ID   A0A2L2BQN1_9MICO        Unreviewed;      1191 AA.
AC   A0A2L2BQN1;
DT   25-APR-2018, integrated into UniProtKB/TrEMBL.
DT   25-APR-2018, sequence version 1.
DT   24-JAN-2024, entry version 23.
DE   RecName: Full=DNA polymerase III subunit alpha {ECO:0000256|ARBA:ARBA00019114};
DE            EC=2.7.7.7 {ECO:0000256|ARBA:ARBA00012417};
GN   ORFNames=C3B54_11990 {ECO:0000313|EMBL:AVG23958.1};
OS   Pontimonas salivibrio.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC   Pontimonas.
OX   NCBI_TaxID=1159327 {ECO:0000313|EMBL:AVG23958.1, ECO:0000313|Proteomes:UP000243077};
RN   [1] {ECO:0000313|EMBL:AVG23958.1, ECO:0000313|Proteomes:UP000243077}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CL-TW6 {ECO:0000313|EMBL:AVG23958.1,
RC   ECO:0000313|Proteomes:UP000243077};
RA   Cho B.C., Hardies S.C., Jang G.I., Hwang C.Y.;
RT   "Complete genome of the streamlined marine actinobacterium Pontimonas
RT   salivibrio CL-TW6 adapted to coastal planktonic lifestype.";
RL   Submitted (FEB-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}.
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DR   EMBL; CP026923; AVG23958.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2L2BQN1; -.
DR   KEGG; psai:C3B54_11990; -.
DR   OrthoDB; 9803237at2; -.
DR   Proteomes; UP000243077; 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:AVG23958.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000243077};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:AVG23958.1}.
FT   DOMAIN          6..73
FT                   /note="Polymerase/histidinol phosphatase N-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00481"
SQ   SEQUENCE   1191 AA;  131885 MW;  09013F372B1FC248 CRC64;
     MTDSFAHLHV HTEYSMLDGA ARIGELMDEV ARQGMPAVAM TDHGYMFGAY EFWRAARDRG
     INPIIGLEGY LTPGTHRSDK TRVSFGDGGG NDVSGAGAYT HLTLLAENTT GMHNLFKLAS
     KASLEGYYFK PRMDLELLST LHQGIIATTG CPSGEVQTRL RLGQYDEAKR VAGEMRELFG
     KENYFVEVMD HGLGIEKQVM TDLVRLAKEL GIPLVATNDS HYTHAADATA HEALLCVQSG
     STLDDPKRFK FDSQDFYIKS AAEMRELFSD IPEACDNTLL IAERVSVDFD ESANYMPKWA
     VEAGDNEADA FRRAVLTGLD ERYPDGVPEE SMRRAEYEMD VIIQMGFPSY FLVVADFITW
     AKDHGIRVGP GRGSGAGSMA AYAMRITELD PIEHGLIFER FLNPDRVSMP DFDVDFDERR
     RGEVIRYVTD KYGEDRVAQI VTFGTIKAKQ ALKDASRVLG YPFGMGEKLT KAMPPSVMGK
     DITLSGINDP EHERYKEAAD FRALLEQDRD AASVFAVAKG LENLKRQWGV HAAGVIMSRS
     PLEDIIPIMR REQDGQIVTQ FDFPTSEALG LVKMDFLALR NLTIIDDALD NIEKSHGQRP
     VLEVLSLDDR PTYELLSRGD TLGVFQLDGG PMRSLLRLLR PERFADISAV LALYRPGPMG
     ADSHTNYALR KNGVQDITPL HPELAEALDG ILGETYGLIV YQEQVMEIAQ KLAGYTLAQA
     DLLRRAMGKK KKEELDIQFE AFQGGMRDNG YSDDAIDTLW DILLPFSDYA FNKAHSAAYG
     VVSYWTGYLK AHYPAEYMAA LLTSVSDDKD KSAIYLNECR RMKIAVLPPD VNESEVNFSA
     VDGSIRFGLG AVRNVGASVV AHIKQARDDK GSFSDFHDFV HKVSLQALNR RTVDSLIKAG
     AFDQLGNTRR SLSEIHESVV DQAVRTKKAA EHGDVGFDFD ALLDSSDGAP SPKIINLPEW
     PKRELLSLER DMLGLYVSDH PLAGLELGLA EHAEMTVAQL LESDIEDGTV VTIAGLLTQA
     NHKVARASGN PYAQVSLEDF SGEIQVMFLG KSYQEHQGLL QPDNIVGLRG RVQRRDDQVT
     LHAQQAKALD IQSRAEARWS GPLTLAVPEY FATAEVLTQL DRILESHPGN YDVRIRLVTS
     HAARMFALPK RVDVTANLIA ELKGVLGKDC IYQPDKTGSP EDANQRSAAT R
//