ID   A0A448TTK3_9PAST        Unreviewed;      1161 AA.
AC   A0A448TTK3;
DT   08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT   08-MAY-2019, sequence version 1.
DT   27-MAR-2024, entry version 17.
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:VEJ09141.1};
GN   ORFNames=NCTC12871_00577 {ECO:0000313|EMBL:VEJ09141.1};
OS   Actinobacillus delphinicola.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Actinobacillus.
OX   NCBI_TaxID=51161 {ECO:0000313|EMBL:VEJ09141.1, ECO:0000313|Proteomes:UP000279799};
RN   [1] {ECO:0000313|EMBL:VEJ09141.1, ECO:0000313|Proteomes:UP000279799}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NCTC12871 {ECO:0000313|EMBL:VEJ09141.1,
RC   ECO:0000313|Proteomes:UP000279799};
RG   Pathogen Informatics;
RL   Submitted (DEC-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; LR134510; VEJ09141.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A448TTK3; -.
DR   KEGG; adp:NCTC12871_00577; -.
DR   OrthoDB; 9803237at2; -.
DR   Proteomes; UP000279799; Chromosome 1.
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:VEJ09141.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000279799};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:VEJ09141.1}.
FT   DOMAIN          7..74
FT                   /note="Polymerase/histidinol phosphatase N-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00481"
SQ   SEQUENCE   1161 AA;  130050 MW;  799B5954236C9A0B CRC64;
     MAAPRFVHLR VHSDFSMIDG LPKVKPLVKQ AAKQEMVALG LTDFMNFCGL VKFYGECLGA
     GIKPIIGADF KIKSDLLGED FFDLTLYANN NAGYQNITLL LSKAYQRGYT DFPYIDQEWL
     IEHAEGVIIL SGGKEGDIGQ LLLRTRTEPE LLEQAVSFYE THFPDRFYLS LSRTGKNDEE
     RYIQAAVALA KEKNLPVVAV NDVCFLEPED FEAHEIRVAI HDGYTLDDAR RPKNYTRQQY
     FRTEAEMCEL FADIPSALEN SVKIAERCTA TLHLGEYFLP QFPTGEMSTE DFLVQKAHTG
     LEERLKILFP DEEVRAKERG KYDERLEVEL GVINQMGFPG YFLIVMEFIQ WSKDNDIPVG
     PGRGSGAGSL VAYALKITDL DPLEFDLLFE RFLNPERVSM PDFDVDFCMD GRDRVIDHVA
     ETYGRGAVSQ IITFGTMAAK AVIRDVGRVL GHSYSFVDRI SKLVPTEPGM TLEKAFAAEP
     KLPEIYEADE EVKALIDMAR RLEGVTRNAG KHAGGVVIAP HLITDFAPLY CDSEGKHPVT
     HFDKSDVEYA GLVKFDFLGL RTLTIIKWAL DMINPRLIAQ GKPPVDINHI PLDDPKAFEL
     LLKAETTAVF QLESRGMKDL IKRLRPDCFE DIIALVALFR PGPLQSGMVD NFIRRKHGEE
     EISYPDAEYQ HISLKPILEP TYGIILYQEQ VMQIAQVLAG YTLGGADLLR RAMGKKKPEE
     MAKQRSVFKA GAEKNNIDGE LAMKIFDLVE KFAGYGFNKS HSAAYALVSY QTLWLKAHYP
     AEFMAAVMTS EMDNTDKIVG LYDECLRMGL TVVPPDINTG KHQFTVNDKG EIVYGIGAIK
     GVGEAPIGAI VEARKEGGFF KDLFDLCARV DLKRVNRRTF ESLIKSGAFD KLGPHRAALA
     KNLEDALKAA DQHAKDEDIG QGDMFGVLTD RPEDVETKYA NTPKWTEHQI LEGERETLGL
     YLSGHPISRY LPELEHYAST RLKDLTPSRR GQMSVACGLV VNFRVATTKK GNRIGIATLD
     DRSGRLDVTL FGEALDKNIE KIAKDNIIVC SGQVSFDDFS QGLRMNVRDV MSLEEARVHR
     ANHLAISLSQ DKITPALLRR LKEIIQPYSG GALPIQLYYQ SPQGNALVRF GTQWAVNPQD
     PLLNNLMEFL GSDAVELVFR N
//