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Database: UniProt
Entry: G7WIM9_DESOD
LinkDB: G7WIM9_DESOD
Original site: G7WIM9_DESOD 
ID   G7WIM9_DESOD            Unreviewed;      1183 AA.
AC   G7WIM9;
DT   25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT   25-JAN-2012, sequence version 1.
DT   27-MAR-2024, entry version 62.
DE   RecName: Full=DNA polymerase III subunit alpha {ECO:0000256|ARBA:ARBA00019114};
DE            EC=2.7.7.7 {ECO:0000256|ARBA:ARBA00012417};
GN   OrderedLocusNames=Desor_3625 {ECO:0000313|EMBL:AET69103.1};
OS   Desulfosporosinus orientis (strain ATCC 19365 / DSM 765 / NCIMB 8382 / VKM
OS   B-1628 / Singapore I) (Desulfotomaculum orientis).
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Desulfitobacteriaceae;
OC   Desulfosporosinus.
OX   NCBI_TaxID=768706 {ECO:0000313|EMBL:AET69103.1, ECO:0000313|Proteomes:UP000006346};
RN   [1] {ECO:0000313|Proteomes:UP000006346}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 19365 / DSM 765 / NCIMB 8382 / VKM B-1628
RC   {ECO:0000313|Proteomes:UP000006346};
RA   Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA   Peters L., Ovchinnikova G., Teshima H., Detter J.C., Han C., Tapia R.,
RA   Land M., Hauser L., Kyrpides N., Ivanova N., Pagani I., Pester M.,
RA   Spring S., Ollivier B., Rattei T., Klenk H.-P., Wagner M., Loy A.,
RA   Woyke T.;
RT   "Complete sequence of Desulfosporosinus orientis DSM 765.";
RL   Submitted (NOV-2011) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:AET69103.1, ECO:0000313|Proteomes:UP000006346}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 19365 / DSM 765 / NCIMB 8382 / VKM B-1628
RC   {ECO:0000313|Proteomes:UP000006346};
RX   PubMed=23105050; DOI=10.1128/JB.01392-12;
RA   Pester M., Brambilla E., Alazard D., Rattei T., Weinmaier T., Han J.,
RA   Lucas S., Lapidus A., Cheng J.F., Goodwin L., Pitluck S., Peters L.,
RA   Ovchinnikova G., Teshima H., Detter J.C., Han C.S., Tapia R., Land M.L.,
RA   Hauser L., Kyrpides N.C., Ivanova N.N., Pagani I., Huntmann M., Wei C.L.,
RA   Davenport K.W., Daligault H., Chain P.S., Chen A., Mavromatis K.,
RA   Markowitz V., Szeto E., Mikhailova N., Pati A., Wagner M., Woyke T.,
RA   Ollivier B., Klenk H.P., Spring S., Loy A.;
RT   "Complete genome sequences of Desulfosporosinus orientis DSM765T,
RT   Desulfosporosinus youngiae DSM17734T, Desulfosporosinus meridiei DSM13257T,
RT   and Desulfosporosinus acidiphilus DSM22704T.";
RL   J. Bacteriol. 194:6300-6301(2012).
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; CP003108; AET69103.1; -; Genomic_DNA.
DR   RefSeq; WP_014185911.1; NC_016584.1.
DR   AlphaFoldDB; G7WIM9; -.
DR   STRING; 768706.Desor_3625; -.
DR   KEGG; dor:Desor_3625; -.
DR   PATRIC; fig|768706.3.peg.3658; -.
DR   eggNOG; COG0587; Bacteria.
DR   HOGENOM; CLU_001600_0_0_9; -.
DR   Proteomes; UP000006346; 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   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; 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:AET69103.1};
KW   Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006346};
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   1183 AA;  133020 MW;  163900697BC13ED0 CRC64;
     MMADTPKETC GFVHLHNHTE YSLLDGAARI KSLVQRAADL NMPALAITDH GVMYGVIDFY
     KACRQAGIKP IIGCEVYVAP HKRTDKAAGK DDANFHLVLL AENEQGYRNL IRLVSMAHIE
     GFYYKPRVDK EILRKHSQGL IALSACLAGE VSDHLVHDQL DMAVEKAREY EDIFGKGNFF
     LEVQDHGLEE QREVNAGMWK VHERTGIPMV ATNDVHYVQR EDAFVQDALL CIQTGKTLED
     ASRMRFSSQE FFLKSEQEMA LLFGEHPELL TNTQQIAQRC QLDFQFGENY LPVFDVPAGY
     TLDSFLEAEC RKAFPHFYPQ MTAKEQERLE YELRVIFQTG FSGYFLIVAD FCRYARANGV
     AVGPGRGSAA ASMVAYLLGI TSVEPMRFDL LFERFLNPER VSMPDIDIDF DPEGRERVIH
     YVTDKYGADK VCQIITFGTM GAKAAIRDVG RVMAIPLYRV DKVAKAIPSD PGMTLEKALE
     VSPDLARLID EDEETKRLYT LAKSLEGMPR HASTHAAGIV ISKDSLVNYL PLQRTSEDFV
     MTQFPMKTVE EIGLLKMDFL GLRNLTILQE AVQRIEETQG FKLDLHTLAL DDAKTYELLS
     SGNSTGIFQL ESGGMRGILK DLKPSCFEDI IAVIALYRPG PMEQIPEFLR RKHGGNITYL
     HPKLEPILKS TYGVIVYQEQ VMQIARDLAG YSLGRADLLR RAMGKKKKEI MAEERQNFVH
     GLQDSNGEWI IPGALRLGLT LKEAEEIFDL MAKFAEYGFN KGHATAYAVI SYQTAYLKAN
     YPLEFMAALL STVMGSSDKI SFYIQDARLS GIEVLPPDVQ YSQVGFSIEK QAIRFGLGAI
     RNVGVNVVEK ILEARKEGIF KSLDDFCLRV DQKVLNKRVM ESLIRAGAFS SLCSRNQALK
     VMDQVLESTG RRQKDRLSGQ FSLFDFDEGM DEVTVLPQVP DLSEREILDM EKEYLGLYLS
     GHPLSSVLPI LKNFISSDIL TCLEGDEEKK VILGGLVTGF RQNVTKKGEM MASFVLEDLT
     AGIEVLVFPR VYAQTASLTN DDVIVVTGRY NIRDDEKKIF AEKITKLEDL KPGGENSGGE
     NSVAASGSLP DEKIAAYHAP QAVLPKRLFL RFSHESTDIM ENVLKILQRY PGSQPVYFYF
     EDTRKVLEGN RSYWVSDQDE LTSALQKVLN QQNVVWQSVK NFA
//
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