ID H0QVR1_9ACTN Unreviewed; 649 AA.
AC H0QVR1;
DT 22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT 22-FEB-2012, sequence version 1.
DT 24-JAN-2024, entry version 54.
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:GAB16912.1};
GN ORFNames=GOEFS_017_00280 {ECO:0000313|EMBL:GAB16912.1};
OS Gordonia effusa NBRC 100432.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Gordoniaceae;
OC Gordonia.
OX NCBI_TaxID=1077974 {ECO:0000313|EMBL:GAB16912.1, ECO:0000313|Proteomes:UP000035034};
RN [1] {ECO:0000313|EMBL:GAB16912.1, ECO:0000313|Proteomes:UP000035034}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NBRC 100432 {ECO:0000313|EMBL:GAB16912.1,
RC ECO:0000313|Proteomes:UP000035034};
RA Yoshida I., Takarada H., Hosoyama A., Tsuchikane K., Katsumata H.,
RA Yamazaki S., Fujita N.;
RT "Whole genome shotgun sequence of Gordonia effusa NBRC 100432.";
RL Submitted (DEC-2011) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Facilitates transcription termination by a mechanism that
CC involves Rho binding to the nascent RNA, activation of Rho's RNA-
CC dependent ATPase activity, and release of the mRNA from the DNA
CC 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, ECO:0000256|PROSITE-ProRule:PRU01203}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_01884}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:GAB16912.1}.
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DR EMBL; BAEH01000017; GAB16912.1; -; Genomic_DNA.
DR RefSeq; WP_007316250.1; NZ_BAEH01000017.1.
DR AlphaFoldDB; H0QVR1; -.
DR STRING; 1077974.GOEFS_017_00280; -.
DR eggNOG; COG1158; Bacteria.
DR OrthoDB; 9805197at2; -.
DR Proteomes; UP000035034; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0008186; F:ATP-dependent activity, acting on RNA; IEA:InterPro.
DR GO; GO:0004386; F:helicase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0006353; P:DNA-templated transcription termination; IEA:UniProtKB-UniRule.
DR CDD; cd01128; rho_factor_C; 1.
DR Gene3D; 1.10.720.10; -; 1.
DR Gene3D; 2.40.50.140; Nucleic acid-binding proteins; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 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 NCBIfam; TIGR00767; rho; 1.
DR PANTHER; PTHR46425; TRANSCRIPTION TERMINATION FACTOR RHO; 1.
DR PANTHER; PTHR46425:SF1; TRANSCRIPTION TERMINATION FACTOR RHO; 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; Nucleic acid-binding proteins; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF68912; Rho N-terminal domain-like; 1.
DR PROSITE; PS51856; RHO_RNA_BD; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW Rule:MF_01884};
KW Helicase {ECO:0000256|ARBA:ARBA00022806, ECO:0000256|HAMAP-Rule:MF_01884};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|HAMAP-Rule:MF_01884};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_01884}; Reference proteome {ECO:0000313|Proteomes:UP000035034};
KW RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|HAMAP-
KW Rule:MF_01884};
KW Transcription {ECO:0000256|ARBA:ARBA00023163, ECO:0000256|HAMAP-
KW Rule:MF_01884};
KW Transcription regulation {ECO:0000256|ARBA:ARBA00023015, ECO:0000256|HAMAP-
KW Rule:MF_01884};
KW Transcription termination {ECO:0000256|ARBA:ARBA00022472,
KW ECO:0000256|HAMAP-Rule:MF_01884}.
FT DOMAIN 270..348
FT /note="Rho RNA-BD"
FT /evidence="ECO:0000259|PROSITE:PS51856"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 65..266
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 85..104
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 154..192
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 193..224
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 225..241
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 391..396
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01884"
FT BINDING 403..408
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01884"
FT BINDING 434
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01884"
SQ SEQUENCE 649 AA; 69380 MW; 13CA389A0C6A911F CRC64;
MTDTDLITPA APEADAASPA EPRRASVRIG LTGMVLSELR VLAGELGISG TSGMRKGDLI
AAIRERQAEG AGAPPPSAAK AAKGEPKASR AKKADAKSGD DTPVGDKTAD QVAVAEKASE
ASAPAGQAAS EEKSAGQKPA VESGDNPAGD KSASDRGAAD KGAGDKAAGD KSDGESTGGD
RNRNRNRNNR EGGNNNREGN NNREGTNNRG GGQNQNSGQG NNQNNRDDNR DEDGEGGRNR
RGRRFRERRR GRDRDGAGGG EPQLNEDDVV APVAGILDVL DNYAFVRTSG YLSGPNDVYV
SMNMVRKNGL RRGDAITGAV KVPREGEQNN QRQKFNPLVR LDTVNGGEVE AARNRPEFNK
LTPLYPNQRL RLETTPERLT TRVIDLIMPI GKGQRALIVS PPKAGKTTIM QDIANAITTN
NPECHLMVVL VDERPEEVTD MTRSVRGEVI ASTFDRPPSD HTAVAELAIE RAKRLVETGK
DVVVLLDSIT RLGRAYNNSS PASGRILSGG VDSTALYPPK RFLGAARNIE NGGSLTIIAT
AMVETGSTGD TVIFEEFKGT GNAELKLDRK IAERRVFPAV DVNPSSTRKD ELLLAPEEFQ
IVHKLRRILS GLDSQQAIDL LMSQLKKTKS NVEFLMQVQK NAPGVVNDD
//
