UniProt: A0A2S1R0X5

Database: UniProt
Entry: A0A2S1R0X5_9FLAO

LinkDB:  A0A2S1R0X5_9FLAO 
Original site:  A0A2S1R0X5_9FLAO

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Ontology (8)   
   GO (8)   
Chemical reaction (1)   
   KEGG ENZYME (1)   
Gene (1)   
   KEGG GENES (1)   
DNA sequence (1)   
   EMBL (1)   
Protein domain (10)   
   InterPro (6)   
   Pfam (3)   
   PROSITE (1)   
All databases (21)   

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ID   A0A2S1R0X5_9FLAO        Unreviewed;       846 AA.
AC   A0A2S1R0X5;
DT   18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT   18-JUL-2018, sequence version 1.
DT   27-MAR-2024, entry version 24.
DE   RecName: Full=DNA 3'-5' helicase {ECO:0000256|ARBA:ARBA00034808};
DE            EC=5.6.2.4 {ECO:0000256|ARBA:ARBA00034808};
GN   ORFNames=HYN59_14975 {ECO:0000313|EMBL:AWH86330.1};
OS   Flavobacterium album.
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Flavobacterium.
OX   NCBI_TaxID=2175091 {ECO:0000313|EMBL:AWH86330.1, ECO:0000313|Proteomes:UP000244929};
RN   [1] {ECO:0000313|EMBL:AWH86330.1, ECO:0000313|Proteomes:UP000244929}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HYN0059 {ECO:0000313|EMBL:AWH86330.1,
RC   ECO:0000313|Proteomes:UP000244929};
RA   Yi H., Baek C.;
RT   "Genome sequencing of Flavobacterium sp. HYN0059.";
RL   Submitted (APR-2018) to the EMBL/GenBank/DDBJ databases.
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=5.6.2.4;
CC         Evidence={ECO:0000256|ARBA:ARBA00034618};
CC   -!- SIMILARITY: Belongs to the helicase family. UvrD subfamily.
CC       {ECO:0000256|ARBA:ARBA00009922}.
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DR   EMBL; CP029186; AWH86330.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2S1R0X5; -.
DR   KEGG; falb:HYN59_14975; -.
DR   OrthoDB; 9809039at2; -.
DR   Proteomes; UP000244929; Chromosome.
DR   GO; GO:0005694; C:chromosome; IEA:InterPro.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR   GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR   GO; GO:0003678; F:DNA helicase activity; IEA:InterPro.
DR   GO; GO:0003916; F:DNA topoisomerase activity; IEA:InterPro.
DR   GO; GO:0006265; P:DNA topological change; IEA:InterPro.
DR   Gene3D; 1.10.10.160; -; 1.
DR   Gene3D; 3.30.65.10; Bacterial Topoisomerase I, domain 1; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 3.
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; IPR027417; P-loop_NTPase.
DR   InterPro; IPR013498; Topo_IA_Znf.
DR   InterPro; IPR014016; UvrD-like_ATP-bd.
DR   PANTHER; PTHR11070:SF63; DNA HELICASE IV; 1.
DR   PANTHER; PTHR11070; UVRD / RECB / PCRA DNA HELICASE FAMILY MEMBER; 1.
DR   Pfam; PF00580; UvrD-helicase; 1.
DR   Pfam; PF13361; UvrD_C; 1.
DR   Pfam; PF01396; zf-C4_Topoisom; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   SUPFAM; SSF57783; Zinc beta-ribbon; 1.
DR   PROSITE; PS51198; UVRD_HELICASE_ATP_BIND; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW   ProRule:PRU00560};
KW   Helicase {ECO:0000256|ARBA:ARBA00022806, ECO:0000256|PROSITE-
KW   ProRule:PRU00560};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PROSITE-
KW   ProRule:PRU00560}; Membrane {ECO:0000256|SAM:Phobius};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW   ProRule:PRU00560}; Reference proteome {ECO:0000313|Proteomes:UP000244929};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        9..29
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          141..611
FT                   /note="UvrD-like helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51198"
FT   BINDING         162..169
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00560"
SQ   SEQUENCE   846 AA;  98560 MW;  406E0E96CB24EE02 CRC64;
     MPRKKTSNFF SIMFAVLLCL SVFGIWYLYR KHVLQKKQKQ WLIGARERLE EANFFGERLT
     NFGQYFAFGQ EEQYINGYKD LRKLIVNNYA DLGLDLKLEN DITEFIGRYD EISTLRKNYN
     DEFVKRETET YRYLFDSLEE YPLSDDQIEA VIRDEDNNLV IAGAGTGKTT TISAKVAYIL
     EKGLASPEEL LIISFTKNAV NEMYERCQKF CKDIEGAEKL EVRTFNSFGF LVKRHCSSEE
     IHLAFKGDED AAKAYLQEIF DELFLTDKDF QRKAVNFLAF FNRPERDEFR FETRNDYLKH
     EQGFKNVTLD GISMGSQEEV QIGNFLCLFG INYEYEKHYP LAPEDRNPDF GSYRPDFYLT
     DHDIWHEHFG VDREGNVPNW FGTKQPYTTA KDYYNAGISW KRAIHAKSGT KLIETYSFEN
     AEGSLIANLK KKLRAHGVAL EPRKPEDILP LVKKSAYYED FMNLIHTFLG LMKSNARHPE
     DIQSRGRDRR LAVFLDVFKP LYQRYQEHLH KNSAIDYSDM VNQAAGHIGR GDFTRPYKYI
     LVDEFQDMSL GRYELLKSLK KQYPELKLYA VGDDWQSIFR FTGSDISIIT EFEKHFGFTS
     TTPILRTYRF NDEILQVSSD YIQKNPSQLR KTLFSDRQAQ EKSFAFIPMK FAGNREAYQQ
     AKDLAVRSAL EQISILKEDA RVFLIGRYHH NVPAGFRELK RDYPQLRIDY YTAHRVKGMT
     CDYAILLDIN SGTLGFPSEI ADDPLLGYLL HEGDRFENAE ERRVFYVAIT RARHKNFLLY
     DALNPSKFLG EIMDEPDEGE SSPGKCPECS GQLVERRGPY SEFLGCSNYP NCDYKKIIKS
     NDIINA
//

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