ID Q1YH15_AURMS Unreviewed; 497 AA.
AC Q1YH15;
DT 02-MAY-2006, integrated into UniProtKB/TrEMBL.
DT 02-MAY-2006, sequence version 1.
DT 13-SEP-2023, entry version 88.
DE RecName: Full=Pseudouridine synthase {ECO:0000256|RuleBase:RU003887};
DE EC=5.4.99.- {ECO:0000256|RuleBase:RU003887};
GN ORFNames=SI859A1_00424 {ECO:0000313|EMBL:EAS49764.1};
OS Aurantimonas manganoxydans (strain ATCC BAA-1229 / DSM 21871 / SI85-9A1).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Aurantimonadaceae; Aurantimonas.
OX NCBI_TaxID=287752 {ECO:0000313|EMBL:EAS49764.1, ECO:0000313|Proteomes:UP000000321};
RN [1] {ECO:0000313|EMBL:EAS49764.1, ECO:0000313|Proteomes:UP000000321}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SI85-9A1 {ECO:0000313|EMBL:EAS49764.1,
RC ECO:0000313|Proteomes:UP000000321};
RX PubMed=18344346; DOI=10.1128/AEM.01656-07;
RA Dick G.J., Podell S., Johnson H.A., Rivera-Espinoza Y., Bernier-Latmani R.,
RA McCarthy J.K., Torpey J.W., Clement B.G., Gaasterland T., Tebo B.M.;
RT "Genomic insights into Mn(II) oxidation by the marine alphaproteobacterium
RT Aurantimonas sp. strain SI85-9A1.";
RL Appl. Environ. Microbiol. 74:2646-2658(2008).
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:EAS49764.1}.
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DR EMBL; AAPJ01000004; EAS49764.1; -; Genomic_DNA.
DR AlphaFoldDB; Q1YH15; -.
DR HOGENOM; CLU_024979_1_0_5; -.
DR BioCyc; AURANTIMONAS:SI859A1_00424-MONOMER; -.
DR Proteomes; UP000000321; 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 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:UP000000321};
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..68
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 314..497
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 9..68
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 324..339
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 347..415
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 497 AA; 54370 MW; 51E1B14AD5B23281 CRC64;
MFSHGGARGD KGEGAKPRSF GRLQHDAPKG DRTERSGGER RPVRDDRPKR APRDDRAPRA
ETESAVGEMR IAKRLARAGI ASRRDAEGMI ADGRVKLNGK VLDTPAVVVT ASDRIEIDNA
PLPAIERTRL WLFHKAAGTV TTNRDPEGRP TIFDRLPSDM PRVLTVGRLD INTEGLLLLT
NDGGLARILE LPATGWLRRY RVRAHGAITQ ARLDELRQGI AIDGVFYGAI EATMDREQGS
NVWLTLGLRE GKNREVKKVL AHLGLEVNRL IRLSFGPFQL GDLKEGSVQE IKGRMLRDQL
GERLIEESGA DFDAPVAKPF SNRPVEAERT ERPKKADEWI SASETAPNKK RVREAKREDA
LGRLDTRAGR PERNDRGDRK PYGERPAKRF EGPKKPYGDR DAAGGRDDAA SPPKRPIDAP
KRSANVWMAP GARPQGTKKA LGSQAGRPDR GPSRGERPSG PSAPRGGGGK PGAGRPPRTG
GDAPQRPGRP PRPPRKG
//
