ID A0A1W6YYG8_9BORD Unreviewed; 1164 AA.
AC A0A1W6YYG8;
DT 05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2017, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE RecName: Full=DNA polymerase III subunit alpha {ECO:0000256|ARBA:ARBA00019114};
DE EC=2.7.7.7 {ECO:0000256|ARBA:ARBA00012417};
GN ORFNames=CAL13_07680 {ECO:0000313|EMBL:ARP86096.1};
OS Bordetella genomosp. 9.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Alcaligenaceae; Bordetella.
OX NCBI_TaxID=1416803 {ECO:0000313|EMBL:ARP86096.1, ECO:0000313|Proteomes:UP000194139};
RN [1] {ECO:0000313|EMBL:ARP86096.1, ECO:0000313|Proteomes:UP000194139}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AU17164 {ECO:0000313|EMBL:ARP86096.1,
RC ECO:0000313|Proteomes:UP000194139};
RA Spilker T., LiPuma J.;
RT "Complete and WGS of Bordetella genogroups.";
RL Submitted (MAY-2017) 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; CP021109; ARP86096.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1W6YYG8; -.
DR OrthoDB; 9803237at2; -.
DR Proteomes; UP000194139; 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 Aminoacyl-tRNA synthetase {ECO:0000256|ARBA:ARBA00023146};
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW DNA replication {ECO:0000256|ARBA:ARBA00022705};
KW DNA-directed DNA polymerase {ECO:0000256|ARBA:ARBA00022932};
KW Ligase {ECO:0000256|ARBA:ARBA00023146};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022840};
KW Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695};
KW Reference proteome {ECO:0000313|Proteomes:UP000194139};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 13..80
FT /note="Polymerase/histidinol phosphatase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00481"
SQ SEQUENCE 1164 AA; 130585 MW; 1063E59C3824F0BC CRC64;
MSEEAVVAPS PFVHLRVHSE FSVVDGLVRI PDLVKRAAKL GQPAVALTDL CNLFGLIKFY
KAARGAGIKP IAGCDVWITN DDDREKPHRL LVLVRNRQGY LDLCDLLTRA WLNNQHKGRA
EVRREWLQRA QGLIVLSGGR AGDVGQALEA GNAAQAQALA RQWAAAFPNA YYIELQRAGF
DGDEAYVQAA LRLAGECGLP VVATHPVQFL DKHEFQAHEA RVCIAEGEIL ANPRRVRRFN
EDQYLLDSQE MARRFADVPS ALENTVEIAR RCNLTLVLGK PRLPNFPTPE GVTLDDYLVQ
LSEEGLEKRL KFLFPDEAER AAKRDMYFER LRWECKTIIQ MGFPGYFLIV QDFINWGKNN
GVPVGPGRGS GAGSLVAYAL GITDLDPIRY DLLFERFLNP ERVSMPDFDI DFCQDNRERV
IDYVKSKYGR EAVSQIATFG TLGAKAVVRD AGRVLDMPYT FCDGLSKLIP FNPADPWTLE
RTLKEEPAFR ERYEQEEEVR GLVDLAKPLE GLTRSIGMHA GGVLIAPGKL TDFCPLYCQP
GQENSAVSQF DKDDVEAAGL VKFDFLGLRN LTILDWAVRY VRQFNEDKRD FDIMAVPLDD
PAAYKVLTDA NTTAVFQLES RGMKELLKKL RPSTFEDIIA MLALYRPGPL ESGMVDDFVN
RKHGRAPVDY FHPDLEGTLK STYGVIVYQE QVMLISQIIG GYSLGGADLL RRAMGKKKPE
EMAKHRELFQ KGAQEKGHDP NLAVKLFDLM EKFAGYGFNK SHSAAYALIA YQTAWLKAYH
PAEFLAATLS SDMDDTDKVQ TFWRDAVENG VEVLPPDVNA SNYRFEPVAD ARTAKGLPPR
TMRYGLGAVK GTGQSAVEEI IRARNEGGPF KDLFDFCRRV DKHTVNRRTI EALIKAGAFD
SIEPNRAALL ASVPTAMEAA EQAARSANQV SLFGDDGSDV VASELAKVPP WNLHTKLTEE
KSALGFYFSG HLFDAWRDEV RRIVPMTLAR LEPQREPQWM CGVLSGVRAM MTRRGKMVFA
VLDDGTAQVE ISIFNELYEK HRNRLREDQL LIVHGKVSND EYSGGMRIVA ENLFDLQLAR
EARARALRIR LNGNADAAHL RKLLNPYRAE PENGVPGTPV EVVYTRDNFL CTVRLGEDWR
VRMADALLER LNEWTRPEGV EIAY
//
