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Database: UniProt
Entry: A0A0Q4L6U4_9SPHN
LinkDB: A0A0Q4L6U4_9SPHN
Original site: A0A0Q4L6U4_9SPHN 
ID   A0A0Q4L6U4_9SPHN        Unreviewed;       501 AA.
AC   A0A0Q4L6U4;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   24-JAN-2024, entry version 35.
DE   RecName: Full=Pseudouridine synthase {ECO:0000256|RuleBase:RU003887};
DE            EC=5.4.99.- {ECO:0000256|RuleBase:RU003887};
GN   ORFNames=ASF00_00105 {ECO:0000313|EMBL:KQN32169.1};
OS   Sphingomonas sp. Leaf34.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC   Sphingomonadaceae; Sphingomonas.
OX   NCBI_TaxID=1736216 {ECO:0000313|EMBL:KQN32169.1, ECO:0000313|Proteomes:UP000051932};
RN   [1] {ECO:0000313|EMBL:KQN32169.1, ECO:0000313|Proteomes:UP000051932}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Leaf34 {ECO:0000313|EMBL:KQN32169.1,
RC   ECO:0000313|Proteomes:UP000051932};
RA   Gilbert D.G.;
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KQN32169.1, ECO:0000313|Proteomes:UP000051932}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Leaf34 {ECO:0000313|EMBL:KQN32169.1,
RC   ECO:0000313|Proteomes:UP000051932};
RA   Schulze-Lefert P.;
RT   "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL   Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
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}.
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:KQN32169.1}.
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DR   EMBL; LMLC01000001; KQN32169.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0Q4L6U4; -.
DR   Proteomes; UP000051932; Unassembled WGS sequence.
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   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   RNA-binding {ECO:0000256|PROSITE-ProRule:PRU00182}.
FT   DOMAIN          3..40
FT                   /note="RNA-binding S4"
FT                   /evidence="ECO:0000259|Pfam:PF01479"
FT   DOMAIN          60..192
FT                   /note="Pseudouridine synthase RsuA/RluA-like"
FT                   /evidence="ECO:0000259|Pfam:PF00849"
FT   REGION          255..501
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        262..282
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        303..321
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        374..392
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        424..450
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   501 AA;  53538 MW;  C27E24D8F9455DD4 CRC64;
     MAKLLARAGI ASRRDIERMI AEGRVALNGS TLDTPATILR NLAGVTVDGD PVEAPSAARL
     FLYHKPTGLL VTERDPAGRT TIYDRLPQDL PRLVPVGRLD LNTEGLLLMT TDGGLKRQLE
     LPATGVERAY RARAYGNITQ PQLEELIEGI EIEGVRYGSI NANIERRTGA NVWIEMILTE
     GKNREVRRVL EHLGLQVSRL IRTRYGPFVL GDLPPGQIGE VLQHDVVAFQ KELAKGRPEG
     PGARANIGIS ASAGAGAGIG ARSNQRGSNA PRPASTGHSA STGRPAFGAR PAPGGARTPA
     RTPYSAPASS GFASTSAPTE RPSRPARPER IRPTAAMQRG DVNDPWARPD ARNAARPTGT
     HHARPTSGET SKPYARQERA DRGEELSTSP KIKHFRAAKP PRDRAAPSRV GAGGTVTPRR
     GDTPQRQEQP RGFRPQADDS RGRSSLDKRA ARSAAGRPGA EPRPMRDAPA RPERGSRPTA
     PGKGPSGGRG HPPRAPRGGK R
//
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