ID   A0A1C5JZ53_9ACTN        Unreviewed;      1177 AA.
AC   A0A1C5JZ53;
DT   02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT   02-NOV-2016, sequence version 1.
DT   27-MAR-2024, entry version 27.
DE   RecName: Full=DNA polymerase III subunit alpha {ECO:0000256|ARBA:ARBA00019114};
DE            EC=2.7.7.7 {ECO:0000256|ARBA:ARBA00012417};
GN   ORFNames=GA0070613_5870 {ECO:0000313|EMBL:SCG75874.1};
OS   Micromonospora inositola.
OC   Bacteria; Actinomycetota; Actinomycetes; Micromonosporales;
OC   Micromonosporaceae; Micromonospora.
OX   NCBI_TaxID=47865 {ECO:0000313|EMBL:SCG75874.1, ECO:0000313|Proteomes:UP000198221};
RN   [1] {ECO:0000313|EMBL:SCG75874.1, ECO:0000313|Proteomes:UP000198221}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 43819 {ECO:0000313|EMBL:SCG75874.1,
RC   ECO:0000313|Proteomes:UP000198221};
RA   Kjaerup R.B., Dalgaard T.S., Juul-Madsen H.R.;
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; LT607754; SCG75874.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1C5JZ53; -.
DR   OrthoDB; 9803237at2; -.
DR   Proteomes; UP000198221; Chromosome i.
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:UP000198221};
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   1177 AA;  129285 MW;  C8F111C3D60A9B2C CRC64;
     MGDSFAHLHV HTEYSMLDGA ARLKDLFAEA NRLGMPAVAI TDHGNMHGAN DFYKQAMAAG
     ITPILGVEAY VAPESRYHKA RVKWGRPEQK SDDISGNGAI THKTMWARNA TGLKNLFTLN
     SRASMEGHYV KWPRMDMELI AEHAEGIMAT TGCPSGAVQT RLRLGQFDEA LKVAASYQDI
     FGKENYFLEI MDHGLDIERR VRDGLTEIAR KLDIPPVVTN DSHYTHEAQA TAHDVLLCVQ
     TGSNIDDPNR FRFEGGGYFI KSAEQMRAVD SSELWQQGCR NTLLVAEKVD PAGMFEFHNL
     MPRFPVPEGE TEESWFRKET HRGLARRFPN GIPEGHVVQA EYELGIIIQM GFPSYFLVVA
     DFIQWAKSQG IAVGPGRGSA AGSLVAYALG ITDLDPIPHG LIFERFLNPE RVSMPDVDID
     FDERRRGEVI KYVTDKWGED KVAQIATFGT IKAKAAIKDS ARVLGYPYAV GDRITKAMPP
     AVMGKDIPLT GIFDPKHARY AEAGEIRGLY ESDPDVKKVI DTARGIEGLI RQTGVHAAGV
     IMSAEPIIEH IPLMRRDADG AIITQFDYPT CESLGLLKMD FLGLRNLTII DDALKNIELN
     HGRKVDLLTL PLDDKPTYEL LARGDTLGVF QLDGGPMRSL LRLMKPDNFE DISAVLALYR
     PGPMGANSHT NYALRKNGQQ DITPIHPELA EPLEEILGPT YGLIVYQEQV QRAAQKLAGY
     SLGQADLLRR AMGKKKKEVL DKEFIPFRDG MRNNGYSDEA IQTLWDILVP FADYAFNKAH
     TAGYGLVSYW TGYLKANYPA EYMAGLLTSV GDDKDKMALY LSECRRMGIQ VLPPDVNTSA
     GPFTPVGRDI RFGLAAIRNV GANVVASIMR CREEKGEYAD FYDFLSKVDA VVCNKKTIES
     LIKAGAFDSM GHPRKGLLAV HADAIDAYAD VKRKEAVGQY DLFGAGFGEA DTGGSTTVMP
     TIGEGEWDKR DKLAFEREML GLYVSDHPLF GLEHVLGAAA DTTIAALAEE GGVPDGAVVT
     LAGILSGVQR RVTKQGRAWA SATLEDLAGG VETLFFPNTY EVIGQYIAED AIVVVKGRVD
     RRDDTPRIMA MDMSMPDISS NPASKPVTLT IPVHRCTPPL VERLKETLVL HPGDTEVHVK
     LLNGGKVTTL RLGPFRVAAT TALMGDLKSV LGPTNVS
//