(data stored in ACNUC7421 zone)

SWISSPROT: C5BBB4_EDWI9

ID   C5BBB4_EDWI9            Unreviewed;       419 AA.
AC   C5BBB4;
DT   28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT   28-JUL-2009, sequence version 1.
DT   05-JUL-2017, entry version 62.
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=NT01EI_0089 {ECO:0000313|EMBL:ACR67349.1};
OS   Edwardsiella ictaluri (strain 93-146).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Hafniaceae; Edwardsiella.
OX   NCBI_TaxID=634503 {ECO:0000313|EMBL:ACR67349.1, 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: 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}.
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DR   EMBL; CP001600; ACR67349.1; -; Genomic_DNA.
DR   RefSeq; WP_005297111.1; NC_012779.2.
DR   ProteinModelPortal; C5BBB4; -.
DR   STRING; 634503.NT01EI_0089; -.
DR   EnsemblBacteria; ACR67349; ACR67349; NT01EI_0089.
DR   GeneID; 7959808; -.
DR   KEGG; eic:NT01EI_0089; -.
DR   eggNOG; ENOG4105C4P; Bacteria.
DR   eggNOG; COG1158; LUCA.
DR   HOGENOM; HOG000076952; -.
DR   KO; K03628; -.
DR   OMA; DYNYLPG; -.
DR   OrthoDB; POG091H05EO; -.
DR   Proteomes; UP000001485; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP.
DR   GO; GO:0004386; F:helicase activity; IEA:UniProtKB-HAMAP.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-HAMAP.
DR   GO; GO:0008186; F:RNA-dependent ATPase activity; IEA:InterPro.
DR   GO; GO:0006353; P:DNA-templated transcription, termination; IEA:UniProtKB-HAMAP.
DR   GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:UniProtKB-KW.
DR   CDD; cd04459; Rho_CSD; 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; IPR011112; Rho_N.
DR   InterPro; IPR011113; Rho_RNA-bd.
DR   InterPro; IPR004665; Term_rho.
DR   PANTHER; PTHR15184:SF54; PTHR15184:SF54; 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; C5BBB4.
DR   SWISS-2DPAGE; C5BBB4.
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_01884};
KW   Complete proteome {ECO:0000313|Proteomes:UP000001485};
KW   Helicase {ECO:0000256|HAMAP-Rule:MF_01884};
KW   Hydrolase {ECO:0000256|HAMAP-Rule:MF_01884,
KW   ECO:0000256|SAAS:SAAS00061541};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_01884};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001485};
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        5     47       Rho_N. {ECO:0000259|SMART:SM00959}.
FT   DOMAIN       52    118       CSP. {ECO:0000259|SMART:SM00357}.
FT   DOMAIN      170    355       AAA. {ECO:0000259|SMART:SM00382}.
FT   NP_BIND     169    174       ATP. {ECO:0000256|HAMAP-Rule:MF_01884}.
FT   NP_BIND     181    186       ATP. {ECO:0000256|HAMAP-Rule:MF_01884}.
FT   REGION       61     66       RNA-binding 1. {ECO:0000256|HAMAP-Rule:
FT                                MF_01884}.
FT   REGION       78     80       RNA-binding 1. {ECO:0000256|HAMAP-Rule:
FT                                MF_01884}.
FT   REGION      108    110       RNA-binding 1. {ECO:0000256|HAMAP-Rule:
FT                                MF_01884}.
FT   REGION      284    288       RNA-binding 2. {ECO:0000256|HAMAP-Rule:
FT                                MF_01884}.
FT   BINDING     212    212       ATP. {ECO:0000256|HAMAP-Rule:MF_01884}.
FT   SITE        326    326       RNA-binding 2. {ECO:0000256|HAMAP-Rule:
FT                                MF_01884}.
SQ   SEQUENCE   419 AA;  46935 MW;  ECE917F477F330A5 CRC64;
     MNLTELKNTP VSELITLGES MGLENLARMR KQDIIFAILK QHAKSGEDIF GDGVLEILQD
     GFGFLRSADS SYLAGPDDIY VSPSQIRRFN LRTGDTISGK IRPPKEGERY FALLKVNEVN
     YDKPENARSK ILFENLTPLH ANSRLRMERG NGSTEDLTAR VLDLASPIGR GQRGLIVAPP
     KAGKTMLLQN IAQSIAYNHP DCVLMVLLID ERPEEVTEMQ RLVKGEVVAS TFDEPASRHV
     QVAEMVIEKA KRLVEHKKDV IILLDSITRL ARAYNTVVPA SGKVLTGGVD ANALHRPKRF
     FGAARNVEEG GSLTIIATAL IDTGSKMDEV IYEEFKGTGN MELHLSRKIA EKRVFPAIDY
     NRSGTRKEEL LTTPEELQKM WILRKIIHPM GEIDAMEFLI NKLAMTKTND EFFDMMKRS
//

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