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Database: UniProt
Entry: A0A411HQI9_9GAMM
LinkDB: A0A411HQI9_9GAMM
Original site: A0A411HQI9_9GAMM 
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
//
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