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Database: UniProt
Entry: A0A2N3Y8Z4_SACSN
LinkDB: A0A2N3Y8Z4_SACSN
Original site: A0A2N3Y8Z4_SACSN 
ID   A0A2N3Y8Z4_SACSN        Unreviewed;      1194 AA.
AC   A0A2N3Y8Z4;
DT   25-APR-2018, integrated into UniProtKB/TrEMBL.
DT   25-APR-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=A8926_7561 {ECO:0000313|EMBL:PKW19394.1};
OS   Saccharopolyspora spinosa.
OC   Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC   Pseudonocardiaceae; Saccharopolyspora.
OX   NCBI_TaxID=60894 {ECO:0000313|EMBL:PKW19394.1, ECO:0000313|Proteomes:UP000233786};
RN   [1] {ECO:0000313|EMBL:PKW19394.1, ECO:0000313|Proteomes:UP000233786}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 44228 {ECO:0000313|EMBL:PKW19394.1,
RC   ECO:0000313|Proteomes:UP000233786};
RA   Klenk H.-P.;
RT   "Sequencing the genomes of 1000 Actinobacteria strains.";
RL   Submitted (DEC-2017) 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:PKW19394.1}.
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DR   EMBL; PJNB01000001; PKW19394.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2N3Y8Z4; -.
DR   OrthoDB; 9803237at2; -.
DR   Proteomes; UP000233786; 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          7..74
FT                   /note="Polymerase/histidinol phosphatase N-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00481"
SQ   SEQUENCE   1194 AA;  131646 MW;  FFB5F1D3D88B313A CRC64;
     MPVDPFVHLH VHTEYSMLDG AAKVGALFAE AERLGMPAVG MTDHGNMFGA DEFYQQACRA
     GIKPIIGIEA YLAPTSRFHK KPVFWGEAKQ RGTDEFGEGG DVSGAGAYTH MTMLARNATG
     LRNLFTLSSR ASFEGYYRKP RMDRELISEF SEGIIATTGC PSGEVQTRLR LRQFDEALQA
     AADYRDIFGA ENFFLELMDH GLPIERSVRQ GLLKISRELG LKPLATNDSH YVTVDQAESH
     GALLCVQSGK TLSDESRFKF DGDGYYLKSA GEMREYWDQE VPGAADSTLL VAEMVESYKD
     VWSFQDRMPR VTDGSGRSER ELLEAEVRQY LPTRYPDGAS EECLERIKVE LDVLDTKGYC
     AYFLVVGDLT RWAKSQGIHV GPGRGSAAGS LLAYILHITN LDPLEHGLIF ERFLNPERDS
     PPDIDLDFDD RRRDEVLQYA INKYGRDKVA QVITFGKIKT KAAIKDSARV HHGQPGFAIA
     DKISKALPPP IAAKDIPLSG IVDPQHERYA EAAEVRSLIE TDPAVSQIFD TARGLEGLIR
     NAGVHACAVI LSSQPLLGTV PLWARDDGSI ITGWDYPSCE AIGLLKMDFL GLSNLTILGD
     ALTMVKENHD RDIDLSNLGL DDKTTYEMLA RGESLGVFQF EGGGMRELLK RLQPTEFGDL
     VAANALYRPG PMDVNAHLDY ADRKNGRKAI EPIHPDLEDD LRDILDETYG LIVYQEQIMA
     IAQKVAGYSL GRADILRRAM GKKKKSVLDQ EFEGFQAGMR ANGYRDEAIT KLWETVLPFA
     GYAFNKSHAA GYALVAYWTA YLKANYPAEY MAGLLTSNGD NKDKMAVYLA ECRRMGVKVL
     SPDVNDSRDT FAAVGSDIRF GMSAIRNVGS NVVASIVTTR KEKGRYTSFT DFLDKSEILA
     CNKRVIESLI KAGAFDSLGH TRMSLVQHHE AAVDAVIGLK RQQAMGQFDL FGADTSEDSA
     DASPLAHLHF THEEWPRKQL LSYEREMLGL YVSAHPLDGA ERLLAPYQDT GIADLVGGER
     EFGNGKEQLK IAGMISGIQR RINKNGHPWA IVTLEDLDAS VEVLFFPKSY EMFADCLMED
     TALAVKGRIN EREGTISVFA SDAVPVDISA AETDPGTDPA FVIKVPVGRV NQSLVAELKR
     TLRAHTGTTP VQLKLQSPRG TTRLALSSDY FVSTENGLQG ELKGLLGAGC FEAY
//
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