(data stored in SCRATCH zone)

SWISSPROT: C5BBB2_EDWI9

ID   C5BBB2_EDWI9            Unreviewed;       429 AA.
AC   C5BBB2;
DT   28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT   28-NOV-2012, sequence version 2.
DT   07-JUN-2017, entry version 65.
DE   RecName: Full=ATP-dependent RNA helicase RhlB {ECO:0000256|HAMAP-Rule:MF_00661, ECO:0000256|SAAS:SAAS00633006};
DE            EC=3.6.4.13 {ECO:0000256|HAMAP-Rule:MF_00661, ECO:0000256|SAAS:SAAS00632982};
GN   Name=rhlB {ECO:0000256|HAMAP-Rule:MF_00661};
GN   OrderedLocusNames=NT01EI_0087 {ECO:0000313|EMBL:ACR67347.2};
OS   Edwardsiella ictaluri (strain 93-146).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Hafniaceae; Edwardsiella.
OX   NCBI_TaxID=634503 {ECO:0000313|EMBL:ACR67347.2, ECO:0000313|Proteomes:UP000001485};
RN   [1] {ECO:0000313|Proteomes:UP000001485}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=93-146 {ECO:0000313|Proteomes:UP000001485};
RA   Williams M.L., Gillaspy A.F., Dyer D.W., Thune R.L., Waldbieser G.C.,
RA   Schuster S.C., Gipson J., Zaitshik J., Landry C., Lawrence M.L.;
RT   "Complete genome sequence of Edwardsiella ictaluri 93-146.";
RL   Submitted (MAR-2009) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: DEAD-box RNA helicase involved in RNA degradation. Has
CC       RNA-dependent ATPase activity and unwinds double-stranded RNA.
CC       {ECO:0000256|HAMAP-Rule:MF_00661, ECO:0000256|SAAS:SAAS00632992}.
CC   -!- CATALYTIC ACTIVITY: ATP + H(2)O = ADP + phosphate.
CC       {ECO:0000256|HAMAP-Rule:MF_00661, ECO:0000256|SAAS:SAAS00632985}.
CC   -!- SUBUNIT: Component of the RNA degradosome, which is a multiprotein
CC       complex involved in RNA processing and mRNA degradation.
CC       {ECO:0000256|HAMAP-Rule:MF_00661, ECO:0000256|SAAS:SAAS00633000}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00661,
CC       ECO:0000256|SAAS:SAAS00633003}.
CC   -!- SIMILARITY: Belongs to the DEAD box helicase family. RhlB
CC       subfamily. {ECO:0000256|HAMAP-Rule:MF_00661,
CC       ECO:0000256|SAAS:SAAS00632990}.
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DR   EMBL; CP001600; ACR67347.2; -; Genomic_DNA.
DR   RefSeq; WP_015869568.1; NC_012779.2.
DR   STRING; 634503.NT01EI_0087; -.
DR   EnsemblBacteria; ACR67347; ACR67347; NT01EI_0087.
DR   GeneID; 7959806; -.
DR   KEGG; eic:NT01EI_0087; -.
DR   PATRIC; fig|634503.3.peg.81; -.
DR   eggNOG; ENOG4105C1J; Bacteria.
DR   eggNOG; COG0513; LUCA.
DR   HOGENOM; HOG000268807; -.
DR   KO; K03732; -.
DR   OrthoDB; POG091H01ST; -.
DR   Proteomes; UP000001485; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP.
DR   GO; GO:0004004; F:ATP-dependent RNA helicase activity; IEA:UniProtKB-HAMAP.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-HAMAP.
DR   GO; GO:0006401; P:RNA catabolic process; IEA:UniProtKB-HAMAP.
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; 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   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;
DR   PRODOM; C5BBB2.
DR   SWISS-2DPAGE; C5BBB2.
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_00661,
KW   ECO:0000256|RuleBase:RU000492, ECO:0000256|SAAS:SAAS00633009};
KW   Complete proteome {ECO:0000313|Proteomes:UP000001485};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00661,
KW   ECO:0000256|SAAS:SAAS00632987};
KW   Helicase {ECO:0000256|HAMAP-Rule:MF_00661,
KW   ECO:0000256|RuleBase:RU000492, ECO:0000256|SAAS:SAAS00633007,
KW   ECO:0000313|EMBL:ACR67347.2};
KW   Hydrolase {ECO:0000256|HAMAP-Rule:MF_00661,
KW   ECO:0000256|RuleBase:RU000492, ECO:0000256|SAAS:SAAS00632983};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00661,
KW   ECO:0000256|RuleBase:RU000492, ECO:0000256|SAAS:SAAS00632986};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001485};
KW   RNA-binding {ECO:0000256|HAMAP-Rule:MF_00661,
KW   ECO:0000256|SAAS:SAAS00632988}.
FT   DOMAIN        9     37       Q_MOTIF. {ECO:0000259|PROSITE:PS51195}.
FT   DOMAIN       40    219       Helicase ATP-binding.
FT                                {ECO:0000259|PROSITE:PS51192}.
FT   DOMAIN      245    390       Helicase C-terminal.
FT                                {ECO:0000259|PROSITE:PS51194}.
FT   MOTIF         9     37       Q motif. {ECO:0000256|PROSITE-ProRule:
FT                                PRU00552}.
SQ   SEQUENCE   429 AA;  47745 MW;  9DC5D6BE553355F7 CRC64;
     MSKTHLTEQK FADFALHPMV IKALESKGFH SCTPIQALAL PLAIAGRDVA GQAQTGTGKT
     LAFLASTFHY LLTHPAIAER KTNQPRALIM APTRELAVQI HSDAEPLAQE TGLRLGLAYG
     GDGYDKQLRV LEQGVDILIG TTGRLIDYAK QGHVDLGAIQ VVVLDEADRM FDLGFIKDIR
     WLFRRMPPTA QRLNMLFSAT LSYRVRELAF EHMNNAEYVE VEPEQKTGHR IQEELFYPSN
     EEKMRLLQTL LEEEWPDRCI IFANTKHRCE DIWGHLAADG HRVGLLTGDV PQKKRLRILE
     DFTKGHIDIL VATDVAARGL HIPAVTHVFN YDLPDDCEDY VHRIGRTGRA GASGNSISLA
     CEEYVLNLPA IESYIGHSIP VSKYNGDALL KDLPAPKRLS RSRNGTGARR PGSPRRGSGA
     PRPNRKRSG
//

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