ID A0A411HQI9_9GAMM Unreviewed; 1176 AA.
AC A0A411HQI9;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE RecName: Full=DNA polymerase III subunit alpha {ECO:0000256|ARBA:ARBA00019114};
DE EC=2.7.7.7 {ECO:0000256|ARBA:ARBA00012417};
GN ORFNames=ELE36_14605 {ECO:0000313|EMBL:QBB72712.1};
OS Pseudolysobacter antarcticus.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Pseudolysobacter.
OX NCBI_TaxID=2511995 {ECO:0000313|EMBL:QBB72712.1, ECO:0000313|Proteomes:UP000291562};
RN [1] {ECO:0000313|EMBL:QBB72712.1, ECO:0000313|Proteomes:UP000291562}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AQ6-296 {ECO:0000313|EMBL:QBB72712.1,
RC ECO:0000313|Proteomes:UP000291562};
RA Wei Z., Peng F.;
RT "Pseudolysobacter antarctica gen. nov., sp. nov., isolated from Fildes
RT Peninsula, Antarctica.";
RL Submitted (JAN-2019) 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; CP035704; QBB72712.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A411HQI9; -.
DR KEGG; xbc:ELE36_14605; -.
DR OrthoDB; 9803237at2; -.
DR Proteomes; UP000291562; 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; SSF50249; Nucleic acid-binding proteins; 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:QBB72712.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000291562};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:QBB72712.1}.
FT DOMAIN 6..84
FT /note="Polymerase/histidinol phosphatase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00481"
SQ SEQUENCE 1176 AA; 129506 MW; 676FF721910D542C CRC64;
MSPSFVHLHI HSDYSLIDST IRLPEKAEPG ATPRANLIDQ AVALGMPALA LTDQSNQFAL
VKFFKAAQYA GIKPIIGADL WIADATDAAR PTRITLLCQN REGYLNLSRL ISRGWVEGQR
GDFAMLQPEW FDHACGGLIA MLGRDSDLGR LLLADKRDAI ASCAQHWLQR FDDRLYLELT
RTGHADEEHF LQAALQLANA RDIAAVASND VRFLTRDDFE AHEARVCIQQ GRVINDPKRP
RDYTAEQYLK SPEEMAILFS DLPEALENSI QIAKRCNLDF SFGTYYLPAF PTPPSEDEPA
FLRRLSREGL RGRIERYGID ANFAHADYIQ RLETELDVIV KMGFPGYFLI VADFINWAKQ
HGIPVGPGRG SGAGSLVAYA LGITDLDPLR YGLLFERFLN PDRVSMPDFD VDFCMDRRDE
VIDYVAQKYG RERVSQIITY GTMAAKAVIR DCGRVLGMGY GHVDGIAKLI PNTLGISLEG
ALKESQDLRT RYVEEEEIKD LLDLALKLED LTRNAGKHAG GVVIAPTPLT DFAPLYCEAG
GGGVVTQFDK DDVEAVGLVK FDFLGLRTLT IIDWAVKAIN LRLAKTEQTP LDITQLPLDD
PAVFALLKKA QSVAVFQFES RGMQALLKDA KPDRFEDLIA LVSLFRPGPM DLIPSFCARK
HGREAVTYPD ARVEPILSET YGIMVYQEQV MQMAQIIGGY TLGGADLLRR AMGKKNVQEM
ANHRAIFAEG AAKNGLSNKQ ADAIFDLMEK FAGYGFNKSH AAAYALIAYQ TAWLKAHYPA
EFMAAVLSAD MDNTDKVVTF LDEARALGLR VAPPDVNTSG YMFEALNDGS VCYGLGAIKG
VGHGVCDAIV HARSSGPYLS ITDFCQRMDL HKLNKRVLEA LVLSGSMDAL ARNRATLMAQ
LPEAIKTAEQ AARNTAAGQN DMFGSSSAVA APQIDLPTVE EWPIEQKLIG ERETLGHYLS
GHPTDAWRDA LVQLSTCPLG EIAQHYKPVQ PSERRGRFSD QPFIVAGQVI AVRKRGDAMG
FVQLEDWSGR IEVSFYREAF VEFGPLLTRD TILIIEGGLS IDDFNGGYQL RARTVHSLSQ
ACERFARVMR IKLNGIDASF VAQLEHTLAA HRGGNTPLRL SYANDSGRAE IELGAEWRVR
ASPELKRALE NLPGVIGSEL VLSKPVASAP SSGGGN
//