ID B3U4L2_9BACT Unreviewed; 420 AA.
AC B3U4L2;
DT 02-SEP-2008, integrated into UniProtKB/TrEMBL.
DT 02-SEP-2008, sequence version 1.
DT 27-MAR-2024, entry version 87.
DE RecName: Full=Pseudouridine synthase {ECO:0000256|RuleBase:RU003887};
DE EC=5.4.99.- {ECO:0000256|RuleBase:RU003887};
GN Name=rluB {ECO:0000313|EMBL:ACE75579.1};
GN ORFNames=NIDE1423 {ECO:0000313|EMBL:CBK41172.1};
OS Nitrospira defluvii.
OC Bacteria; Nitrospirota; Nitrospiria; Nitrospirales; Nitrospiraceae;
OC Nitrospira.
OX NCBI_TaxID=330214 {ECO:0000313|EMBL:ACE75579.1};
RN [1] {ECO:0000313|EMBL:ACE75579.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=18459973; DOI=10.1111/j.1462-2920.2008.01646.x;
RA Maixner F., Wagner M., Lucker S., Pelletier E., Schmitz-Esser S., Hace K.,
RA Spieck E., Konrat R., Le Paslier D., Daims H.;
RT "Environmental genomics reveals a functional chlorite dismutase in the
RT nitrite-oxidizing bacterium 'Candidatus Nitrospira defluvii'.";
RL Environ. Microbiol. 10:3043-3056(2008).
RN [2] {ECO:0000313|EMBL:CBK41172.1, ECO:0000313|Proteomes:UP000001660}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=20624973; DOI=10.1073/pnas.1003860107;
RA Lucker S., Wagner M., Maixner F., Pelletier E., Koch H., Vacherie B.,
RA Rattei T., Sinninghe Damste J., Spieck E., Le Paslier D., Daims H.;
RT "A Nitrospira metagenome illuminates the physiology and evolution of
RT globally important nitrite-oxidizing bacteria.";
RL Proc. Natl. Acad. Sci. U.S.A. 0:13479-13484(2010).
RN [3] {ECO:0000313|EMBL:CBK41172.1}
RP NUCLEOTIDE SEQUENCE.
RA Genoscope - CEA;
RL Submitted (MAR-2010) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the pseudouridine synthase RsuA family.
CC {ECO:0000256|ARBA:ARBA00008348, ECO:0000256|RuleBase:RU003887}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; EU559167; ACE75579.1; -; Genomic_DNA.
DR EMBL; FP929003; CBK41172.1; -; Genomic_DNA.
DR AlphaFoldDB; B3U4L2; -.
DR STRING; 330214.NIDE1423; -.
DR KEGG; nde:NIDE1423; -.
DR eggNOG; COG1187; Bacteria.
DR HOGENOM; CLU_024979_1_0_0; -.
DR OrthoDB; 9807213at2; -.
DR Proteomes; UP000001660; 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; cd02870; PseudoU_synth_RsuA_like; 1.
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:ACE75579.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000001660};
KW RNA-binding {ECO:0000256|PROSITE-ProRule:PRU00182}.
FT DOMAIN 3..64
FT /note="RNA-binding S4"
FT /evidence="ECO:0000259|SMART:SM00363"
FT REGION 245..420
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 274..288
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 289..308
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 378..400
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 420 AA; 46150 MW; 6F76F3C634B8F4B0 CRC64;
MDVRLQKLIA GTGLASRRKA EELITSGRVT INGSVVKELG TKVDPARDHV KVDGKHLRAA
QPYVYLILNK PKNVMSTLDD PEGRPTVKDL LHGVTVRVFP VGRLDFDSEG LMLLTNHGDL
AQALLHPRYH VPKTYLIKVK GVLDDAKIEA LERGVKLEDG FTAPAKVKKV SRAESNSWLE
VTIHEGRKHQ VKRMVEAVGH SVIKLVRVRM GPLLLGDLAP REYRFLTDRE ANRLRELVED
RVARAERPEL DASGKPTRWM PPTEPAPPRP PKPERSGRGP KSQRSERGPR SQRSLAGSKP
SRSGRGNTRR PMSPGAKFRR PAKGVGFQRT QAGPIPQGAD RGPGSRPTGS DQKIQRTQPG
GGFQRPRASA KPQGPGRGTT VRRSSPGQNF QQNRRGGSSA SRPGQRGPAG KSRPSTRRRA
//
