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Database: UniProt
Entry: Q7VNI3_HAEDU
LinkDB: Q7VNI3_HAEDU
Original site: Q7VNI3_HAEDU 
ID   Q7VNI3_HAEDU            Unreviewed;      1158 AA.
AC   Q7VNI3;
DT   01-OCT-2003, integrated into UniProtKB/TrEMBL.
DT   01-OCT-2003, sequence version 1.
DT   27-MAR-2024, entry version 125.
DE   RecName: Full=DNA polymerase III subunit alpha {ECO:0000256|ARBA:ARBA00019114};
DE            EC=2.7.7.7 {ECO:0000256|ARBA:ARBA00012417};
GN   Name=dnaE {ECO:0000313|EMBL:AAP95487.1};
GN   OrderedLocusNames=HD_0551 {ECO:0000313|EMBL:AAP95487.1};
OS   Haemophilus ducreyi (strain 35000HP / ATCC 700724).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Haemophilus.
OX   NCBI_TaxID=233412 {ECO:0000313|EMBL:AAP95487.1, ECO:0000313|Proteomes:UP000001022};
RN   [1] {ECO:0000313|Proteomes:UP000001022}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=35000HP / ATCC 700724 {ECO:0000313|Proteomes:UP000001022};
RA   Munson R.S. Jr., Ray W.C., Mahairas G., Sabo P., Mungur R., Johnson L.,
RA   Nguyen D., Wang J., Forst C., Hood L.;
RT   "The complete genome sequence of Haemophilus ducreyi.";
RL   Submitted (JUN-2003) 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; AE017143; AAP95487.1; -; Genomic_DNA.
DR   RefSeq; WP_010944540.1; NC_002940.2.
DR   AlphaFoldDB; Q7VNI3; -.
DR   STRING; 233412.HD_0551; -.
DR   KEGG; hdu:HD_0551; -.
DR   eggNOG; COG0587; Bacteria.
DR   HOGENOM; CLU_001600_0_0_6; -.
DR   OrthoDB; 9803237at2; -.
DR   Proteomes; UP000001022; 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   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:UP000001022};
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   1158 AA;  129602 MW;  B75D10DDFDA1FED6 CRC64;
     MTQPRFVHLK VHSDFSMING LAKVKALVKT AAAKQMAAMA LTDFSNFCGL VKFYGESLTA
     GLKPIIGADI YVRSDPTSED IFELTLLAKN NQGYHNITVL LSRAYQQGYV EFPIVEKAWL
     AELNEGIIVL SGGRSGDVGK ALLKENEQEA ATLVAFYQQY FADHYYLSLC RTGRSDEERY
     LQQAVQFAKK YQLPLVAVND VVFLKEDDFD AHEIRVAIHD SYTLDDPKRP QKYSPQQYFR
     SEEEMCALFA DLPQALMNSI QIAMRCNVTI RLGEYFLPNF PTGELSTEDF LIKKSQEGLE
     ERLAFLFPDA ETRKNKRSVY DERLQVELDV INQMGFPGYF LIVMEFIQWS KDNDIPVGPG
     RGSGAGSLVA YALKITDLDP LQFDLLFERF LNPERISMPD FDVDFCMDGR DHVIEHVADT
     YGRQAVSQII TFGTMAAKAV IRDVGRVLGH PYNFVDRISK LIPADPGMTL AKAFEAEPKL
     PELYNADEEV KDLIDMARKL EGVTRNAGKH AGGVVIAPTA ITDFSPLYCD SEGLHPVTHF
     DKNDVEYAGL VKFDFLGLRT LTIIKWALEM INQRLTREGK PPIRIENIPL DDKPSFKLLL
     AAKTTAVFQL ESRGMKDLIS RLKPDCFEDI IALVALFRPG PLESGMVQNF IDRKHGIEEV
     SYPDAQYQHE CLKPILEPTY GIIVYQEQVM QIAQELAGYT LGSADLLRRA MGKKKPEEMA
     AQRDIFEKGA IEKGIDGQLA IKIFDLVEKF AGYGFNKSHS AAYALVSYQT LWLKAHYPAE
     FMAAVMTSEM DNTDKIVGLY DECINMGLTV VPPDVNSGKH RFSVNEKGQI VYGLGAIKGV
     GEGPIEAILE ARNKGGIFKD LFDLTARVDL KKINRRTFES LIMSGAFDKL GPHRAALMKN
     LEDALKASDQ HSKMEALGQS DMFGVLTETP EQVQKAYANT PKWSEQAVLE GERTTLGLYL
     SGHPIGRFLK ELAHYAPTRL NELQPTRRGQ MVTVAGIIVA SRIAVTKRGS RLGIATLEDR
     AGKIDITLFS EALENYGDLL VKDNIIIATG SVQSDDFNGG LKMSVREIAN LDEIRSRYAK
     SLALAISQQQ LTPQFVKALR EIIEPYKEGT LPLHFYYQSP EGRALLRGGV EWRVTPKDEM
     LDKLAVLLGE NAVELEFE
//
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