ID A6GNL7_9BURK Unreviewed; 458 AA.
AC A6GNL7;
DT 24-JUL-2007, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2007, sequence version 1.
DT 08-NOV-2023, entry version 81.
DE RecName: Full=Pseudouridine synthase {ECO:0000256|RuleBase:RU003887};
DE EC=5.4.99.- {ECO:0000256|RuleBase:RU003887};
GN ORFNames=LMED105_02043 {ECO:0000313|EMBL:EDM84305.1};
OS Limnobacter sp. MED105.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Limnobacter.
OX NCBI_TaxID=391597 {ECO:0000313|EMBL:EDM84305.1, ECO:0000313|Proteomes:UP000010322};
RN [1] {ECO:0000313|EMBL:EDM84305.1, ECO:0000313|Proteomes:UP000010322}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MED105 {ECO:0000313|EMBL:EDM84305.1,
RC ECO:0000313|Proteomes:UP000010322};
RA Pinhassi J., Pedros-Alio C., Ferriera S., Johnson J., Kravitz S.,
RA Beeson K., Sutton G., Rogers Y.-H., Friedman R., Frazier M., Venter J.C.;
RL Submitted (JUN-2007) 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 -!- 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:EDM84305.1}.
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DR EMBL; ABCT01000003; EDM84305.1; -; Genomic_DNA.
DR RefSeq; WP_008248747.1; NZ_ABCT01000003.1.
DR AlphaFoldDB; A6GNL7; -.
DR STRING; 391597.LMED105_02043; -.
DR Proteomes; UP000010322; 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; cd02556; PseudoU_synth_RluB; 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 Reference proteome {ECO:0000313|Proteomes:UP000010322};
KW RNA-binding {ECO:0000256|PROSITE-ProRule:PRU00182}.
FT DOMAIN 69..126
FT /note="RNA-binding S4"
FT /evidence="ECO:0000259|SMART:SM00363"
FT REGION 1..30
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 314..345
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 371..458
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 10..27
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 458 AA; 49560 MW; 70BA3408E0C6DFC1 CRC64;
MRTNKRKATE TPDTNPIPEQ VSVSVDSESH DLEWGEVLDQ VEGLKSEEGG GASKNRSKLN
VRLDPELAPK LHKVLADSGM GSRREMEELI VAGRVSVNAE PAHLGQRVLP TDQVRVNGKL
IQRKNKSKPP RVLIYHKPAG EIVSMDDPQG RTTVFQKLPK ISNGKWIAVG RLDFNTEGLL
LFTSSGELAN RLMHPRYEVQ REYAVRILGE LSEEQRQQLL TGIQLEDGPA KFLYVDAAGG
EGANRWYKVG LKEGRNREVR RMFEACNLTV SRLIRTRFGD IMMPSTLKRG RHMEMEALEA
MSYMQSLGLK VDESAQEGAI RRDKKNIGSK NNKRRNGQPL IDPGLAFTTP TQTYLTVSGA
TAAAALSNQN NLSSAGGSAR RNGGGGDRNG NRAGANGNGA AAPAGKFAGA GKRPSGPRNA
GPRSGGPSAG RGPGRGNEGG NGAAQKPQQR RRRKAPAV
//
