ID A0A366EAQ1_9BACI Unreviewed; 1115 AA.
AC A0A366EAQ1;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 24-JAN-2024, entry version 18.
DE RecName: Full=DNA polymerase III subunit alpha {ECO:0000256|ARBA:ARBA00019114};
DE EC=2.7.7.7 {ECO:0000256|ARBA:ARBA00012417};
GN ORFNames=DES48_10466 {ECO:0000313|EMBL:RBO99397.1};
OS Paraliobacillus ryukyuensis.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Paraliobacillus.
OX NCBI_TaxID=200904 {ECO:0000313|EMBL:RBO99397.1, ECO:0000313|Proteomes:UP000252254};
RN [1] {ECO:0000313|EMBL:RBO99397.1, ECO:0000313|Proteomes:UP000252254}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 15140 {ECO:0000313|EMBL:RBO99397.1,
RC ECO:0000313|Proteomes:UP000252254};
RA Goeker M.;
RT "Genomic Encyclopedia of Type Strains, Phase IV (KMG-IV): sequencing the
RT most valuable type-strain genomes for metagenomic binning, comparative
RT biology and taxonomic classification.";
RL Submitted (JUN-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: DNA polymerase III is a complex, multichain enzyme
CC responsible for most of the replicative synthesis in bacteria. This DNA
CC polymerase also exhibits 3' to 5' exonuclease activity. The alpha chain
CC is the DNA polymerase. {ECO:0000256|ARBA:ARBA00025611}.
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 -!- SUBUNIT: DNA polymerase III contains a core (composed of alpha, epsilon
CC and theta chains) that associates with a tau subunit. This core
CC dimerizes to form the POLIII' complex. PolIII' associates with the
CC gamma complex (composed of gamma, delta, delta', psi and chi chains)
CC and with the beta chain to form the complete DNA polymerase III
CC complex. {ECO:0000256|ARBA:ARBA00026073}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC -!- SIMILARITY: Belongs to the DNA polymerase type-C family. DnaE
CC subfamily. {ECO:0000256|ARBA:ARBA00009496}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:RBO99397.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; QNRI01000004; RBO99397.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A366EAQ1; -.
DR STRING; 200904.GCA_900168775_02257; -.
DR OrthoDB; 9803237at2; -.
DR Proteomes; UP000252254; Unassembled WGS sequence.
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 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; 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 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; PF14579; HHH_6; 1.
DR Pfam; PF02811; PHP; 1.
DR Pfam; PF01336; tRNA_anti-codon; 1.
DR SMART; SM00481; POLIIIAc; 1.
DR SUPFAM; SSF160975; AF1531-like; 1.
DR SUPFAM; SSF89550; PHP domain-like; 1.
PE 3: Inferred from homology;
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:UP000252254};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 4..71
FT /note="Polymerase/histidinol phosphatase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00481"
SQ SEQUENCE 1115 AA; 126612 MW; D6873CD394F15D79 CRC64;
MTFSHLFVRS GYSFLKSTVK LKELIEQAKQ YNIQAVALTD EQVLHGAVQF YQLAIEAGIK
PIIGMIVYVT EETGGTTPIT VLAKNNQGYQ DLLKLSTALN VAGETSLSLP ELAGYTEHVH
VILPITSSPI ASFLQTGEEA LIKNYLNNWN QLLHKEVCIG VDRKQRLSFP ILKQIVKQLP
NQAIAIQDVR YLRQEDQQAY RCLRAMDQGT TWTSMQQNQD NNDQHFATSE EMHHWFQDWS
ELIEETNQLA NTCNISLELH VHALPKYPLE SGHTASSYLS ELCERALKNK YPDANQVVRN
RMNHELQVIT NMGFSDYFLI VWDFVQYAKN NNIMVGPGRG SAAGSLVAYL LNITEIDPIK
YQLLFERFLN PERISMPDID IDFSDTRRDE VIAYVQQKYG QDHVAQIGTF GTFATRSTIR
ELAKVMEISP EDLAFILKEI PSHSSKSVVE SVKGSTLLRD YIKTSPKLQQ FFTVATKLEG
LPRHLSTHAA GIIISEEPLV NRVALTASHE SIYLTQFAMK DVETIGLLKM DFLGLRNLTL
IERILQSIKK STKDDLDIHH LPLHDKRTFE LLQHAKTNGI FQLESQGMQG VLQQLHPTTF
EDIVAVNALY RPGPMAFIST YINRKHGKEQ VTYPHPDLQP ILQSTYGVLV YQEQIMQIAN
QLAGFSLGQA DLLRRAVSKK NENEIKQLEQ TFLDGCVRNG YDRKVATDVF DWIVRFSNYG
FNRSHAVAYS KISYQLAFLK AHHAANFFAE ILSSVAGQQD KVRIYTNEAQ TFGLSLLPPS
INKSFGKFHV EANQIRVGLW AIKGVGHQAI NHIIEIRKNG SFRSLFDFCM RVSLKIINRS
VIESLILAGA FDALFSDRAS LLATIDRAME QAELFNEFDD QSSLFQDELE LDINYVQVKP
FSDLQQLKYE KDLIGIYISS HPLQKYRKSL RKHGFVTLAK VKTLVNKNKQ QIVAIIQSIK
VIRTKRGDQM AFLTIADESV ELEAVIFPNL FREIKPWLSE ELLVAMTGKV EGRNGKLQFI
INEVEQLDMA SLEKKALARI YIKLEAENEQ QALSHLNQLA EQYPGSAAVI IYHSRTDQTY
QLASSYNLKI ERGCIQTLNN IFGKSNVVIK QHNET
//
