(data stored in SCRATCH zone)

SWISSPROT: A0A0E1NWJ3_YERPA

ID   A0A0E1NWJ3_YERPA        Unreviewed;       673 AA.
AC   A0A0E1NWJ3;
DT   27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT   27-MAY-2015, sequence version 1.
DT   08-MAY-2019, entry version 25.
DE   RecName: Full=ATP-dependent DNA helicase Rep {ECO:0000256|HAMAP-Rule:MF_01920};
DE            EC=3.6.4.12 {ECO:0000256|HAMAP-Rule:MF_01920};
GN   Name=rep {ECO:0000256|HAMAP-Rule:MF_01920};
GN   OrderedLocusNames=YPA_0146 {ECO:0000313|EMBL:ABG12115.1};
OS   Yersinia pestis bv. Antiqua (strain Antiqua).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Yersiniaceae; Yersinia.
OX   NCBI_TaxID=360102 {ECO:0000313|EMBL:ABG12115.1, ECO:0000313|Proteomes:UP000001971};
RN   [1] {ECO:0000313|EMBL:ABG12115.1, ECO:0000313|Proteomes:UP000001971}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Antiqua {ECO:0000313|EMBL:ABG12115.1,
RC   ECO:0000313|Proteomes:UP000001971};
RX   PubMed=16740952; DOI=10.1128/JB.00124-06;
RA   Chain P.S., Hu P., Malfatti S.A., Radnedge L., Larimer F.,
RA   Vergez L.M., Worsham P., Chu M.C., Andersen G.L.;
RT   "Complete genome sequence of Yersinia pestis strains Antiqua and
RT   Nepal516: evidence of gene reduction in an emerging pathogen.";
RL   J. Bacteriol. 188:4453-4463(2006).
CC   -!- FUNCTION: Rep helicase is a single-stranded DNA-dependent ATPase
CC       involved in DNA replication; it can initiate unwinding at a nick
CC       in the DNA. It binds to the single-stranded DNA and acts in a
CC       progressive fashion along the DNA in the 3' to 5' direction.
CC       {ECO:0000256|HAMAP-Rule:MF_01920}.
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|HAMAP-Rule:MF_01920,
CC         ECO:0000256|SAAS:SAAS01129065};
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_01920}.
CC   -!- SIMILARITY: Belongs to the helicase family. UvrD subfamily.
CC       {ECO:0000256|HAMAP-Rule:MF_01920, ECO:0000256|SAAS:SAAS00709641}.
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DR   EMBL; CP000308; ABG12115.1; -; Genomic_DNA.
DR   RefSeq; WP_002211993.1; NZ_CP009906.1.
DR   EnsemblBacteria; ABG12115; ABG12115; YPA_0146.
DR   EnsemblBacteria; AJJ81329; AJJ81329; CH58_2988.
DR   KEGG; ypa:YPA_0146; -.
DR   PATRIC; fig|360102.15.peg.3139; -.
DR   KO; K03656; -.
DR   OMA; HCANILI; -.
DR   Proteomes; UP000001971; Chromosome.
DR   GO; GO:0008408; F:3'-5' exonuclease activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004003; F:ATP-dependent DNA helicase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0003697; F:single-stranded DNA binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0006268; P:DNA unwinding involved in DNA replication; IEA:UniProtKB-UniRule.
DR   Gene3D; 1.10.10.160; -; 1.
DR   HAMAP; MF_01920; Helicase_Rep; 1.
DR   InterPro; IPR013986; DExx_box_DNA_helicase_dom_sf.
DR   InterPro; IPR014017; DNA_helicase_UvrD-like_C.
DR   InterPro; IPR000212; DNA_helicase_UvrD/REP.
DR   InterPro; IPR005752; Helicase_Rep.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR014016; UvrD-like_ATP-bd.
DR   InterPro; IPR034739; UvrD/AddA_N.
DR   PANTHER; PTHR11070; PTHR11070; 1.
DR   Pfam; PF00580; UvrD-helicase; 1.
DR   Pfam; PF13361; UvrD_C; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   TIGRFAMs; TIGR01074; rep; 1.
DR   PROSITE; PS51198; UVRD_HELICASE_ATP_BIND; 1.
DR   PROSITE; PS51217; UVRD_HELICASE_CTER; 1.
PE   3: Inferred from homology;
DR   PRODOM; A0A0E1NWJ3.
DR   SWISS-2DPAGE; A0A0E1NWJ3.
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_01920,
KW   ECO:0000256|SAAS:SAAS00146071};
KW   Complete proteome {ECO:0000313|Proteomes:UP000001971};
KW   DNA replication {ECO:0000256|HAMAP-Rule:MF_01920};
KW   DNA-binding {ECO:0000256|HAMAP-Rule:MF_01920,
KW   ECO:0000256|SAAS:SAAS00745286};
KW   Helicase {ECO:0000256|HAMAP-Rule:MF_01920,
KW   ECO:0000256|SAAS:SAAS00553650, ECO:0000313|EMBL:ABG12115.1};
KW   Hydrolase {ECO:0000256|HAMAP-Rule:MF_01920,
KW   ECO:0000256|SAAS:SAAS00146062, ECO:0000313|EMBL:ABG12115.1};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_01920,
KW   ECO:0000256|SAAS:SAAS00145996}.
FT   BINDING     278    278       ATP. {ECO:0000256|HAMAP-Rule:MF_01920}.
SQ   SEQUENCE   673 AA;  77316 MW;  6040EAA1BE22DC61 CRC64;
     MRLNPSQQEA VEFVTGPCLV LAGAGSGKTR VITNKIAHLI RQCGYQPKHI AAVTFTNKAA
     REMKERVAQT LGRKEARGLM IATFHTLGLE IIKKEYVALG MKSNFSLFDA QDQMGLLKDL
     THKWLEDDKT LLQQLVSAIS NWKNDLLDPA AAAATARSER DKLFVHCYGL YDAHLKACNV
     LDFDDLISLP TLLLQKNLEV RERWQNRLRY LLVDEYQDTN TSQYQMVKLL VGNRARFTVV
     GDDDQSIYSW RGARPQNLVL LNEDFPALRV IKLEQNYRSS GRILKAANIL IANNPHVFEK
     KLFSELSYGD ELKVITANNE DHEAERVVGE LIAHHFVKKT QYSDYAILYR GNHQSRLFEK
     LLMQNRIPYR ISGGDSFFSR PEIKDLLAYL RVLTNQDDDS AFLRIVNTPK REIGAATVQK
     LGEWANLRNK SLFRASFDLG LGEHLKGRGL ESLQRFTHWM DGIIRLVERE PVAAVRDLIH
     GIDYESWLFE TAPSPKAAEM RMKNVNLLFS WMTEMLEGSE LDEPMTLTQV VTRFTLRDMM
     ERGESDEELD QVQLMTLHAS KGLEFPYVFL VGMEEGLLPH QSSIDEDNVD EERRLAYVGI
     TRAQRELFFT LCKERRQYGE LIRPEPSRFL MELPQDDLNW ENERKAVSPE ERMQKGQSHL
     ANLRAQLANA KKP
//

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