ID   J3Z602_9ENTR            Unreviewed;      1161 AA.
AC   J3Z602;
DT   31-OCT-2012, integrated into UniProtKB/TrEMBL.
DT   31-OCT-2012, sequence version 1.
DT   27-MAR-2024, entry version 58.
DE   RecName: Full=DNA polymerase III subunit alpha {ECO:0000256|ARBA:ARBA00019114};
DE            EC=2.7.7.7 {ECO:0000256|ARBA:ARBA00012417};
GN   ORFNames=A35E_00510 {ECO:0000313|EMBL:AFP85799.1};
OS   secondary endosymbiont of Heteropsylla cubana.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; aphid secondary symbionts.
OX   NCBI_TaxID=134287 {ECO:0000313|EMBL:AFP85799.1, ECO:0000313|Proteomes:UP000003937};
RN   [1] {ECO:0000313|EMBL:AFP85799.1, ECO:0000313|Proteomes:UP000003937}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Hcub_S {ECO:0000313|EMBL:AFP85799.1};
RX   PubMed=22821013; DOI=10.1093/molbev/mss180;
RA   Sloan D.B., Moran N.A.;
RT   "Genome reduction and co-evolution between the primary and secondary
RT   bacterial symbionts of psyllids.";
RL   Mol. Biol. Evol. 29:3781-3792(2012).
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; CP003547; AFP85799.1; -; Genomic_DNA.
DR   RefSeq; WP_014889096.1; NC_018420.1.
DR   AlphaFoldDB; J3Z602; -.
DR   STRING; 134287.A35E_00510; -.
DR   KEGG; sehc:A35E_00510; -.
DR   PATRIC; fig|134287.3.peg.483; -.
DR   HOGENOM; CLU_001600_0_0_6; -.
DR   OrthoDB; 9803237at2; -.
DR   Proteomes; UP000003937; 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; 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   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; 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   Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW   DNA replication {ECO:0000256|ARBA:ARBA00022705};
KW   DNA-directed DNA polymerase {ECO:0000256|ARBA:ARBA00022932,
KW   ECO:0000313|EMBL:AFP85799.1};
KW   Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695};
KW   Reference proteome {ECO:0000313|Proteomes:UP000003937};
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   1161 AA;  131729 MW;  BF70FAC67266BF05 CRC64;
     MVEPRFIHLH VHSDYSIVDG IIKIGSLIDK AAALYMPAIA ITDFNNLCGT LKFYCSAYKV
     GIKPIIGADF LIKSDILTNE VGELTLLAAN DIGYRHLTLL ISEAYKRGYG SSGLVINREW
     LIKYNKGLIL LSGGRKGDIG KLLIRGNMLK VEKCLLFYEK YFPNHYYIEL IRTKREDEEN
     YIHAAVDLAA RRGIPIVATN DVRFINQEDF NAHEIRVAIH HGFTLNDPKR PRIYSPQQYI
     RKEEEMCTLF ADLPEALTNS VEIAKRCNIS IPMGKYFLPK FPTGEISIEN YLIKCAQEGL
     EKRLRFLFQD PKIRRKKRHL YDVRLNVELK VINQMGFPGY FLIVMEFIQW SKNNGIPVGP
     GRGSGAGSLV AYALNITDLD PLRFDLLFER FLNPERISLP DFDVDFCMEK RDLVIEHVAK
     TYGRDAVAQI ITFGTMTAKA VIRDVGRVLG YPYGFVYQIS KLIPQDAGMT LEKALYMEPQ
     LQSIYDRDEE IKILIDMARK LEGIIRNVGK HAGGVVIAPT KITDFSALYC DAKGNHPVTQ
     FDKNDVEYVG LVKFDFLGLR TLTIINWALE KINNRRENQG QSLIDIKTIP LDDKKSFDIL
     QKSETTGVFQ LESRGMKDLI KRLQPDCFED MIALVALFRP GPLQSGMVDN FIDRKHGNEA
     ISYPDSEWQH LSLKSVLDPT YGIILYQEQV MQIAQVLANY TLGGADILRR AMGKKNPREM
     VTQRSIFKKG AESIGIDGKL SMKIFDLVEK FAGYGFNKSH SAAYALVSYQ TLWLKAHYPA
     EFMAATMTAD MDNTEKVVGL VDECLRMNLR VLPPDINTGQ YYFYVNSDGE IVYGIGAIKG
     VGEGFVEEII KARNKNGKFT DLFDFCMRIN IKKINRHSVE KLIMSGAFDR LGSHRAALIN
     NLKDAFKTAI QQAQADSMGQ TDMFGILPGN SVVPEKVSNS NITPWSKQLI LEGERETIGF
     YLTGHPITQY LDEIAHYTTG ERLKDIHPTE NGKIVKAVGL VLSSRIILTK RGNRIGVFTL
     DDRSGRLDVI LFQNVLKQYQ HLVEKNRILI VEGEVNLDEI NGRLKMTART LMDLSEARQK
     YARRLVVSLS NKTIDENFLN HLQSLLEPYR FGTIPVHIAY RGKYVLGRLH CGSDWKVTPS
     DHLLNDLRQL VGDEHVVLEF K
//