.1, ECO:0000313|Proteomes:UP000037743}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NRRL F-6491 {ECO:0000313|EMBL:KOX36769.1,
RC   ECO:0000313|Proteomes:UP000037743};
RA   Noorani M.;
RL   Submitted (JUL-2015) 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:KOX36769.1}.
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DR   EMBL; LGEE01000022; KOX36769.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0N0TV74; -.
DR   PATRIC; fig|1519495.3.peg.909; -.
DR   Proteomes; UP000037743; 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   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          1..58
FT                   /note="Polymerase/histidinol phosphatase N-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00481"
FT   REGION          63..82
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1163 AA;  129051 MW;  3E733EC46E89D928 CRC64;
     MLDGAARLKD MFDACNEMGM THIAMSDHGN LHGAYDFFHT AKKAGVTPII GIEAYVAPES
     RRNKRKIQWG QPHQKRDDVS GSGGYTHKTI WAANATGLHN LFRLSSDAYA EGWLQKWPRM
     DKETISQWSE GLIASTGCPS GELQTRLRLG QFDEALKAAS EYQDIFGKDR YFLELMDHGI
     EIEHRVRDGL LEIGKKLGIP PLVTNDSHYT YAHEATAHDA LLCIQTGKNL SDPDRFRFDG
     TGYYLKSTDE MYAVDSSDAW QEGCRNTLLV AEQIDTSGMF EAKNLMPRFD IPDGYTEVTW
     FREETMRGMA RRFPGGIPED RMKQVEYEMD TIISMGFPGY FLVVADFIMW AKKQGIAVGP
     GRGSAAGSIV AYAMGITDLD PIPHGLIFER FLNPERISMP DVDIDFDERR RVEVIRYVTE
     KYGSDKVAMI GTYGKIKAKN AIKDSARVLG YPYAMGDRLT KAMPADVLGK GIDLDGITNP
     SHPRYSEAGE IRAMYENEPD VKKVIDTARG VEGLVRQMGV HAAGVIMSSE PIVDHAPIWV
     RHTDGVTITQ WDYPQCESLG LLKMDFLGLR NLTIMDDAVK MVKANKGVDL DLLALPLDDP
     KTFELLQRGD TLGVFQFDGG PMRSLLRLMK PDNFEDISAV SALYRPGPMG MNSHTNYALR
     KNKQQEITPI HPELEKPLEE VLAVTYGLIV YQEQVQKAAQ IIAGYSLGEA DILRRVMGKK
     KPEELAKNFT IFQAGARKNG YSDEAIQSLW DVLVPFAGYA FNKAHSAAYG LVSYWTAYLK
     ANHPAEYMAG LLTSVKDDKD KSAVYLNECR RMGIKVLPPN VNESQSNFAA QGDDVILFGL
     TAVRNVGTNV VESIIKTRKS KGKYSSFPDF LDKVEAVVCN KRTVESLIKA GAFDEMGHTR
     KGLVAHHEPM IDNVVAVKRK EAEGQFDLFG GMGEETNDEP GFGLDVEFSD VEWEKSYLLA
     QEREMLGLYV SDHPLFGIEH VLSDKTDAAI SQLTGGEHSD GAVVTIGGII SGLQRKMTKQ
     GNAWAIATVE DLAGSIECMF FPATYQLVST QLVEDTVVFV KGRLDKREDV PRLVAMELQV
     PDLSNAGTNA PVILTIPTVK VTPPMVSRLG EILKHHKGNT EVRIRLQGPR KTTVLRLDRH
     RVTADPALFG DLKVLLGPSC LAG
//
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