GenomeNet

Database: UniProt
Entry: Q8PFZ3
LinkDB: Q8PFZ3
Original site: Q8PFZ3 
ID   RHLB_XANAC              Reviewed;         571 AA.
AC   Q8PFZ3;
DT   27-JUN-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   16-OCT-2019, entry version 102.
DE   RecName: Full=ATP-dependent RNA helicase RhlB {ECO:0000255|HAMAP-Rule:MF_00661};
DE            EC=3.6.4.13 {ECO:0000255|HAMAP-Rule:MF_00661};
GN   Name=rhlB {ECO:0000255|HAMAP-Rule:MF_00661};
GN   OrderedLocusNames=XAC3829;
OS   Xanthomonas axonopodis pv. citri (strain 306).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales;
OC   Xanthomonadaceae; Xanthomonas.
OX   NCBI_TaxID=190486;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=306;
RX   PubMed=12024217; DOI=10.1038/417459a;
RA   da Silva A.C.R., Ferro J.A., Reinach F.C., Farah C.S., Furlan L.R.,
RA   Quaggio R.B., Monteiro-Vitorello C.B., Van Sluys M.A.,
RA   Almeida N.F. Jr., Alves L.M.C., do Amaral A.M., Bertolini M.C.,
RA   Camargo L.E.A., Camarotte G., Cannavan F., Cardozo J., Chambergo F.,
RA   Ciapina L.P., Cicarelli R.M.B., Coutinho L.L., Cursino-Santos J.R.,
RA   El-Dorry H., Faria J.B., Ferreira A.J.S., Ferreira R.C.C.,
RA   Ferro M.I.T., Formighieri E.F., Franco M.C., Greggio C.C., Gruber A.,
RA   Katsuyama A.M., Kishi L.T., Leite R.P., Lemos E.G.M., Lemos M.V.F.,
RA   Locali E.C., Machado M.A., Madeira A.M.B.N., Martinez-Rossi N.M.,
RA   Martins E.C., Meidanis J., Menck C.F.M., Miyaki C.Y., Moon D.H.,
RA   Moreira L.M., Novo M.T.M., Okura V.K., Oliveira M.C., Oliveira V.R.,
RA   Pereira H.A., Rossi A., Sena J.A.D., Silva C., de Souza R.F.,
RA   Spinola L.A.F., Takita M.A., Tamura R.E., Teixeira E.C., Tezza R.I.D.,
RA   Trindade dos Santos M., Truffi D., Tsai S.M., White F.F.,
RA   Setubal J.C., Kitajima J.P.;
RT   "Comparison of the genomes of two Xanthomonas pathogens with differing
RT   host specificities.";
RL   Nature 417:459-463(2002).
CC   -!- FUNCTION: DEAD-box RNA helicase involved in RNA degradation. Has
CC       RNA-dependent ATPase activity and unwinds double-stranded RNA.
CC       {ECO:0000255|HAMAP-Rule:MF_00661}.
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=3.6.4.13;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00661};
CC   -!- SUBUNIT: Component of the RNA degradosome, which is a multiprotein
CC       complex involved in RNA processing and mRNA degradation.
CC       {ECO:0000255|HAMAP-Rule:MF_00661}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00661}.
CC   -!- SIMILARITY: Belongs to the DEAD box helicase family. RhlB
CC       subfamily. {ECO:0000255|HAMAP-Rule:MF_00661}.
DR   EMBL; AE008923; AAM38671.1; -; Genomic_DNA.
DR   RefSeq; WP_011052551.1; NC_003919.1.
DR   SMR; Q8PFZ3; -.
DR   STRING; 190486.XAC3829; -.
DR   EnsemblBacteria; AAM38671; AAM38671; XAC3829.
DR   KEGG; xac:XAC3829; -.
DR   eggNOG; ENOG4105C1J; Bacteria.
DR   eggNOG; COG0513; LUCA.
DR   HOGENOM; HOG000268807; -.
DR   KO; K03732; -.
DR   OMA; TRFHDFK; -.
DR   BioCyc; XAXO190486:XAC_RS19330-MONOMER; -.
DR   Proteomes; UP000000576; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0003724; F:RNA helicase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006401; P:RNA catabolic process; IEA:UniProtKB-UniRule.
DR   HAMAP; MF_00661; DEAD_helicase_RhlB; 1.
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; IPR022077; RhlB.
DR   InterPro; IPR000629; RNA-helicase_DEAD-box_CS.
DR   InterPro; IPR023554; RNA_helicase_ATP-dep_RhlB.
DR   InterPro; IPR014014; RNA_helicase_DEAD_Q_motif.
DR   Pfam; PF00270; DEAD; 1.
DR   Pfam; PF00271; Helicase_C; 1.
DR   Pfam; PF12300; RhlB; 1.
DR   SMART; SM00487; DEXDc; 1.
DR   SMART; SM00490; HELICc; 1.
DR   SUPFAM; SSF52540; SSF52540; 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; Complete proteome; Cytoplasm; Helicase; Hydrolase;
KW   Nucleotide-binding; RNA-binding.
FT   CHAIN         1    571       ATP-dependent RNA helicase RhlB.
FT                                /FTId=PRO_0000200790.
FT   DOMAIN       40    220       Helicase ATP-binding. {ECO:0000255|HAMAP-
FT                                Rule:MF_00661}.
FT   DOMAIN      231    393       Helicase C-terminal. {ECO:0000255|HAMAP-
FT                                Rule:MF_00661}.
FT   NP_BIND      53     60       ATP. {ECO:0000255|HAMAP-Rule:MF_00661}.
FT   MOTIF         9     37       Q motif.
FT   MOTIF       166    169       DEAD box.
SQ   SEQUENCE   571 AA;  62077 MW;  6AB1041B794375A7 CRC64;
     MSDKPLTDVT FSSFDLHPAL IAGLESAGFT RCTPIQALTL PVALPGGDVA GQAQTGTGKT
     LAFLVAVMNR LLIRPALADR KPEDPRALIL APTRELAIQI HKDAVKFGAD LGLRFALVYG
     GVDYDKQREL LQQGVDVIIA TPGRLIDYVK QHKVVSLHAC EICVLDEADR MFDLGFIKDI
     RFLLRRMPER GTRQTLLFSA TLSHRVLELA YEHMNEPEKL VVETESITAA RVRQRIYFPS
     DEEKQTLLLG LLSRSEGART MVFVNTKAFV ERVARTLERH GYRVGVLSGD VPQKKRESLL
     NRFQKGQLEI LVATDVAARG LHIDGVKYVY NYDLPFDAED YVHRIGRTAR LGEEGDAISF
     ACERYAMSLP DIEAYIEQKI PVEPVTSELL TPLPRAPRVP VEGEEADDDA GDSVGTIFRE
     AREQRAAEEQ RRGGGRGGPG GSRSGSGGGR RDGAGADGKP RPRRKPRVEG QAPAAAASTE
     HPVVAAVAAQ APSAGVADAE RAPRKRRRRR NGRPVEGAEP ALASTPVPAP AAPRKPTQVV
     AKPVRAAAKP SGSPSLLSRI GRRLRSLVSG N
//
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