(data stored in SCRATCH zone)

SWISSPROT: Q13E23_RHOPS

ID   Q13E23_RHOPS            Unreviewed;       421 AA.
AC   Q13E23;
DT   31-OCT-2006, integrated into UniProtKB/TrEMBL.
DT   31-OCT-2006, sequence version 1.
DT   08-MAY-2019, entry version 92.
DE   RecName: Full=Transcription termination factor Rho {ECO:0000256|HAMAP-Rule:MF_01884};
DE            EC=3.6.4.- {ECO:0000256|HAMAP-Rule:MF_01884};
DE   AltName: Full=ATP-dependent helicase Rho {ECO:0000256|HAMAP-Rule:MF_01884};
GN   Name=rho {ECO:0000256|HAMAP-Rule:MF_01884};
GN   OrderedLocusNames=RPD_0428 {ECO:0000313|EMBL:ABE37666.1};
OS   Rhodopseudomonas palustris (strain BisB5).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
OC   Bradyrhizobiaceae; Rhodopseudomonas.
OX   NCBI_TaxID=316057 {ECO:0000313|EMBL:ABE37666.1, ECO:0000313|Proteomes:UP000001818};
RN   [1] {ECO:0000313|EMBL:ABE37666.1, ECO:0000313|Proteomes:UP000001818}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BisB5 {ECO:0000313|EMBL:ABE37666.1,
RC   ECO:0000313|Proteomes:UP000001818};
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H.,
RA   Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Pelletier D.A., Kyrpides N.,
RA   Lykidis A., Oda Y., Harwood C.S., Richardson P.;
RT   "Complete sequence of Rhodopseudomonas palustris BisB5.";
RL   Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Facilitates transcription termination by a mechanism
CC       that involves Rho binding to the nascent RNA, activation of Rho's
CC       RNA-dependent ATPase activity, and release of the mRNA from the
CC       DNA template. {ECO:0000256|HAMAP-Rule:MF_01884}.
CC   -!- SUBUNIT: Homohexamer. The homohexamer assembles into an open ring
CC       structure. {ECO:0000256|HAMAP-Rule:MF_01884}.
CC   -!- SIMILARITY: Belongs to the Rho family. {ECO:0000256|HAMAP-
CC       Rule:MF_01884}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation
CC       of feature annotation. {ECO:0000256|HAMAP-Rule:MF_01884}.
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DR   EMBL; CP000283; ABE37666.1; -; Genomic_DNA.
DR   RefSeq; WP_011500854.1; NC_007958.1.
DR   STRING; 316057.RPD_0428; -.
DR   PRIDE; Q13E23; -.
DR   EnsemblBacteria; ABE37666; ABE37666; RPD_0428.
DR   KEGG; rpd:RPD_0428; -.
DR   eggNOG; ENOG4105C4P; Bacteria.
DR   eggNOG; COG1158; LUCA.
DR   HOGENOM; HOG000076952; -.
DR   KO; K03628; -.
DR   OMA; DYNYLPG; -.
DR   OrthoDB; 1619125at2; -.
DR   BioCyc; RPAL316057:RPD_RS02200-MONOMER; -.
DR   Proteomes; UP000001818; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004386; F:helicase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0008186; F:RNA-dependent ATPase activity; IEA:InterPro.
DR   GO; GO:0006353; P:DNA-templated transcription, termination; IEA:UniProtKB-UniRule.
DR   CDD; cd04459; Rho_CSD; 1.
DR   CDD; cd01128; rho_factor; 1.
DR   HAMAP; MF_01884; Rho; 1.
DR   InterPro; IPR003593; AAA+_ATPase.
DR   InterPro; IPR000194; ATPase_F1/V1/A1_a/bsu_nucl-bd.
DR   InterPro; IPR011129; CSD.
DR   InterPro; IPR012340; NA-bd_OB-fold.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR041703; Rho_factor_ATP-bd.
DR   InterPro; IPR011112; Rho_N.
DR   InterPro; IPR036269; Rho_N_sf.
DR   InterPro; IPR011113; Rho_RNA-bd.
DR   InterPro; IPR004665; Term_rho.
DR   PANTHER; PTHR46425; PTHR46425; 1.
DR   Pfam; PF00006; ATP-synt_ab; 1.
DR   Pfam; PF07498; Rho_N; 1.
DR   Pfam; PF07497; Rho_RNA_bind; 1.
DR   SMART; SM00382; AAA; 1.
DR   SMART; SM00357; CSP; 1.
DR   SMART; SM00959; Rho_N; 1.
DR   SUPFAM; SSF50249; SSF50249; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   SUPFAM; SSF68912; SSF68912; 1.
DR   TIGRFAMs; TIGR00767; rho; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q13E23.
DR   SWISS-2DPAGE; Q13E23.
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_01884};
KW   Complete proteome {ECO:0000313|Proteomes:UP000001818};
KW   Helicase {ECO:0000256|HAMAP-Rule:MF_01884};
KW   Hydrolase {ECO:0000256|HAMAP-Rule:MF_01884,
KW   ECO:0000256|SAAS:SAAS00446781};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_01884};
KW   RNA-binding {ECO:0000256|HAMAP-Rule:MF_01884};
KW   Transcription {ECO:0000256|HAMAP-Rule:MF_01884};
KW   Transcription regulation {ECO:0000256|HAMAP-Rule:MF_01884};
KW   Transcription termination {ECO:0000256|HAMAP-Rule:MF_01884}.
FT   DOMAIN        8     50       Rho_N. {ECO:0000259|SMART:SM00959}.
FT   DOMAIN       55    121       CSP. {ECO:0000259|SMART:SM00357}.
FT   DOMAIN      173    358       AAA. {ECO:0000259|SMART:SM00382}.
FT   NP_BIND     172    177       ATP. {ECO:0000256|HAMAP-Rule:MF_01884}.
FT   NP_BIND     184    189       ATP. {ECO:0000256|HAMAP-Rule:MF_01884}.
FT   BINDING     215    215       ATP. {ECO:0000256|HAMAP-Rule:MF_01884}.
SQ   SEQUENCE   421 AA;  47133 MW;  C6E116923EF6E8D0 CRC64;
     MREMKLQDLK AKTPAELVSF AEELGVENAS TMRKQELMFA CLKQLSAKET DIIGEGVVEV
     LSDGFGFLRS PDANYLPGPD DIYVSPSQIR RFGLRTGDTI EGHIRSPKEG ERYFALLKVN
     TLNFEDPEKS KHKVNFDNLT PLFPDERFRL EIDDPTRKDL SARVIDIVAP IGKGQRALIV
     APPRTGKTVL MQNIAHSITA NHPECYLIVL LIDERPEEVT DMQRSVKGEV VSSTFDEPAV
     RHVQVAEMVI EKAKRLVEHG RDVVILLDSI TRLGRAYNTV VPSSGKVLTG GVDANALQRP
     KRFFGAARNI EEGGSLTIIA TALVDTGSRM DEVIFEEFKG TGNSELILDR KVSDKRTFPA
     IDISRSGTRK EELITDPQVL KKMYVLRRIL NPMGTMDAID FLLDKLRNTK NNSEFFESMN
     T
//

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