(data stored in ACNUC7421 zone)

SWISSPROT: A0KEH1_AERHH

ID   A0KEH1_AERHH            Unreviewed;       421 AA.
AC   A0KEH1;
DT   12-DEC-2006, integrated into UniProtKB/TrEMBL.
DT   12-DEC-2006, sequence version 1.
DT   08-MAY-2019, entry version 95.
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   ECO:0000313|EMBL:ABK39781.1};
GN   OrderedLocusNames=AHA_0099 {ECO:0000313|EMBL:ABK39781.1};
OS   Aeromonas hydrophila subsp. hydrophila (strain ATCC 7966 / DSM 30187 /
OS   JCM 1027 / KCTC 2358 / NCIMB 9240).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Aeromonadales;
OC   Aeromonadaceae; Aeromonas.
OX   NCBI_TaxID=380703 {ECO:0000313|EMBL:ABK39781.1, ECO:0000313|Proteomes:UP000000756};
RN   [1] {ECO:0000313|EMBL:ABK39781.1, ECO:0000313|Proteomes:UP000000756}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 7966 / DSM 30187 / JCM 1027 / KCTC 2358 / NCIMB 9240
RC   {ECO:0000313|Proteomes:UP000000756};
RX   PubMed=16980456; DOI=10.1128/JB.00621-06;
RA   Seshadri R., Joseph S.W., Chopra A.K., Sha J., Shaw J., Graf J.,
RA   Haft D., Wu M., Ren Q., Rosovitz M.J., Madupu R., Tallon L., Kim M.,
RA   Jin S., Vuong H., Stine O.C., Ali A., Horneman A.J., Heidelberg J.F.;
RT   "Genome sequence of Aeromonas hydrophila ATCC 7966T: jack of all
RT   trades.";
RL   J. Bacteriol. 188:8272-8282(2006).
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; CP000462; ABK39781.1; -; Genomic_DNA.
DR   RefSeq; WP_005307308.1; NC_008570.1.
DR   RefSeq; YP_854624.1; NC_008570.1.
DR   STRING; 380703.AHA_0099; -.
DR   PRIDE; A0KEH1; -.
DR   EnsemblBacteria; ABK39781; ABK39781; AHA_0099.
DR   GeneID; 4489139; -.
DR   KEGG; aha:AHA_0099; -.
DR   PATRIC; fig|380703.7.peg.91; -.
DR   eggNOG; ENOG4105C4P; Bacteria.
DR   eggNOG; COG1158; LUCA.
DR   HOGENOM; HOG000076952; -.
DR   KO; K03628; -.
DR   OMA; DYNYLPG; -.
DR   BioCyc; AHYD380703:G1G7B-99-MONOMER; -.
DR   Proteomes; UP000000756; 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; A0KEH1.
DR   SWISS-2DPAGE; A0KEH1.
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_01884};
KW   Complete proteome {ECO:0000313|Proteomes:UP000000756};
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   Reference proteome {ECO:0000313|Proteomes:UP000000756};
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    356       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   421 AA;  46989 MW;  9AF8A27220B08A8F CRC64;
     MNLTELKNTP VSELVQLGES MGLENLARAH KKDIIFAILK AHAKGGEDIF GDGVLEILTD
     GFGFLRSADG SYLAGPDDIY VSPSQIRRFN LRTGDTISGK IRPPKEGERY FALLKVNEVN
     YDRPENSRNK ILFENLTPLH ANERLRMERG NGSTEDITAR VLDLASPIGK GQRGLIVAPP
     KAGKTMLLQN IAQSIAYNHP DCELIVLLID ERPEEVTEMQ RMVKGEVIAS TFDEPASRHV
     QVAEMVIEKA KRLVEHKKDV VILLDSITRL ARAYNTVIPS SGKVLTGGVD ANALHRPKRF
     FGAARNVEEG GSLTIIATAL IDTGSKMDEV IYEEFKGTGN MELHLSRKIA EKRVYPAIDI
     TRSGTRKEEL LTTGDELQKM WILRKIVHPM GEIDGIEFLI DKLAMTKTND EFFDAMRRQQ
     K
//

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