(data stored in ACNUC7421 zone)

SWISSPROT: D6ZB13_SEGRD

ID   D6ZB13_SEGRD            Unreviewed;       485 AA.
AC   D6ZB13;
DT   10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT   10-AUG-2010, sequence version 1.
DT   08-MAY-2019, entry version 49.
DE   RecName: Full=Replicative DNA helicase {ECO:0000256|RuleBase:RU362085};
DE            EC=3.6.4.12 {ECO:0000256|RuleBase:RU362085};
GN   OrderedLocusNames=Srot_0285 {ECO:0000313|EMBL:ADG96772.1};
OS   Segniliparus rotundus (strain ATCC BAA-972 / CDC 1076 / CIP 108378 /
OS   DSM 44985 / JCM 13578).
OC   Bacteria; Actinobacteria; Corynebacteriales; Segniliparaceae;
OC   Segniliparus.
OX   NCBI_TaxID=640132 {ECO:0000313|EMBL:ADG96772.1, ECO:0000313|Proteomes:UP000002247};
RN   [1] {ECO:0000313|EMBL:ADG96772.1, ECO:0000313|Proteomes:UP000002247}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-972 / CDC 1076 / CIP 108378 / DSM 44985 / JCM 13578
RC   {ECO:0000313|Proteomes:UP000002247};
RX   PubMed=21304703; DOI=10.4056/sigs.791633;
RA   Sikorski J., Lapidus A., Copeland A., Misra M., Glavina Del Rio T.,
RA   Nolan M., Lucas S., Chen F., Tice H., Cheng J.F., Jando M.,
RA   Schneider S., Bruce D., Goodwin L., Pitluck S., Liolios K.,
RA   Mikhailova N., Pati A., Ivanova N., Mavromatis K., Chen A.,
RA   Palaniappan K., Chertkov O., Land M., Hauser L., Chang Y.J.,
RA   Jeffries C.D., Brettin T., Detter J.C., Han C., Rohde M., Goker M.,
RA   Bristow J., Eisen J.A., Markowitz V., Hugenholtz P., Kyrpides N.C.,
RA   Klenk H.P.;
RT   "Complete genome sequence of Segniliparus rotundus type strain (CDC
RT   1076).";
RL   Stand. Genomic Sci. 2:203-211(2010).
CC   -!- FUNCTION: Participates in initiation and elongation during
CC       chromosome replication; it exhibits DNA-dependent ATPase activity.
CC       {ECO:0000256|RuleBase:RU362085}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.12;
CC         Evidence={ECO:0000256|RuleBase:RU362085};
CC   -!- SIMILARITY: Belongs to the helicase family. DnaB subfamily.
CC       {ECO:0000256|RuleBase:RU362085}.
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; CP001958; ADG96772.1; -; Genomic_DNA.
DR   STRING; 640132.Srot_0285; -.
DR   EnsemblBacteria; ADG96772; ADG96772; Srot_0285.
DR   KEGG; srt:Srot_0285; -.
DR   eggNOG; ENOG4105CDU; Bacteria.
DR   eggNOG; COG0305; LUCA.
DR   HOGENOM; HOG000113195; -.
DR   KO; K02314; -.
DR   OMA; FQIAEAR; -.
DR   Proteomes; UP000002247; Chromosome.
DR   GO; GO:1990077; C:primosome complex; IEA:UniProtKB-UniRule.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0003678; F:DNA helicase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006269; P:DNA replication, synthesis of RNA primer; IEA:UniProtKB-UniRule.
DR   CDD; cd00984; DnaB_C; 1.
DR   Gene3D; 1.10.860.10; -; 1.
DR   InterPro; IPR003593; AAA+_ATPase.
DR   InterPro; IPR036185; DNA_heli_DnaB-like_N_sf.
DR   InterPro; IPR007692; DNA_helicase_DnaB.
DR   InterPro; IPR007694; DNA_helicase_DnaB-like_C.
DR   InterPro; IPR007693; DNA_helicase_DnaB-like_N.
DR   InterPro; IPR016136; DNA_helicase_N/primase_C.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   Pfam; PF00772; DnaB; 1.
DR   Pfam; PF03796; DnaB_C; 1.
DR   SMART; SM00382; AAA; 1.
DR   SUPFAM; SSF48024; SSF48024; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   TIGRFAMs; TIGR00665; DnaB; 1.
DR   PROSITE; PS51199; SF4_HELICASE; 1.
PE   3: Inferred from homology;
DR   PRODOM; D6ZB13.
DR   SWISS-2DPAGE; D6ZB13.
KW   ATP-binding {ECO:0000256|RuleBase:RU362085};
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Complete proteome {ECO:0000313|Proteomes:UP000002247};
KW   DNA replication {ECO:0000256|RuleBase:RU362085,
KW   ECO:0000256|SAAS:SAAS00740714};
KW   DNA-binding {ECO:0000256|RuleBase:RU362085,
KW   ECO:0000256|SAAS:SAAS00740674};
KW   Helicase {ECO:0000256|RuleBase:RU362085, ECO:0000313|EMBL:ADG96772.1};
KW   Hydrolase {ECO:0000256|RuleBase:RU362085};
KW   Nucleotide-binding {ECO:0000256|RuleBase:RU362085};
KW   Primosome {ECO:0000256|RuleBase:RU362085};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002247}.
FT   DOMAIN      221    485       SF4 helicase. {ECO:0000259|PROSITE:
FT                                PS51199}.
FT   COILED      373    393       {ECO:0000256|SAM:Coils}.
SQ   SEQUENCE   485 AA;  52950 MW;  17716B4048D0758B CRC64;
     MPMPVGESRE RVGLVRAEDA PREDHGLGSA VASRDRGPSS DGPYDAGRQP PQDAVAEQSV
     LGGMLLSKDA IADVLEHVQG KDFYRPAHQL VFDAILELFG RGEPADAVLV AAELERKGHL
     GRIGGAPYLH TLISSVPTAA NASYYAEIVA EKAIMRRLVE AGTRIVQYGY GGADGQDAAE
     VVDRAQAEIF DVTQRKRADE VVALEDLLQP TMDEIDSIAS RGGISLGVPT GFADLDKVTN
     GFHPGQMIIV AARPGVGKST LALDFLRSCS VQNGLASALF SLEMSKMEIV MKLLSAEARI
     RLADMRSGRM SDDDWSRLAR RMSQISEAPL FIDDSPNLTI MEIRAKARRL KQRHDLKLVV
     VDYLQLMTSG KKVESRQQEV SEFSRQLKLL AKELEVPVVA LSQLNRGPEQ RTDKRPMVSD
     LRESGSLEQD ADMVILVHRP DAIEPDDPRG GEADLILGKH RNGPTCTITV AHQLHVSRFV
     DMARG
//

If you have problems or comments...

PBIL Back to PBIL home page