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Database: UniProt
Entry: A0A1C5BX94_9ACTN
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ID   A0A1C5BX94_9ACTN        Unreviewed;      1179 AA.
AC   A0A1C5BX94;
DT   02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT   02-NOV-2016, sequence version 1.
DT   24-JAN-2024, entry version 25.
DE   RecName: Full=DNA polymerase III subunit alpha {ECO:0000256|ARBA:ARBA00019114};
DE            EC=2.7.7.7 {ECO:0000256|ARBA:ARBA00012417};
GN   ORFNames=GA0115254_108627 {ECO:0000313|EMBL:SCF62938.1};
OS   Streptomyces sp. Ncost-T10-10d.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=1839774 {ECO:0000313|EMBL:SCF62938.1, ECO:0000313|Proteomes:UP000198750};
RN   [1] {ECO:0000313|Proteomes:UP000198750}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Ncost-T10-10d {ECO:0000313|Proteomes:UP000198750};
RA   Varghese N., Submissions Spin;
RL   Submitted (JUN-2016) 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; FMDF01000071; SCF62938.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1C5BX94; -.
DR   OrthoDB; 9803237at2; -.
DR   Proteomes; UP000198750; 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:UP000198750};
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;  130843 MW;  7EFFC0FD49D5E1FE CRC64;
     MTKPPFTHLH VHTQYSLLDG AARLKDMFAA CNEMGMSHIA MTDHGNLHGA YDFFHSAQKA
     GVTPIIGIEA YVAPESRKHK RKIQWGQPHQ KRDDVSGSGG YTHKTIWASN ATGLHNLFRL
     SSDAYAEGWL QKWPRMDKET IAQWSEGLIA STGCPSGEVQ TRLRLGQFDE AVQAASDYKD
     IFGEGKYFLE LMDHGIEIER RVRDGLLEIG KKLNIPPLVT NDSHYTYAHE ATAHDALLCI
     QTGKNLSDPD RFRFDGTGYY LKTTDEMYAV DSSDAWQEGC ANTLLVAQQI DTGGMFEKRD
     LMPKFEIPDG FTEITWFQEE VRRGMERRFP GGVPDDRQKQ VEYEMDIIIQ MGFPGYFLVV
     ADFIMWAKNN GIAVGPGRGS AAGSIVAYAM GITDLDPIEH GLIFERFLNP ERVSMPDVDI
     DFDERRRVEV IRYVTEKYGA DKVAMIGTYG KIKAKNAIKD SARVLGYPYA MGDRLTKAMP
     ADVLGKGIDL NGITDPKHPR YSEAGEIRGM YENEPDVKKV IDTAKGVEGL VRQMGVHAAG
     VIMSSEPIVD HAPIWVRHTD GVTITQWDYP QCESLGLLKM DFLGLRNLTI MDDAVKMVES
     NKGVKLDLLG LPLDDPKTYE MLCRGDTLGV FQFDGGPMRS LLRQMQPDNF EDISAVSALY
     RPGPMGMNSH TNYAERKNGR QEITPIHPEL EEPLKEVLGL TYGLIVYQEQ VQKAAQIVAG
     YSLGEADILR RVMGKKKPEE LAKNFVLFEA GAKEKGFSDA AIKALWDVLV PFAGYAFNKA
     HSSAYGLVTY WTAYLKANYP AEYMAALLTS VKDDKDKSAV YLNECRRMGI KVLPPNVNES
     LSNFAAQGDD VILFGLTAVR NVGQNVVDSI IRCRKAKGKY SSFPDFLDKV EAVVCNKRTV
     ESLIKAGAFD EMGHTRKGLV AHHEPMIDNV VQVKRKEAEG QFDLFGGMGE EESDEPGFGL
     DVEFSDIEWE KSYLLAQERE MLGLYVSDHP LFGLEHVLSD KADSSISQLT GGEHADGAIV
     TVGGIISGLQ RKMTKQGNAW AIATVEDLAG SIECMFFPAT YQLVSTQLVE DTVVFVKGRL
     DKREDVPRLV AMEMQVPDIS SAGTNAPVVL TIPTVKITPP MVSRLGEVLS NHRGDTEVRI
     KLQGPRKTTV LRLDRHRVKP DPALFGDLKV LLGPSCLAG
//
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