ID H5Y5D8_9FIRM Unreviewed; 1163 AA.
AC H5Y5D8;
DT 18-APR-2012, integrated into UniProtKB/TrEMBL.
DT 18-APR-2012, sequence version 1.
DT 27-MAR-2024, entry version 54.
DE RecName: Full=DNA polymerase III subunit alpha {ECO:0000256|ARBA:ARBA00019114};
DE EC=2.7.7.7 {ECO:0000256|ARBA:ARBA00012417};
GN ORFNames=DesyoDRAFT_3363 {ECO:0000313|EMBL:EHQ90388.1};
OS Desulfosporosinus youngiae DSM 17734.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Desulfitobacteriaceae;
OC Desulfosporosinus.
OX NCBI_TaxID=768710 {ECO:0000313|EMBL:EHQ90388.1, ECO:0000313|Proteomes:UP000005104};
RN [1] {ECO:0000313|EMBL:EHQ90388.1, ECO:0000313|Proteomes:UP000005104}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 17734 {ECO:0000313|EMBL:EHQ90388.1,
RC ECO:0000313|Proteomes:UP000005104};
RG US DOE Joint Genome Institute (JGI-PGF);
RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA Peters L., Ovchinnikova G., Lu M., Land M.L., Hauser L., Pester M.,
RA Spring S., Ollivier B., Rattei T., Klenk H.-P., Wagner M., Loy A.,
RA Woyke T.J.;
RT "The Noncontiguous Finished genome of Desulfosporosinus youngiae DSM
RT 17734.";
RL Submitted (NOV-2011) 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}.
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DR EMBL; CM001441; EHQ90388.1; -; Genomic_DNA.
DR RefSeq; WP_007784767.1; NZ_CM001441.1.
DR AlphaFoldDB; H5Y5D8; -.
DR STRING; 768710.DesyoDRAFT_3363; -.
DR eggNOG; COG0587; Bacteria.
DR HOGENOM; CLU_001600_0_0_9; -.
DR OrthoDB; 9803237at2; -.
DR Proteomes; UP000005104; 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; cd12113; PHP_PolIIIA_DnaE3; 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 ECO:0000313|EMBL:EHQ90388.1};
KW Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695};
KW Reference proteome {ECO:0000313|Proteomes:UP000005104};
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 1163 AA; 131512 MW; C711349879F237A9 CRC64;
MKTEKTQKTC GFVHLHNHTE FSLLDGAARI KNLVQRAADL QMPALAITDH GVMYGVLDFY
KACRKAGIKP IIGCEVYVAP NKRTDKISGK DDSNYHLVLL AENEQGYRNL IRLVSMAHIE
GFYYKPRVDK EILRKHAEGI IALSACLAGE VADYLVQDQL EMAVQSAREY ESIFGQGNFF
LELQDHGLEE QRKVIIGMWK VHERTGIPMV ATNDVHYVKR EDAFVQDALL CIQMGKTLED
TARMRFSSEE FFLKSEEEMA MLFGEHPELL TNTSLIAERC QMDFHFGENF LPVFEVPSGY
TLNGYLEAEC RKAFPRFYPQ MTERECARLD YELQVIFQTG FAGYFLIVAD FCRYARENGV
VVGPGRGSAA ASMVAYLLGI TSVEPLRFDL LFERFLNPER VSMPDIDIDF DPEGRERVIR
YVTEKYGADK VCQIITFGTM GAKAAIRDGG RVLAIPLFRV DKVAKAIPSD LGMTLEKALE
VSPDLARMVE EDEEIKRLYT LARSLEGMTR HASTHAAGVV IAKEPLMNYL PLQRTSEDFV
MTQFPMKAVE EIGLLKMDFL GLRNLTILQE AVRRIEETHG FKLDLQTLAL DDPKTYSLLA
SGNSTGIFQL ESGGMRTILK DLKPNCFEDI IAVVALYRPG PMEQIPEFIR RKRGGNITYL
HPKLEPILKS TYGIIVYQEQ VMQIARDLGG YSLGRADLLR RAMGKKKKEI MAEERQNFID
GLQDSDGTWI IPGALRLGLT LKDAEEIFDL MAKFAEYGFN KGHATAYAVI SYQTAYLKAN
YPLEFMAALL STVMGSSDKI SFYIQDARSS GIKVLPPDVQ YSQVGFSIED QAIRFGLGAI
RNVGINVVEK ILEARQEGPF KSLDDFCLRV DQKVLNRRVL ESLVRAGAFS SICTRAQALA
VMDQVLDTTG RRQKDRLSGQ FSLFDLDEEM DEGTKLPQLP DFKERDILNM EKEYLGLYLS
GHPLSSVLPQ LKEYISSDII TCLEGEEEKK VALGGLVTGF RQNVTKKGEM MASFVLEDLT
GGIEVLVFPR VFAQTGTLSN DQAVVVVGRY NIRDEEKKIF AEKITRLEDL KPSGENKTIM
SPAASKRLFL RFSHEKSDLM QLVLSIIQRF PGNQPVYFYF EDTQKVLEGK RQFWVNDQDE
LTNALREVMD QHNIVWQQTK NFA
//
