ID   D0YWC9_PHODD            Unreviewed;      1159 AA.
AC   D0YWC9;
DT   19-JAN-2010, integrated into UniProtKB/TrEMBL.
DT   19-JAN-2010, sequence version 1.
DT   27-MAR-2024, entry version 59.
DE   RecName: Full=DNA polymerase III subunit alpha {ECO:0000256|ARBA:ARBA00019114};
DE            EC=2.7.7.7 {ECO:0000256|ARBA:ARBA00012417};
GN   ORFNames=VDA_001373 {ECO:0000313|EMBL:EEZ40348.1};
OS   Photobacterium damselae subsp. damselae CIP 102761.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Photobacterium.
OX   NCBI_TaxID=675817 {ECO:0000313|EMBL:EEZ40348.1, ECO:0000313|Proteomes:UP000003579};
RN   [1] {ECO:0000313|EMBL:EEZ40348.1, ECO:0000313|Proteomes:UP000003579}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CIP 102761 {ECO:0000313|EMBL:EEZ40348.1,
RC   ECO:0000313|Proteomes:UP000003579};
RG   Los Alamos National Laboratory (LANL);
RG   National Microbial Pathogen Data Resource (NMPDR);
RA   Munk A.C., Tapia R., Green L., Rogers Y., Detter J.C., Bruce D.,
RA   Brettin T.S., Colwell R., Huq A., Grim C.J., Hasan N.A., Vonstein V.,
RA   Bartels D.;
RL   Submitted (NOV-2009) 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; ADBS01000001; EEZ40348.1; -; Genomic_DNA.
DR   RefSeq; WP_005297951.1; NZ_ADBS01000001.1.
DR   AlphaFoldDB; D0YWC9; -.
DR   eggNOG; COG0587; Bacteria.
DR   Proteomes; UP000003579; 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; cd07433; PHP_PolIIIA_DnaE1; 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; IPR048472; DNA_pol_IIIA_C.
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   InterPro; IPR049821; PolIIIA_DnaE1_PHP.
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; PF20914; DNA_pol_IIIA_C; 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:EEZ40348.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000003579};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:EEZ40348.1}.
FT   DOMAIN          7..74
FT                   /note="Polymerase/histidinol phosphatase N-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00481"
SQ   SEQUENCE   1159 AA;  129988 MW;  9F73D860C6C1F6B9 CRC64;
     MAEPRFIHLR VHSDFSMIDG LAKVKPIIKK ASELQMPALA ITDFTNLCGL VKFYYAAHDA
     GIKPIIGADF KVQSEELGDE LFDLTILAAN NEGYKNLTLL ISEAYQRGHV QHQPVIDKEW
     LIKHKDGLIL LSGGKTGDVG KALLKGNQNM VEQCVAFYQT YFSDSYYLEL VRTGRPDEEA
     YLHFAIELAE KAQLPVVATN DVRLLSADQF EAHEIRVAIH DGYTLADPNR PKNYSAQQYL
     RSEEEMCELF ADIPEALENS VEIAKRCNVT VRLGEYFLPN FPTGELSTED FLVVKSKEGL
     EERLEFLFPD PDIRAERRPE YDERLEVELE VINQMGFPGY FLIVMEFIQW SKDNGVPVGP
     GRGSGAGSLV AYALKITDLD PLEFDLLFER FLNPERVSMP DFDVDFCMDK RDQVIDHVAD
     MYGRDAVSQI ITFGTMAAKA VIRDVGRVLG HPYGFVDRIS KLVPAEPGMT LAKAFDAEPQ
     LQQSYDSDEE VKDLIDMCRI LEGVTRNAGK HAGGVVISPT TITDFAPLYC DAEGHHPVTQ
     FDKNDVESAG LVKFDFLGLR TLTIIDWALG MINPRLEAQG EDPVNIAAIP MADQKSFTML
     QRSETTAVFQ LESRGMKDLI KRLQPDCFED MIALVALFRP GPLQSGMVDN FIDRKHGREA
     VSYPDEKWQH ESLKDILDPT YGIILYQEQV MQIAQVLAGY TLGGADMLRR AMGKKKPEEM
     AKQRAVFEAG AIKNGVDGEL SMKIFDLVEK FAGYGFNKSH SAAYALVSYQ TLWLKAHYPA
     EFMAAVMTAD MDNTDKIIGL VDECHRMKLK LLPPDVNKGL YRFNVDDQGA IVYGIGAVKG
     VGEGPIENII AAREAGGHFK DLFDFCARID TKKVNKRVLE RLIKSGAMDR LGPNRASMMA
     SLDDAIRAAS QHHQAEAFGQ TDMFGVLTEA PEEVEHKYAN IPEWPDKVWL EGERETLGLY
     LTGHPINSYL SELKHYTTWR LKDAQPTRRD GAATVAGLVI AARVMTTKRG TRIGLLTLDD
     RSGRMEVMLF SEALERYLDL IETDRIVVVT GQVSFDDYNG GLRMSAREVL DISDAREKHL
     RGLAISVTEQ QIDDKFFARF SEILEPHKAG TVPVNVYYQR SNARAKLTLG TEWRITPADQ
     LISDLKILLG EKQVELEFN
//