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Database: UniProt
Entry: A0A495JEL7_9ACTN
LinkDB: A0A495JEL7_9ACTN
Original site: A0A495JEL7_9ACTN 
ID   A0A495JEL7_9ACTN        Unreviewed;      1177 AA.
AC   A0A495JEL7;
DT   05-JUN-2019, integrated into UniProtKB/TrEMBL.
DT   05-JUN-2019, sequence version 1.
DT   27-MAR-2024, entry version 15.
DE   RecName: Full=DNA polymerase III subunit alpha {ECO:0000256|ARBA:ARBA00019114};
DE            EC=2.7.7.7 {ECO:0000256|ARBA:ARBA00012417};
GN   ORFNames=BDK92_1444 {ECO:0000313|EMBL:RKR87171.1};
OS   Micromonospora pisi.
OC   Bacteria; Actinomycetota; Actinomycetes; Micromonosporales;
OC   Micromonosporaceae; Micromonospora.
OX   NCBI_TaxID=589240 {ECO:0000313|EMBL:RKR87171.1, ECO:0000313|Proteomes:UP000277671};
RN   [1] {ECO:0000313|EMBL:RKR87171.1, ECO:0000313|Proteomes:UP000277671}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 45175 {ECO:0000313|EMBL:RKR87171.1,
RC   ECO:0000313|Proteomes:UP000277671};
RA   Klenk H.-P.;
RT   "Sequencing the genomes of 1000 actinobacteria strains.";
RL   Submitted (OCT-2018) 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:RKR87171.1}.
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DR   EMBL; RBKT01000001; RKR87171.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A495JEL7; -.
DR   OrthoDB; 9803237at2; -.
DR   Proteomes; UP000277671; 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:UP000277671};
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;  129459 MW;  509785377C448CEB CRC64;
     MSDSFVHLHT HTEYSMLDGA ARLKELFAET NRLGMPALAM TDHGNLYGAY DFHKQATAAG
     VKPIIGLEAY LTPGTDRRDR TRVRWADGGE NDVSGGGAYT HMTMLAQDAD GLRNLFALGS
     RSSLEGYFYK PRADRELLNQ YGKGIIATTG CPSGEVQTWL RIGNFEKACE SAAEFRDIFG
     ADNFYLELMD HGLDIETRIR QDLIRLGKTL NLKPIATNDL HYTHAADADA HEVLLCVQSG
     STMADPKRFR FDARDFYLKS PAEMRAIWDA EVPGACDNTL EIAEKIGDYS VMFASRNLMP
     QFPVPEGETE ETFLRKEVMR GLARRFPNGV PEDRQRQAEY ELDVILKMGF PGYFLVTADL
     IAYAKREGIR VGPGRGSAAG ALIAYALGIT ELDPMQHGLL FERFLNPDRI SMPDIDMDFD
     ERRRGDMIRY ATEKYGEARV AQIITYGTIK AKAAIKDAAR VLGYPFAVGD RITKAMPPAV
     MGKDIPLGGI FDKNHPRYQE AAEFRSLYDS DAEVAKIVDT AKGLEGLKRQ WGVHAAGVIL
     SRDPLLDVLP IHKREQDGSI ITQWDMGACE TIGLLKMDFL GLRNLTIMDD CLESIKENRG
     IDLVLEDLPL DDAATYALLG RGDTLGVFQF DGGPMRALLR SMAPDNFEDI SAVGALYRPG
     PMGANAHNEY ADRKNKRKPV VPIHPELAES LAEILGDTYG LIVYQEQVMA IAQKVAGYTL
     GAADLLRRAM GKKKKEILDK EFKPFAAGMK ANGYSDEAIK TLWDILVPFS DYAFNKAHSA
     AYGVVSYWTA YLKANYPAEY MGALLTSVGD DKDKSAVYLA ECRRMGIKVL PPDVNESNAR
     FAAVGEDIRF GLAAVRNVGA NVVESIRRTR KEKGRFTDFY DYLRKVDAVA CNKKTIESLI
     KAGAFDSLGH TRKGLLAVHT DAIDSFLDVK KKEATGQYDL FGTAFESEAS AVPGISVTPT
     IPTTEWDKTD LLTFEREMLG LYVSDHPLFG VEHVLAAAAD MSIASLAEEG NVADGQIVNL
     AGILSGVQRR ITKQGRAWAS ATLEDLGGAV EVLFFPNTYE VVGQYIAEDA IVVIKGRVDR
     RDDQPRLMAM DMSMPEITAA DEVKPVVLAL PPSRCTPPLV ERLREVLTSH PGSAEVHVRL
     VNGSRGTLLR LGRMRVAPST ALMADLKALL GPSAVAG
//
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