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Database: UniProt
Entry: C7MNY8_CRYCD
LinkDB: C7MNY8_CRYCD
Original site: C7MNY8_CRYCD 
ID   C7MNY8_CRYCD            Unreviewed;       638 AA.
AC   C7MNY8;
DT   13-OCT-2009, integrated into UniProtKB/TrEMBL.
DT   13-OCT-2009, sequence version 1.
DT   24-JAN-2024, entry version 92.
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=Ccur_09300 {ECO:0000313|EMBL:ACU94628.1};
OS   Cryptobacterium curtum (strain ATCC 700683 / DSM 15641 / CCUG 43107 /
OS   12-3).
OC   Bacteria; Actinomycetota; Coriobacteriia; Eggerthellales; Eggerthellaceae;
OC   Cryptobacterium.
OX   NCBI_TaxID=469378 {ECO:0000313|EMBL:ACU94628.1, ECO:0000313|Proteomes:UP000000954};
RN   [1] {ECO:0000313|EMBL:ACU94628.1, ECO:0000313|Proteomes:UP000000954}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700683 / DSM 15641 / 12-3
RC   {ECO:0000313|Proteomes:UP000000954};
RX   PubMed=21304644; DOI=10.40456/sigs.12260;
RA   Mavrommatis K., Pukall R., Rohde C., Chen F., Sims D., Brettin T.,
RA   Kuske C., Detter J.C., Han C., Lapidus A., Copeland A., Glavina Del Rio T.,
RA   Nolan M., Lucas S., Tice H., Cheng J.F., Bruce D., Goodwin L., Pitluck S.,
RA   Ovchinnikova G., Pati A., Ivanova N., Chen A., Palaniappan K., Chain P.,
RA   D'haeseleer P., Goker M., Bristow J., Eisen J.A., Markowitz V.,
RA   Hugenholtz P., Rohde M., Klenk H.P., Kyrpides N.C.;
RT   "Complete genome sequence of Cryptobacterium curtum type strain (12-3).";
RL   Stand. Genomic Sci. 1:93-100(2009).
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}.
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DR   EMBL; CP001682; ACU94628.1; -; Genomic_DNA.
DR   RefSeq; WP_012803314.1; NC_013170.1.
DR   AlphaFoldDB; C7MNY8; -.
DR   STRING; 469378.Ccur_09300; -.
DR   KEGG; ccu:Ccur_09300; -.
DR   eggNOG; COG1158; Bacteria.
DR   HOGENOM; CLU_016377_2_0_11; -.
DR   OMA; TERATDM; -.
DR   OrthoDB; 9805197at2; -.
DR   Proteomes; UP000000954; Chromosome.
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; 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; PF07497; Rho_RNA_bind; 1.
DR   SMART; SM00382; AAA; 1.
DR   SMART; SM00357; CSP; 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}; Reference proteome {ECO:0000313|Proteomes:UP000000954};
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          259..332
FT                   /note="Rho RNA-BD"
FT                   /evidence="ECO:0000259|PROSITE:PS51856"
FT   REGION          1..213
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        14..46
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        150..165
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        166..213
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         375..380
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01884"
FT   BINDING         387..392
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01884"
FT   BINDING         418
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01884"
SQ   SEQUENCE   638 AA;  70403 MW;  2634C178980B5B9F CRC64;
     MSDSETTDSV PEKPATPTRR KRTTASKSKD ESPSTQTRRR RTGTEDLSDA APSPSRRRRS
     SAADENASAD AASARSTRRA ASKDADQSAP NKVDEGTSPS QPAQQHRRRT RRIETGTDAP
     AAHESAIPAS ERQDSSSTGE RRPKGRVKRH QSQNRFERGD NRSDNRTGNA ARSGTNSSRS
     NGNGNRQQGN GNGQNRRQQR YNRPDNASAS PKLSIEDLSK LKVAELREKA DALDIDWKGL
     LKADLVKAVY DATLKKDGFV EAEGVLDVLA DGYGFLRTEG YLPSEHDVYV GTSLIRRQHL
     RKGDRITGQI RPARSGEKYG ALQRLYTVNG IPADEVGERP RFKDLTPVYP DERLVMEHGR
     TSITSRVIDL AAPIGKGQRG LIVSPPKAGK TTVLKQIAAS IAQNNPECHL MCLLVDERPE
     EVTDMQRSVH GEVISSTFDM PAENHIAVAE MVIERAKRLV EMGKDVVILL DSITRLARAY
     NLAQPASGRI LSGGVDSTAL YPPKRFLGAA RNIEFGGSLT ILASALIDTG SKMDEVIFEE
     FKGTGNMELK LDRNLADRRI YPAIDPVASG TRKEDLLLDQ QEAPLIWAVR RILANMNNTE
     RSMDMLIKSL KQTETNQEFL LRTAKKAQGR RLEDNLEL
//
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