ID   B2KB15_ELUMP            Unreviewed;      1167 AA.
AC   B2KB15;
DT   10-JUN-2008, integrated into UniProtKB/TrEMBL.
DT   10-JUN-2008, sequence version 1.
DT   27-MAR-2024, entry version 91.
DE   RecName: Full=DNA polymerase III subunit alpha {ECO:0000256|ARBA:ARBA00019114};
DE            EC=2.7.7.7 {ECO:0000256|ARBA:ARBA00012417};
GN   OrderedLocusNames=Emin_0212 {ECO:0000313|EMBL:ACC97774.1};
OS   Elusimicrobium minutum (strain Pei191).
OC   Bacteria; Elusimicrobiota; Elusimicrobia; Elusimicrobiales;
OC   Elusimicrobiaceae; Elusimicrobium.
OX   NCBI_TaxID=445932 {ECO:0000313|EMBL:ACC97774.1, ECO:0000313|Proteomes:UP000001029};
RN   [1] {ECO:0000313|EMBL:ACC97774.1, ECO:0000313|Proteomes:UP000001029}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Pei191 {ECO:0000313|EMBL:ACC97774.1,
RC   ECO:0000313|Proteomes:UP000001029};
RX   PubMed=19270133; DOI=10.1128/AEM.02698-08;
RA   Herlemann D.P.R., Geissinger O., Ikeda-Ohtsubo W., Kunin V., Sun H.,
RA   Lapidus A., Hugenholtz P., Brune A.;
RT   "Genomic analysis of 'Elusimicrobium minutum,' the first cultivated
RT   representative of the phylum 'Elusimicrobia' (formerly termite group 1).";
RL   Appl. Environ. Microbiol. 75:2841-2849(2009).
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; CP001055; ACC97774.1; -; Genomic_DNA.
DR   AlphaFoldDB; B2KB15; -.
DR   STRING; 445932.Emin_0212; -.
DR   KEGG; emi:Emin_0212; -.
DR   HOGENOM; CLU_001600_0_0_0; -.
DR   OrthoDB; 9803237at2; -.
DR   Proteomes; UP000001029; Chromosome.
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   Gene3D; 2.40.50.140; Nucleic acid-binding proteins; 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; IPR012340; NA-bd_OB-fold.
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   ECO:0000313|EMBL:ACC97774.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001029};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:ACC97774.1}.
FT   DOMAIN          4..76
FT                   /note="Polymerase/histidinol phosphatase N-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00481"
SQ   SEQUENCE   1167 AA;  130005 MW;  944DCC45D8F6B48F CRC64;
     MEFVHLHNHS EYSLLDGMLR LSEKGPSKFL KQVAADGFKA MAITDHGNMY GAMDFYKNAA
     AAGIKPIIGC EAYITNGSHK NKEKGLDKTF HLTLLAKDYE GYQNLMALIS KAWLDGFYYH
     PRIDKDILAQ HAKGIMALSG CLKGEVSQEL LNGTFAQACE YAKTYESILG KGNYYIELMD
     HGIEEEQIIL PKLIEVSKST GIPVVATNDC HYEKQEDWQA HDIHMCISMG KTLDDPNRLK
     SSTHELYFKS AQEMAELFSY IPEAVSNTLE VAEKCNVVMP KSGFVLPVFD IPPSFSDTDS
     YIKNLCQEGL AKKMSGIIPP NYQERLDYEL GVIGKMGFSS YFLIVADFID YARQNHIPVG
     PGRGSGAGSI VAYSLNITKV DPIKNGLLFE RFLNPDRLSM PDLDIDFSDE GREQVINYVR
     NKYGETNVAQ IITFGTMKAK MAVKDVARVL NIPVSESNRI TKLIPNDLGT TIDSAIETVK
     ELKQEIASNP QTAKLFDFAK KLEGLKRHAG IHAAGIVVTR EEVSKYAPLA RGSKEAITTQ
     YEGGILADDL GLLKIDFLGL RTLTIIDNAV DIIKNMRGID IDIDNIPLDN KKTYELLSSA
     KTLGIFQLES GGMRDLVKRL KPSEFSDISA LVALYRPGPM ESGMLESFVR RKAGQEKITY
     DTPLMEPVLK ETYGTMVYQE QIMELSKLLG GFTPGQADSL RKAMGKKKVD EMEKARVNFV
     NGCAGKKINP KTADKIFEQM SKFAGYGFNK SHSVAYALVS YQTAYLKANY PIEFMCSLLT
     NEIGHNAIGS DDKENKIVTY IEEAKKMGFE TLGPDVNHSK ENFSIEEVNG KEIIRFGLEA
     VKNVGTEAAA SIVSARGDRP YCGFQDLLER IDLKASNKKT IESLIKAGAL DSLIPGKTPN
     SARAVMLAEM EDMLEITAKI KEEKESSICS LFGEDSSAFV SVKKKETKTA PRPLKQEQLL
     EMEKEVLGFY NSGHPLAKYK KHMDKIKSVT IEEINENNIK GAVNILGIIT RVKKRQNKRK
     EDWAQFIIED ETGQMSANAY SRVYAEIAEK IENNAIVYLT GDIKTDEESA RTEIMVSNIE
     SIIPVISRAA AKVTIDIPKG YSETNSRLLN TLLERGKGIT EVYFNIESPD EDKAPFLVRS
     QHKIVLHKAL IDHIENTLGE NSWTFEK
//