GenomeNet

Database: UniProt
Entry: B0SU57_LEPBP
LinkDB: B0SU57_LEPBP
Original site: B0SU57_LEPBP 
ID   B0SU57_LEPBP            Unreviewed;       534 AA.
AC   B0SU57;
DT   08-APR-2008, integrated into UniProtKB/TrEMBL.
DT   08-APR-2008, sequence version 1.
DT   27-MAR-2024, entry version 93.
DE   SubName: Full=ATP-dependent RNA helicase, DEAD-box family (DeaD) {ECO:0000313|EMBL:ABZ99741.1};
GN   Name=deaD {ECO:0000313|EMBL:ABZ99741.1};
GN   OrderedLocusNames=LEPBI_II0208 {ECO:0000313|EMBL:ABZ99741.1};
OS   Leptospira biflexa serovar Patoc (strain Patoc 1 / ATCC 23582 / Paris).
OC   Bacteria; Spirochaetota; Spirochaetia; Leptospirales; Leptospiraceae;
OC   Leptospira.
OX   NCBI_TaxID=456481 {ECO:0000313|EMBL:ABZ99741.1, ECO:0000313|Proteomes:UP000001847};
RN   [1] {ECO:0000313|EMBL:ABZ99741.1, ECO:0000313|Proteomes:UP000001847}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Patoc 1 / ATCC 23582 / Paris
RC   {ECO:0000313|Proteomes:UP000001847};
RX   PubMed=18270594; DOI=10.1371/journal.pone.0001607;
RA   Picardeau M., Bulach D.M., Bouchier C., Zuerner R.L., Zidane N.,
RA   Wilson P.J., Creno S., Kuczek E.S., Bommezzadri S., Davis J.C., McGrath A.,
RA   Johnson M.J., Boursaux-Eude C., Seemann T., Rouy Z., Coppel R.L.,
RA   Rood J.I., Lajus A., Davies J.K., Medigue C., Adler B.;
RT   "Genome sequence of the saprophyte Leptospira biflexa provides insights
RT   into the evolution of Leptospira and the pathogenesis of leptospirosis.";
RL   PLoS ONE 3:E1607-E1607(2008).
CC   -!- SIMILARITY: Belongs to the DEAD box helicase family.
CC       {ECO:0000256|RuleBase:RU000492}.
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DR   EMBL; CP000787; ABZ99741.1; -; Genomic_DNA.
DR   AlphaFoldDB; B0SU57; -.
DR   STRING; 456481.LEPBI_II0208; -.
DR   KEGG; lbi:LEPBI_II0208; -.
DR   HOGENOM; CLU_003041_21_4_12; -.
DR   Proteomes; UP000001847; Chromosome II.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR   GO; GO:0003724; F:RNA helicase activity; IEA:InterPro.
DR   CDD; cd00268; DEADc; 1.
DR   CDD; cd18787; SF2_C_DEAD; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR   InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR   InterPro; IPR014001; Helicase_ATP-bd.
DR   InterPro; IPR001650; Helicase_C.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR000629; RNA-helicase_DEAD-box_CS.
DR   InterPro; IPR014014; RNA_helicase_DEAD_Q_motif.
DR   PANTHER; PTHR47959:SF19; ATP-DEPENDENT RNA HELICASE DBPA; 1.
DR   PANTHER; PTHR47959; ATP-DEPENDENT RNA HELICASE RHLE-RELATED; 1.
DR   Pfam; PF00270; DEAD; 1.
DR   Pfam; PF00271; Helicase_C; 1.
DR   SMART; SM00487; DEXDc; 1.
DR   SMART; SM00490; HELICc; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   PROSITE; PS00039; DEAD_ATP_HELICASE; 1.
DR   PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR   PROSITE; PS51194; HELICASE_CTER; 1.
DR   PROSITE; PS51195; Q_MOTIF; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU000492};
KW   Helicase {ECO:0000256|ARBA:ARBA00022806, ECO:0000256|RuleBase:RU000492};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU000492};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|RuleBase:RU000492};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001847}.
FT   DOMAIN          15..43
FT                   /note="DEAD-box RNA helicase Q"
FT                   /evidence="ECO:0000259|PROSITE:PS51195"
FT   DOMAIN          46..215
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   DOMAIN          226..388
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
FT   REGION          436..534
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           15..43
FT                   /note="Q motif"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00552"
FT   COMPBIAS        482..504
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   534 AA;  58594 MW;  9E3DABAE81703548 CRC64;
     MYPISMTKND TEVGNDFQSF GLRPEILQGI TEAGFESPSP IQKQAIPLVL EGKDLIAQAQ
     TGTGKTAAYG LPCLNRIKVE DGMQVLVLTP TRELALQVSD ELFKLGKHLG IKTTTIYGGS
     SYSKQITQVA KGAQVAVATP GRLLDLLKGK ELKNFKPSMV ILDEADEMLD MGFMDDIESI
     FNLLPTKRQT LLFSATMPEP IKKLASKYQT HPAHVKIAAT EKSSKNIEQV YYIIDEAERE
     IAVVRILDYE NPFKAIIFTK TKKEADDLKS TLSFKGYPVE ALHGDLNQKQ REQVLKSLHD
     GRVKILVATD VAARGLDVKD LSLVINYHLP FDSESYTHRI GRTGRAGKSG KAVTLVTTRE
     SRALLRLKGT SGTNLTIAAL PTKKEVHLSR EEDFLKKVVD TEIHADAEAV LEKLLKLEDK
     RSIALKLLSK MLDNTKISGP EKIGKTPAEW SEMPPGGGSG GRRRRDDGGG SGGGRGGYRG
     ARSNSDRSER SDRGDRKERG GESSSRRAST PASKKEGGVY VKAAGKKTQR FRNK
//
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