(data stored in SCRATCH zone)

SWISSPROT: Q47TX9_THEFY

ID   Q47TX9_THEFY            Unreviewed;      1188 AA.
AC   Q47TX9;
DT   13-SEP-2005, integrated into UniProtKB/TrEMBL.
DT   13-SEP-2005, sequence version 1.
DT   08-MAY-2019, entry version 104.
DE   RecName: Full=DNA polymerase III subunit alpha {ECO:0000256|SAAS:SAAS01159143};
DE            EC=2.7.7.7 {ECO:0000256|SAAS:SAAS01144005};
GN   OrderedLocusNames=Tfu_0047 {ECO:0000313|EMBL:AAZ54085.1};
OS   Thermobifida fusca (strain YX).
OC   Bacteria; Actinobacteria; Streptosporangiales; Nocardiopsaceae;
OC   Thermobifida.
OX   NCBI_TaxID=269800 {ECO:0000313|EMBL:AAZ54085.1, ECO:0000313|Proteomes:UP000000434};
RN   [1] {ECO:0000313|Proteomes:UP000000434}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=YX {ECO:0000313|Proteomes:UP000000434};
RX   PubMed=17209016; DOI=10.1128/JB.01899-06;
RA   Lykidis A., Mavromatis K., Ivanova N., Anderson I., Land M.,
RA   DiBartolo G., Martinez M., Lapidus A., Lucas S., Copeland A.,
RA   Richardson P., Wilson D.B., Kyrpides N.;
RT   "Genome sequence and analysis of the soil cellulolytic actinomycete
RT   Thermobifida fusca YX.";
RL   J. Bacteriol. 189:2477-2486(2007).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) =
CC         diphosphate + DNA(n+1); Xref=Rhea:RHEA:22508, Rhea:RHEA-
CC         COMP:11130, Rhea:RHEA-COMP:11131, ChEBI:CHEBI:33019,
CC         ChEBI:CHEBI:61560, ChEBI:CHEBI:83828; EC=2.7.7.7;
CC         Evidence={ECO:0000256|SAAS:SAAS01143971};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|SAAS:SAAS01143988}.
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DR   EMBL; CP000088; AAZ54085.1; -; Genomic_DNA.
DR   STRING; 269800.Tfu_0047; -.
DR   EnsemblBacteria; AAZ54085; AAZ54085; Tfu_0047.
DR   KEGG; tfu:Tfu_0047; -.
DR   eggNOG; ENOG4105C0B; Bacteria.
DR   eggNOG; COG0587; LUCA.
DR   HOGENOM; HOG000021785; -.
DR   KO; K02337; -.
DR   OMA; DFCMDGR; -.
DR   BioCyc; TFUS269800:G1G4Q-46-MONOMER; -.
DR   Proteomes; UP000000434; 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   Gene3D; 1.10.10.1600; -; 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; 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   InterPro; IPR004805; PolC_alpha.
DR   PANTHER; PTHR32294; PTHR32294; 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; SSF89550; SSF89550; 1.
DR   TIGRFAMs; TIGR00594; polc; 1.
PE   4: Predicted;
DR   PRODOM; Q47TX9.
DR   SWISS-2DPAGE; Q47TX9.
KW   Complete proteome {ECO:0000313|Proteomes:UP000000434};
KW   Cytoplasm {ECO:0000256|SAAS:SAAS01144001};
KW   DNA replication {ECO:0000256|SAAS:SAAS01143938};
KW   DNA-directed DNA polymerase {ECO:0000256|SAAS:SAAS01144000};
KW   Nucleotidyltransferase {ECO:0000256|SAAS:SAAS01143921,
KW   ECO:0000313|EMBL:AAZ54085.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000434};
KW   Transferase {ECO:0000256|SAAS:SAAS01143903,
KW   ECO:0000313|EMBL:AAZ54085.1}.
FT   DOMAIN        7     74       POLIIIAc. {ECO:0000259|SMART:SM00481}.
SQ   SEQUENCE   1188 AA;  132201 MW;  5112C542EBFE21E6 CRC64;
     MTNDPFVHLH VHTEYSMLDG AAKLKPLFEE AARLGMPAVA MTDHGNMFGS YEFWQTSKES
     GVKPIIGIEA YVAPESRFHK QRVFWGTGKT GDEAAEGGKD VSGGGRYLHL TMWARNAKGL
     RNLFRLSSLA SFEGYYTKPR MDLELMAQYS EGIMVTTGCP SGGVQTRLRL GQEREAIEYA
     GKLRDIFGRD SVFVELMDHG LDIEREVRSG LLTVAKKLGL RPVVTNDSHY VTEDQAAAHD
     ALLAVGVGKN LDDPTRFRFN GTGYYLKSAE EMRSLNTFDE WLEGCRNTLW IAEQVEDGAY
     DDVFRPRDLM PKFPVPEGET QASWLRKEIE RCIPNRYPNG PSREVRERIE HELSIIERMG
     FPAYFLVVAD ICQYARRSGI ALGPGRGSAT GSMVAYVLGI TDLDPLEHSL LFERFLNPER
     VSMPDIDLDF DERKRGDMIR YVTERYGEDR VAQILTFGTI KAKAAIKDAT RILGYPYALG
     DKITKAFPPA VGGKEIPLSA VFDESHPRYN EAAELRQLIE SNPDVRKVYE TASGLEGLTR
     GTGVHAAGVI LSAEPLLDVI PLHKRETDGA IITGFPYPQC EEMGLLKMDF LGLRNLTVID
     DAIQNIKANE GKEINLSALP LDNKKTYELL SRGDTLGVFQ LDGGPMRALL KRMEPKKFGD
     IAAVLALYRP GPMAANAHND YADRSNGRQE ITPIHPELKE ALDPILAESF HLIVYQEQVM
     AIAQQLAGYT LGGADLLRRA MGKKKKEALE KEYTKFSEGM LSRGFSKEAM QALWDVMLPF
     SGYAFNKSHT AGYGMISYWT AYLKANHPAS YMAALLTSVA DDKDKMAVYL AECRKMGIRV
     LPPDVNESGL QFTPVGNDIR FGLGAVRNVG ANVVESILKT REEKGKFTSF VDFLSKIELT
     VCNKRVIESL IKAGAFDSLG HSRLDLYRHH EAAVDAVLSS KKQEAHGQFD LFGGGDEEDG
     GESAPLGFSI NWTGEEWDRK TKLAFEREML GLYVSSHPLA GAERILARAS DAPLLDVVNG
     ERRNNDEVRI AGLISKVEKR INKAGNQWAI ATVEDLDASI EALFFPKVYP LYVDALVEDT
     AVSIKGRLND RDGTFSLFVS EMSILDISHV SEGEPPVLLT IPEKRVTREL ISELKQTLRS
     HRGDTPVRIR VDNPRRSRIF AIDDYPVRVS PEFSGEVKSL LGPESITY
//

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