(data stored in ACNUC7421 zone)

SWISSPROT: Q3IDJ1_PSEHT

ID   Q3IDJ1_PSEHT            Unreviewed;       419 AA.
AC   Q3IDJ1;
DT   08-NOV-2005, integrated into UniProtKB/TrEMBL.
DT   08-NOV-2005, sequence version 1.
DT   05-JUL-2017, entry version 97.
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:CAI85221.1};
GN   OrderedLocusNames=PSHAa0112 {ECO:0000313|EMBL:CAI85221.1};
OS   Pseudoalteromonas haloplanktis (strain TAC 125).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Pseudoalteromonadaceae; Pseudoalteromonas.
OX   NCBI_TaxID=326442 {ECO:0000313|EMBL:CAI85221.1, ECO:0000313|Proteomes:UP000006843};
RN   [1] {ECO:0000313|EMBL:CAI85221.1, 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: 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; CR954246; CAI85221.1; -; Genomic_DNA.
DR   RefSeq; WP_011326839.1; NC_007481.1.
DR   ProteinModelPortal; Q3IDJ1; -.
DR   STRING; 326442.PSHAa0112; -.
DR   EnsemblBacteria; CAI85221; CAI85221; PSHAa0112.
DR   GeneID; 32567566; -.
DR   KEGG; pha:PSHAa0112; -.
DR   eggNOG; ENOG4105C4P; Bacteria.
DR   eggNOG; COG1158; LUCA.
DR   HOGENOM; HOG000076952; -.
DR   KO; K03628; -.
DR   OMA; DYNYLPG; -.
DR   OrthoDB; POG091H05EO; -.
DR   Proteomes; UP000006843; Chromosome I.
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; Q3IDJ1.
DR   SWISS-2DPAGE; Q3IDJ1.
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_01884};
KW   Complete proteome {ECO:0000313|Proteomes:UP000006843};
KW   Helicase {ECO:0000256|HAMAP-Rule:MF_01884};
KW   Hydrolase {ECO:0000256|HAMAP-Rule:MF_01884,
KW   ECO:0000256|SAAS:SAAS00061541, ECO:0000313|EMBL:CAI85221.1};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_01884};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006843};
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;  47089 MW;  115F5DA7165FA959 CRC64;
     MHLRELKDKS IKELVDLAES MGLENVARLR KQDIIFAILK SHAKGGENIF GGGVLEILQD
     GFGFLRSSEA SYLAGPDDIY VSPSQIRRFS MRTGDSISGL IRPPKDGERY FALLKVNEVN
     FDKPENSRTK ILFENLTPLH ANERFRMERG NGSKEDITAR VLDLASPIGR GQRGLLVAPP
     KAGKTMLLQN IAQSITHNHP DATLMVLLID ERPEEVTEMQ RLVKGEVIAS TFDEPASRHV
     QVAEMVIEKA KRLVEHKKDV VILLDSITRL ARAYNTVIPS SGKVLTGGVD ANALHKPKRF
     FGAARNVEEG GSLTIIATAL IDTGSKMDEV IYEEFKGTGN MELHLNRKIA ERRVFPAIDF
     NRSGTRREEL LTKPDELQKL WILRKIVHDM SEIDAMEFLI DKLSMSKTND EFFDSMKRQ
//

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