ID A0A2H5F2V7_9RHOB Unreviewed; 562 AA.
AC A0A2H5F2V7;
DT 28-FEB-2018, integrated into UniProtKB/TrEMBL.
DT 28-FEB-2018, sequence version 1.
DT 24-JAN-2024, entry version 23.
DE RecName: Full=Pseudouridine synthase {ECO:0000256|RuleBase:RU003887};
DE EC=5.4.99.- {ECO:0000256|RuleBase:RU003887};
GN ORFNames=CX676_18235 {ECO:0000313|EMBL:AUH65857.1};
OS Paracoccus zhejiangensis.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Paracoccus.
OX NCBI_TaxID=1077935 {ECO:0000313|EMBL:AUH65857.1, ECO:0000313|Proteomes:UP000234530};
RN [1] {ECO:0000313|EMBL:AUH65857.1, ECO:0000313|Proteomes:UP000234530}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=J6 {ECO:0000313|EMBL:AUH65857.1,
RC ECO:0000313|Proteomes:UP000234530};
RX PubMed=23653121; DOI=10.1007/s10482-013-9932-2;
RA Wu Z.G., Zhang D.F., Liu Y.L., Wang F., Jiang X., Li C., Li S.P., Hong Q.,
RA Li W.J.;
RT "Paracoccus zhejiangensis sp. nov., isolated from activated sludge in
RT wastewater-treatment system.";
RL Antonie Van Leeuwenhoek 104:123-128(2013).
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}.
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DR EMBL; CP025430; AUH65857.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2H5F2V7; -.
DR KEGG; pzh:CX676_18235; -.
DR OrthoDB; 9807213at2; -.
DR Proteomes; UP000234530; Chromosome.
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 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:UP000234530};
KW RNA-binding {ECO:0000256|PROSITE-ProRule:PRU00182}.
FT DOMAIN 18..76
FT /note="RNA-binding S4"
FT /evidence="ECO:0000259|SMART:SM00363"
FT REGION 251..562
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 253..506
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 562 AA; 63222 MW; 4FBF66E34A373EA6 CRC64;
MTDDQTPDSN TDKPADVDRI AKVIARAGVA SRRDAERIIL EGRVTVNGEK ITSPALDVRP
TDRITVDGKP LDAPQETRLW MYYKPVGLVT SEADEKGRQT IFDALPRDLP RVMTVGRLDL
NSEGLLLLTN DGELKRRLEL PATGWLRRYR VRVNGTPTDL TFDPLRRGVT IDGEDFQPME
VRLDSQQGAN AWLTVGIREG RNREIRRAMT HIGLQVNRLI RIGYGPFKLT GMEENEVREV
KRKVLRDQLG GLLTGETEDE KPRDFRARGA ESGPRRSAAD GERKPRFGKP DGERKPFGRN
DDRGERRDGG KPFARREDGD RKPWAKREDG DRKPFARRED GDRKPWAKRE DGDRKPFARR
EDGDRKPFAR REDGDRKPWT KREEGDRKPF ARREDGDRKP FARREDGDRK PWAKREDGDR
KPYAKREDGD RKPWAKREDG DRKPFARRED GDKKPWVKRD RSDEGFKPRG EGGFKPRGEG
GFKPRGEGGF KPRGEGDFKP RGEGGFKPRG EGFNSGGPRK GGFSGGPAGG KGRPAAGKGP
RPGGGKPGGG RPGGGKPRAP RG
//