ID A0A099Y1F8_9FLAO Unreviewed; 296 AA.
AC A0A099Y1F8;
DT 07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT 07-JAN-2015, sequence version 1.
DT 24-JAN-2024, entry version 36.
DE RecName: Full=Pseudouridine synthase {ECO:0000256|RuleBase:RU003887};
DE EC=5.4.99.- {ECO:0000256|RuleBase:RU003887};
GN ORFNames=PHEL85_1124 {ECO:0000313|EMBL:KGL64079.1};
OS Polaribacter sp. Hel1_85.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae.
OX NCBI_TaxID=1250005 {ECO:0000313|EMBL:KGL64079.1, ECO:0000313|Proteomes:UP000029991};
RN [1] {ECO:0000313|EMBL:KGL64079.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Hel1_85 {ECO:0000313|EMBL:KGL64079.1};
RA Xing P., Hahnke R.L., Unfried F., Markert S., Huang S., Barbeyron T.,
RA Harder J., Becher D., Schweder T., Gloenk F.O., Amann R.I., Teeling H.;
RT "Niches of two polysaccharide-degrading Polaribacter strains isolated from
RT the North Sea during a spring diatom bloom.";
RL ISME J. 0:0-0(2014).
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:KGL64079.1}.
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DR EMBL; JPDS01000001; KGL64079.1; -; Genomic_DNA.
DR RefSeq; WP_036822138.1; NZ_JPDS01000001.1.
DR AlphaFoldDB; A0A099Y1F8; -.
DR STRING; 1250005.PHEL85_1124; -.
DR eggNOG; COG1187; Bacteria.
DR OrthoDB; 9807213at2; -.
DR Proteomes; UP000029991; Unassembled WGS sequence.
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; cd02554; PseudoU_synth_RluF; 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:SF2; S4 RNA-BINDING DOMAIN-CONTAINING PROTEIN; 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:KGL64079.1};
KW RNA-binding {ECO:0000256|PROSITE-ProRule:PRU00182}.
FT DOMAIN 9..66
FT /note="RNA-binding S4"
FT /evidence="ECO:0000259|SMART:SM00363"
FT REGION 236..296
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 260..274
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 276..296
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 296 AA; 33767 MW; B28D3B921B9EBB36 CRC64;
MDKNNQQSTN LNKYISSSGI CSRREAERFI NEGRVTINGK PTQLGNRVGK KDVVKLDGRI
VKPKNTTLYI ALNKPVGIVS TTDEREPNNI VKHVNYPERL FPIGRLDKPS EGLIFLTNDG
DIVNKILRAG NNHEKEYFVT VNKSITDAFI QKMGSGIPIL GTVTKNCLVE KVSDKIFKIV
LTQGLNRQIR RMCEYLDYEV TKLKRTRIMN VELGYLQAGD WRELTEEEMK EINKMISTSS
KTEEASVVKE KPKAQKPKRK QAPTKNDFNK KSASFRKSSP KNKKKKSGFS SKKKRW
//