ID A0A0M8MFJ4_9FLAO Unreviewed; 347 AA.
AC A0A0M8MFJ4;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE RecName: Full=Pseudouridine synthase {ECO:0000256|RuleBase:RU362028};
DE EC=5.4.99.- {ECO:0000256|RuleBase:RU362028};
GN ORFNames=AM493_00700 {ECO:0000313|EMBL:KOS04727.1};
OS Flavobacterium akiainvivens.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Flavobacterium.
OX NCBI_TaxID=1202724 {ECO:0000313|EMBL:KOS04727.1, ECO:0000313|Proteomes:UP000037755};
RN [1] {ECO:0000313|EMBL:KOS04727.1, ECO:0000313|Proteomes:UP000037755}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IK-1 {ECO:0000313|EMBL:KOS04727.1,
RC ECO:0000313|Proteomes:UP000037755};
RA Wan X., Hou S., Saito J., Donachie S.;
RT "Whole genome sequence of Flavobacterium akiainvivens IK-1T, from decaying
RT Wikstroemia oahuensis, an endemic Hawaiian shrub.";
RL Submitted (AUG-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Responsible for synthesis of pseudouridine from uracil.
CC {ECO:0000256|RuleBase:RU362028}.
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|RuleBase:RU362028};
CC -!- SIMILARITY: Belongs to the pseudouridine synthase RluA family.
CC {ECO:0000256|ARBA:ARBA00010876, ECO:0000256|RuleBase:RU362028}.
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:KOS04727.1}.
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DR EMBL; LIYD01000005; KOS04727.1; -; Genomic_DNA.
DR RefSeq; WP_054405759.1; NZ_LIYD01000005.1.
DR AlphaFoldDB; A0A0M8MFJ4; -.
DR STRING; 1202724.AM493_00700; -.
DR PATRIC; fig|1202724.3.peg.136; -.
DR OrthoDB; 9807829at2; -.
DR Proteomes; UP000037755; 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; cd02869; PseudoU_synth_RluA_like; 1.
DR CDD; cd00165; S4; 1.
DR Gene3D; 3.30.2350.10; Pseudouridine synthase; 1.
DR Gene3D; 3.10.290.10; RNA-binding S4 domain; 1.
DR InterPro; IPR020103; PsdUridine_synth_cat_dom_sf.
DR InterPro; IPR006224; PsdUridine_synth_RluA-like_CS.
DR InterPro; IPR006225; PsdUridine_synth_RluC/D.
DR InterPro; IPR006145; PsdUridine_synth_RsuA/RluA.
DR InterPro; IPR002942; S4_RNA-bd.
DR InterPro; IPR036986; S4_RNA-bd_sf.
DR NCBIfam; TIGR00005; rluA_subfam; 1.
DR PANTHER; PTHR21600; MITOCHONDRIAL RNA PSEUDOURIDINE SYNTHASE; 1.
DR PANTHER; PTHR21600:SF44; PSEUDOU_SYNTH_2 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; PS01129; PSI_RLU; 1.
DR PROSITE; PS50889; S4; 1.
PE 3: Inferred from homology;
KW Isomerase {ECO:0000256|RuleBase:RU362028};
KW Reference proteome {ECO:0000313|Proteomes:UP000037755};
KW RNA-binding {ECO:0000256|PROSITE-ProRule:PRU00182}.
FT DOMAIN 30..89
FT /note="RNA-binding S4"
FT /evidence="ECO:0000259|SMART:SM00363"
FT ACT_SITE 153
FT /evidence="ECO:0000256|PIRSR:PIRSR606225-1"
SQ SEQUENCE 347 AA; 39861 MW; B235B4511BA6FA6D CRC64;
MNKPIVEIDA ENEELYEHYR FEAGKGQQPL RVDKFLMNLV ENATRNKIQK AAEAGNIYIN
DVAVKSNHKV KANDIVRVLM EHPPYEYLLE PENIPLNIPY EDDQLLIVNK EPGMVVHPGH
GNYSGTLVNA LAYHFENLPM NSSERPGLVH RIDKDTSGLL VIAKTEQAMT YLTQQFADKT
SEREYIALVW GNVKEDEGTI EGNIDRHPKD RMQMAVFPDG DQGKHAVTHY KVLERFGYVT
LVSCRLETGR THQIRVHMKY IGHTLFNDAR YGGDAILKGT TFTKYKQFID NCFKILPRQA
LHAKTLGFEH PVTKEFMRFD SEVPADMVEC LEKWRVYAKS HNAEDEE
//