ID   A0A432WH83_9GAMM        Unreviewed;      1160 AA.
AC   A0A432WH83;
DT   08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT   08-MAY-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=CWE14_07865 {ECO:0000313|EMBL:RUO33134.1};
OS   Aliidiomarina soli.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC   Idiomarinaceae; Aliidiomarina.
OX   NCBI_TaxID=1928574 {ECO:0000313|EMBL:RUO33134.1, ECO:0000313|Proteomes:UP000287823};
RN   [1] {ECO:0000313|EMBL:RUO33134.1, ECO:0000313|Proteomes:UP000287823}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Y4G10-17 {ECO:0000313|EMBL:RUO33134.1,
RC   ECO:0000313|Proteomes:UP000287823};
RX   PubMed=30364313; DOI=.3389/fmicb.2018.02453;
RA   Liu Y., Lai Q., Shao Z.;
RT   "Genome-Based Analysis Reveals the Taxonomy and Diversity of the Family
RT   Idiomarinaceae.";
RL   Front. Microbiol. 9:2453-2453(2018).
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:RUO33134.1}.
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DR   EMBL; PIPO01000003; RUO33134.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A432WH83; -.
DR   Proteomes; UP000287823; 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   Reference proteome {ECO:0000313|Proteomes:UP000287823};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          8..75
FT                   /note="Polymerase/histidinol phosphatase N-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00481"
SQ   SEQUENCE   1160 AA;  130196 MW;  6B2985D2EEBECFC6 CRC64;
     MTSTPAFIHL RVHSDFSMID GVQKVGPLCK RASELAMPAV ALTDQMNMCG LVRYYKTSED
     LGLKPLIGAD LWVLSDDWPD TPFRLTVLAA NNTGYQNLTL LISDAYLRGH RCGRPCIEQS
     WLADKADGLI VLSGAKDGDV GQALLQRNEK ALQQSLQFYQ THFADHFYLE LIRTGRPQEE
     DYLHLAVDLA SQYDLPVVAT NEVVFLDAED YDAHEIRVSI HDGYTLGDPR RPKQYSEQQY
     LRSAAEMAEV FADIPEALAN TIEIAKRCNV TVTLDEYVLP DFPTGDMSIA DYLVQASQKG
     LEERLEFLFP DPQQRAAQRG EYDERLQIEL KVINDMGFPG YFLIVMEFIQ WSKDNNIPVG
     PGRGSGAGSL VAYALKITDL DPLEFDLLFE RFLNPERVSM PDFDVDFCMD RRDEVIDHVA
     DLYGRDAVSQ IITFGTMAAK AAVRDVGRVL GHPYGFVDRI SKLIPGAPGM TLAKAFEEEP
     RLPQLYNEDE DVKEVIDMAR RLEGVTRNAG KHAGGVVISP TKITDFSPLY CDEDGNFPVT
     QFDKNDVETA GLVKFDFLGL RTLTIIQWAL DMVNPRLRKE GREPVDIVAI PLDDKECFRS
     LKKAETTAVF QLESRGMKEL IKRLLPDSFE DIIALVALFR PGPLQSGMVD NFIDRKHGRE
     AISYPDAQYQ HDSLKTILEP TYGVILYQEQ VMQIAQVLAG YSLGGADLLR RAMGKKKPEE
     MEKQRAVFEK GAADNGIDPE LAIKIFDLVE KFAGYGFNKS HSAAYALVSY QTLWMKVHYP
     AEFMAAVMSA DMDNTDKIVT LVDECERMGL TILPPDVNKG EHKFSVDDEQ RIVYGIGAIK
     GVGEGPIESI ITARNEDGPF RDLFDFCRRV DLKKLNRRVM ERLIKAGALD NLGPHRATLM
     ATLGKAMKQA DQAAKNEAMG QADLFGVLSA ESTDDIDAEF VQVSKWPEPM WLEAERETLG
     LYLTGHPINR YRRELKHYAS GRLADLGETG RGNYVSAAGL VLDVRMMVNK KGQRWAIVTL
     DDRSMRMDMR LYSQEFEKYE DLLQKDSILW VKGEVRFDNF SGGNTMTAYE VMTVEQARAQ
     YVKGLSIQLD LATLAKPQLT RIEQALQSAA GGTCPIVLQC QLENASVDLK PGGNWFIEPK
     DDVLYELWDI LGTSQVKLVF
//