(data stored in SCRATCH zone)

SWISSPROT: A0A0F6BHH3_GEOS0

ID   A0A0F6BHH3_GEOS0        Unreviewed;       561 AA.
AC   A0A0F6BHH3;
DT   24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT   24-JUN-2015, sequence version 1.
DT   11-DEC-2019, entry version 25.
DE   RecName: Full=DNA polymerase III subunit gamma/tau {ECO:0000256|RuleBase:RU364063};
DE            EC=2.7.7.7 {ECO:0000256|RuleBase:RU364063};
GN   Name=dnaX {ECO:0000256|RuleBase:RU364063};
GN   OrderedLocusNames=GY4MC1_0018 {ECO:0000313|EMBL:ADP72874.1};
OS   Geobacillus sp. (strain Y4.1MC1).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Geobacillus;
OC   unclassified Geobacillus.
OX   NCBI_TaxID=581103 {ECO:0000313|EMBL:ADP72874.1};
RN   [1] {ECO:0000313|EMBL:ADP72874.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Y4.1MC1 {ECO:0000313|EMBL:ADP72874.1};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L.,
RA   Pitluck S., Chertkov O., Zhang X., Detter J.C., Han C., Tapia R., Land M.,
RA   Hauser L., Jeffries C., Kyrpides N., Ivanova N., Ovchinnikova G., Brumm P.,
RA   Mead D., Woyke T.;
RT   "Complete sequence of chromosome of Geobacillus sp. Y4.1MC1.";
RL   Submitted (OCT-2010) 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.
CC       {ECO:0000256|RuleBase:RU364063}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) =
CC         diphosphate + DNA(n+1); Xref=Rhea:RHEA:22508, Rhea:RHEA-COMP:11130,
CC         Rhea:RHEA-COMP:11131, ChEBI:CHEBI:33019, ChEBI:CHEBI:61560,
CC         ChEBI:CHEBI:83828; EC=2.7.7.7;
CC         Evidence={ECO:0000256|RuleBase:RU364063};
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|RuleBase:RU364063}.
CC   -!- SIMILARITY: Belongs to the DnaX/STICHEL family.
CC       {ECO:0000256|RuleBase:RU364063}.
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DR   EMBL; CP002293; ADP72874.1; -; Genomic_DNA.
DR   RefSeq; WP_003247374.1; NC_014650.1.
DR   EnsemblBacteria; ADP72874; ADP72874; GY4MC1_0018.
DR   KEGG; gmc:GY4MC1_0018; -.
DR   KO; K02343; -.
DR   OMA; EIHCKMV; -.
DR   OrthoDB; 556582at2; -.
DR   BioCyc; GSP581103:G1GOQ-25-MONOMER; -.
DR   GO; GO:0009360; C:DNA polymerase III complex; IEA:InterPro.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR   GO; GO:0003887; F:DNA-directed DNA polymerase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
DR   InterPro; IPR003593; AAA+_ATPase.
DR   InterPro; IPR001270; ClpA/B.
DR   InterPro; IPR008921; DNA_pol3_clamp-load_cplx_C.
DR   InterPro; IPR022754; DNA_pol_III_gamma-3.
DR   InterPro; IPR012763; DNA_pol_III_sug/sutau.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   Pfam; PF12169; DNA_pol3_gamma3; 1.
DR   PRINTS; PR00300; CLPPROTEASEA.
DR   SMART; SM00382; AAA; 1.
DR   SUPFAM; SSF48019; SSF48019; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   TIGRFAMs; TIGR02397; dnaX_nterm; 1.
PE   3: Inferred from homology;
DR   PRODOM; A0A0F6BHH3.
DR   SWISS-2DPAGE; A0A0F6BHH3.
KW   ATP-binding {ECO:0000256|RuleBase:RU364063};
KW   DNA replication {ECO:0000256|RuleBase:RU364063};
KW   DNA-directed DNA polymerase {ECO:0000256|RuleBase:RU364063};
KW   Nucleotide-binding {ECO:0000256|RuleBase:RU364063};
KW   Nucleotidyltransferase {ECO:0000256|RuleBase:RU364063};
KW   Transferase {ECO:0000256|RuleBase:RU364063}.
FT   DOMAIN          37..179
FT                   /note="AAA"
FT                   /evidence="ECO:0000259|SMART:SM00382"
FT   REGION          394..414
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        398..412
FT                   /note="Polar"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   561 AA;  63181 MW;  E38D01578CC24385 CRC64;
     MTYQALYRVF RPQRFADVVG QEHVTKTLQS ALLQNKISHA YLFSGPRGTG KTSAAKIFAK
     AVNCEHAPTA EPCNECPACI GITNGTIPDV LEIDAASNNR VDEIRDIRDK VKFAPTSVRY
     KVYIIDEVHM LSIGAFNALL KTLEEPPKHV IFILATTEPH KIPLTIISRC QRFDFRRIPL
     HSIVARLRHV MEQQGMTASD EALFAIARAA DGGMRDALSL LDQAISFSDG ELLLEDVLAM
     TGSVSSATLA SLIQAVYEKD AATSLRLLEE MMDQGKDPNR LMEDLILYYR DLLLYKTAPH
     VEGAIKGTIV DDTFQHLAES IPLSDIYEAI EVLNKSQQEM KWTNHPRIFL EVALVKLCHQ
     QASSTSSSAE EIQSLARKVE YLEAELRRLK EHNESVAATA PAQAQKQTRP LKTGGYKTPV
     GRIHEILKQA THQDLSLIKS HWAEMLDTLK KQHKVSHAAL LQESEPVAAS PNAFVLKFKY
     EIHCKMAADN TNYVKDNLEA ILFELTKKRF EMVAVPEEEW GKIREEFIRE KGTKREQEKE
     EDPLIAEAKR LFGEEIIEIK E
//

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