ID Q2KBZ0_RHIEC Unreviewed; 628 AA.
AC Q2KBZ0;
DT 07-MAR-2006, integrated into UniProtKB/TrEMBL.
DT 07-MAR-2006, sequence version 1.
DT 27-MAR-2024, entry version 124.
DE RecName: Full=Pseudouridine synthase {ECO:0000256|RuleBase:RU003887};
DE EC=5.4.99.- {ECO:0000256|RuleBase:RU003887};
GN Name=rluB {ECO:0000313|EMBL:ABC89646.1};
GN OrderedLocusNames=RHE_CH00835 {ECO:0000313|EMBL:ABC89646.1};
OS Rhizobium etli (strain CFN 42 / ATCC 51251).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Rhizobiaceae; Rhizobium/Agrobacterium group; Rhizobium.
OX NCBI_TaxID=347834 {ECO:0000313|EMBL:ABC89646.1, ECO:0000313|Proteomes:UP000001936};
RN [1] {ECO:0000313|EMBL:ABC89646.1, ECO:0000313|Proteomes:UP000001936}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CFN 42 / ATCC 51251 {ECO:0000313|Proteomes:UP000001936};
RX PubMed=16505379; DOI=10.1073/pnas.0508502103;
RA Gonzalez V., Santamaria R.I., Bustos P., Hernandez-Gonzalez I.,
RA Medrano-Soto A., Moreno-Hagelsieb G., Janga S.C., Ramirez M.A.,
RA Jimenez-Jacinto V., Collado-Vides J., Davila G.;
RT "The partitioned Rhizobium etli genome: genetic and metabolic redundancy in
RT seven interacting replicons.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:3834-3839(2006).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a uridine in RNA = a pseudouridine in RNA;
CC Xref=Rhea:RHEA:48348, Rhea:RHEA-COMP:12068, Rhea:RHEA-COMP:12069,
CC ChEBI:CHEBI:65314, ChEBI:CHEBI:65315;
CC Evidence={ECO:0000256|ARBA:ARBA00000073};
CC -!- SIMILARITY: Belongs to the pseudouridine synthase RsuA family.
CC {ECO:0000256|ARBA:ARBA00008348, ECO:0000256|RuleBase:RU003887}.
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DR EMBL; CP000133; ABC89646.1; -; Genomic_DNA.
DR RefSeq; WP_011424184.1; NC_007761.1.
DR AlphaFoldDB; Q2KBZ0; -.
DR KEGG; ret:RHE_CH00835; -.
DR eggNOG; COG1187; Bacteria.
DR HOGENOM; CLU_024979_1_0_5; -.
DR OrthoDB; 9807213at2; -.
DR Proteomes; UP000001936; Chromosome.
DR GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0120159; F:rRNA pseudouridine synthase activity; IEA:UniProt.
DR GO; GO:0000455; P:enzyme-directed rRNA pseudouridine synthesis; IEA:UniProt.
DR CDD; cd00165; S4; 1.
DR Gene3D; 3.30.70.1560; Alpha-L RNA-binding motif; 1.
DR Gene3D; 3.30.70.580; Pseudouridine synthase I, catalytic domain, N-terminal subdomain; 1.
DR Gene3D; 3.10.290.10; RNA-binding S4 domain; 1.
DR InterPro; IPR042092; PsdUridine_s_RsuA/RluB/E/F_cat.
DR InterPro; IPR020103; PsdUridine_synth_cat_dom_sf.
DR InterPro; IPR006145; PsdUridine_synth_RsuA/RluA.
DR InterPro; IPR000748; PsdUridine_synth_RsuA/RluB/E/F.
DR InterPro; IPR018496; PsdUridine_synth_RsuA/RluB_CS.
DR InterPro; IPR002942; S4_RNA-bd.
DR InterPro; IPR036986; S4_RNA-bd_sf.
DR InterPro; IPR020094; TruA/RsuA/RluB/E/F_N.
DR NCBIfam; TIGR00093; pseudouridine synthase; 1.
DR PANTHER; PTHR47683; PSEUDOURIDINE SYNTHASE FAMILY PROTEIN-RELATED; 1.
DR PANTHER; PTHR47683:SF3; RIBOSOMAL LARGE SUBUNIT PSEUDOURIDINE SYNTHASE B; 1.
DR Pfam; PF00849; PseudoU_synth_2; 1.
DR Pfam; PF01479; S4; 1.
DR SMART; SM00363; S4; 1.
DR SUPFAM; SSF55174; Alpha-L RNA-binding motif; 1.
DR SUPFAM; SSF55120; Pseudouridine synthase; 1.
DR PROSITE; PS01149; PSI_RSU; 1.
DR PROSITE; PS50889; S4; 1.
PE 3: Inferred from homology;
KW Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000256|RuleBase:RU003887};
KW Lyase {ECO:0000313|EMBL:ABC89646.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000001936};
KW RNA-binding {ECO:0000256|PROSITE-ProRule:PRU00182}.
FT DOMAIN 52..109
FT /note="RNA-binding S4"
FT /evidence="ECO:0000259|SMART:SM00363"
FT REGION 1..49
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 303..628
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..15
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 311..369
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 410..558
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 628 AA; 68937 MW; F8658F28759ABE5F CRC64;
MTSKDKPKRP GAKPYSRDGG TKAGLKAGDA KPAKAATAPP AAAETESEAK AERISKVMAR
AGVASRRDIE RMIMEGRVTL NGKVLDTPVV NVTLADRIEV DGVPIRGIER TRLWLYHKPA
GLVTTNADPE GRPTVFDNLP EELPRVMSIG RLDINTEGLL LLTNDGGLAR ALELPATGWL
RRYRVRAHGE IDQEALDKLK DGIAVDGVLY GSIEATLDRT QGSNVWITMG LREGKNREIK
NVLGALGLDV NRLIRISYGP FQLGDLPEGH VVEVRGRTLR DQLGPRLIEE AKANFDAPIY
NAPAVAAEEE TEAAAPEKRE RPRRDEDKRE RALSRLDTKR DDRRGAGRRD DDRRDGGRKD
DDKPKRSQPP GQRRSANVWM APGARPLGEK AAAKAAKNAQ AARRRGEQPA AKTNAFDRIE
DRPRTQINRV REEDGEWIRS SEQPRRKDED EGFSRKRSFG DRPSRGERPF GDKPRGDRRP
RADGDERPRA ARASAGEGRS ERPRGDRPFG DRPSRGDRPF GDKPRGDRRP REEGDERPRA
ARSFAGEGRS ERPRGERSFA GKSAGGKPSS DKPRGKGFGA KPGGSKSFSG KPKGKPGSDR
PGGDRPAGGL SRGGARGKGM TRGADRRR
//
