(data stored in SCRATCH zone)

SWISSPROT: Q3IDI9_PSEHT

ID   Q3IDI9_PSEHT            Unreviewed;       420 AA.
AC   Q3IDI9;
DT   08-NOV-2005, integrated into UniProtKB/TrEMBL.
DT   08-NOV-2005, sequence version 1.
DT   07-JUN-2017, entry version 95.
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   ECO:0000313|EMBL:CAI85223.1};
GN   OrderedLocusNames=PSHAa0114 {ECO:0000313|EMBL:CAI85223.1};
OS   Pseudoalteromonas haloplanktis (strain TAC 125).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Pseudoalteromonadaceae; Pseudoalteromonas.
OX   NCBI_TaxID=326442 {ECO:0000313|EMBL:CAI85223.1, ECO:0000313|Proteomes:UP000006843};
RN   [1] {ECO:0000313|EMBL:CAI85223.1, ECO:0000313|Proteomes:UP000006843}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TAC 125 {ECO:0000313|Proteomes:UP000006843};
RX   PubMed=16169927; DOI=10.1101/gr.4126905;
RA   Medigue C., Krin E., Pascal G., Barbe V., Bernsel A., Bertin P.,
RA   Cheung F., Cruveiller S., Damico S., Duilio A., Fang G., Feller G.,
RA   Mangenot S., Marino G., Nilsson J., Parilli E., Rocha E., Rouy Z.,
RA   Sekowska A., Tutino M.L., Vallenet D., von Heijne G., Danchin A.;
RT   "Coping with cold: the genome of the versatile marine Antarctica
RT   bacterium Pseudoalteromonas haloplanktis TAC125.";
RL   Genome Res. 15:1325-1335(2005).
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; CR954246; CAI85223.1; -; Genomic_DNA.
DR   ProteinModelPortal; Q3IDI9; -.
DR   IntAct; Q3IDI9; 2.
DR   STRING; 326442.PSHAa0114; -.
DR   EnsemblBacteria; CAI85223; CAI85223; PSHAa0114.
DR   KEGG; pha:PSHAa0114; -.
DR   eggNOG; ENOG4105C1J; Bacteria.
DR   eggNOG; COG0513; LUCA.
DR   HOGENOM; HOG000268807; -.
DR   KO; K03732; -.
DR   OMA; DEMPVNA; -.
DR   OrthoDB; POG091H01ST; -.
DR   Proteomes; UP000006843; Chromosome I.
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; Q3IDI9.
DR   SWISS-2DPAGE; Q3IDI9.
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_00661,
KW   ECO:0000256|RuleBase:RU000492, ECO:0000256|SAAS:SAAS00633009};
KW   Complete proteome {ECO:0000313|Proteomes:UP000006843};
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:CAI85223.1};
KW   Hydrolase {ECO:0000256|HAMAP-Rule:MF_00661,
KW   ECO:0000256|RuleBase:RU000492, ECO:0000256|SAAS:SAAS00632983,
KW   ECO:0000313|EMBL:CAI85223.1};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00661,
KW   ECO:0000256|RuleBase:RU000492, ECO:0000256|SAAS:SAAS00632986};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006843};
KW   RNA-binding {ECO:0000256|HAMAP-Rule:MF_00661,
KW   ECO:0000256|SAAS:SAAS00632988}.
FT   DOMAIN        4     32       Q_MOTIF. {ECO:0000259|PROSITE:PS51195}.
FT   DOMAIN       35    211       Helicase ATP-binding.
FT                                {ECO:0000259|PROSITE:PS51192}.
FT   DOMAIN      235    382       Helicase C-terminal.
FT                                {ECO:0000259|PROSITE:PS51194}.
FT   MOTIF         4     32       Q motif. {ECO:0000256|PROSITE-ProRule:
FT                                PRU00552}.
SQ   SEQUENCE   420 AA;  47461 MW;  69F97DA4E9EB7763 CRC64;
     MTDKKFSDFA IAPEVVAGLT ESGFEYCTPI QAKCLPFICE GRDIAGQAQT GTGKTLAFLT
     ATCHRLLQSS KAPSKHPRAL IMAPTRELAI QIHKDAKILA PHCNLNLGLV YGGEDYEKQR
     AQLEKGVDIL IGTTGRLIDL YKQGCYTLNE IEVVVLDEAD RMFDLGFIKD IRYMFHRMPD
     TSKRLNLLFS ATLSYRVQEL AFEHMTNPEH VQIEPDVKTG KRIQEELFHP SQEDKIKLLL
     TLIEEEWPEK AIIFANTKHS CETVYAWLKA DGHRVGMLTG DVNQKKRQSI LAEFSKGDLD
     FLVATDVAAR GLHIPEVSHV FNFDLPDDCE DYVHRIGRTA RAGASGHAIS FACEQYAYNL
     HEIEEYIDHS IPLSHYDKTA LLDDLTKPTI HRKRNFSTGP RNRSNNSGRR PNNSYQKGRS
//

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