ID A0A3S3YWF6_9MICO Unreviewed; 792 AA.
AC A0A3S3YWF6;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 24-JAN-2024, entry version 30.
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 ORFNames=ELQ90_14180 {ECO:0000313|EMBL:RWZ46587.1};
OS Labedella phragmitis.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Labedella.
OX NCBI_TaxID=2498849 {ECO:0000313|EMBL:RWZ46587.1, ECO:0000313|Proteomes:UP000288547};
RN [1] {ECO:0000313|EMBL:RWZ46587.1, ECO:0000313|Proteomes:UP000288547}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=11W25H-1 {ECO:0000313|EMBL:RWZ46587.1,
RC ECO:0000313|Proteomes:UP000288547};
RA Li F.;
RL Submitted (DEC-2018) 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:RWZ46587.1}.
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DR EMBL; RZNB01000006; RWZ46587.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3S3YWF6; -.
DR OrthoDB; 9805197at2; -.
DR Proteomes; UP000288547; 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; cd04459; Rho_CSD; 1.
DR CDD; cd01128; rho_factor_C; 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; 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 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};
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 404..481
FT /note="Rho RNA-BD"
FT /evidence="ECO:0000259|PROSITE:PS51856"
FT REGION 89..397
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 196..220
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 236..252
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 259..287
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 288..342
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 343..359
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 524..529
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01884"
FT BINDING 536..541
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01884"
FT BINDING 567
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01884"
SQ SEQUENCE 792 AA; 84773 MW; 454B111090149522 CRC64;
MSDVSLRDRI ADNSVAIGSL KVAELKQLAA EWGIADASKL RKGELVEAIT AASNQLASVD
ESGDSTLDGS AAPTEASLAT AGVATEVDVD EANAPAGDAP EQSAAQAEAA PAAVAPSAAV
ETAPATAPTG RRRGSRRATS EDVQRASVPA AGHVNADQPA QIPSTPAVQP VDVVADASPA
APVEADAPAE VAAPSESVSD ESTGAEQQND QQGEQQNADQ QGRERQNKRG NRRGRGRRNN
DQDQQDQDRT EDSAEQQPEE EQPERAEQTD GGEQQPRQGR SRGRNRNRGG DQNGNASAQN
GNGQNEQSQS GQSGNGQNAA AQNGNGNGNG NGRGQSNAQA EQQGRDRTEK ADNEQQGRDR
NRTTAQQQQD DAEGRGRGRY RDRKRRGGAA GEDAEPEISE DDVLIPVAGI LDVLDNYAFV
RTTGYLPGTN DVYVSLGQVK KYNLRKGDAV VGAIRQPREG ENNSRQKYNA IVKVDSVNGQ
PVDEAGTRVE FGKLTPLYPQ ERLRLETEQG KLTQRIIDLV APIGKGQRGL IVAPPKAGKT
IVLQQIANAI SINNPEVHLM VVLVDERPEE VTDMQRTVKG EVIASTFDRP AEDHTTVAEL
AIERAKRLVE LGHDVVVLLD SITRLGRAYN LAAPASGRIL SGGVDASALY PPKRFFGAAR
NIENGGSLTI LATALVETGS KMDEVIFEEF KGTGNSELRL SRQLADKRIF PAVDVNASST
RREEMLLSND EVKITWKLRR ALAGLDQQQA LEVVLGKLKE TSSNVEFLVQ MQKSMPQPAA
NGHSHGHERD HR
//
