ID E8RUC2_ASTEC Unreviewed; 658 AA.
AC E8RUC2;
DT 05-APR-2011, integrated into UniProtKB/TrEMBL.
DT 05-APR-2011, sequence version 1.
DT 27-MAR-2024, entry version 66.
DE RecName: Full=Pseudouridine synthase {ECO:0000256|RuleBase:RU003887};
DE EC=5.4.99.- {ECO:0000256|RuleBase:RU003887};
GN OrderedLocusNames=Astex_3461 {ECO:0000313|EMBL:ADU15093.1};
OS Asticcacaulis excentricus (strain ATCC 15261 / DSM 4724 / KCTC 12464 /
OS NCIMB 9791 / VKM B-1370 / CB 48).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Caulobacterales;
OC Caulobacteraceae; Asticcacaulis.
OX NCBI_TaxID=573065 {ECO:0000313|EMBL:ADU15093.1, ECO:0000313|Proteomes:UP000001492};
RN [1] {ECO:0000313|Proteomes:UP000001492}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 15261 / DSM 4724 / KCTC 12464 / NCIMB 9791 / VKM B-1370 /
RC CB 48 {ECO:0000313|Proteomes:UP000001492};
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L.,
RA Pitluck S., Teshima H., Davenport K., Detter J.C., Han C., Tapia R.,
RA Land M., Hauser L., Jeffries C., Kyrpides N., Ivanova N., Ovchinnikova G.,
RA Brun Y.V., Woyke T.;
RT "Complete sequence of chromosome 2 of Asticcacaulis excentricus CB 48.";
RL Submitted (DEC-2010) to the EMBL/GenBank/DDBJ databases.
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; CP002396; ADU15093.1; -; Genomic_DNA.
DR AlphaFoldDB; E8RUC2; -.
DR STRING; 573065.Astex_3461; -.
DR KEGG; aex:Astex_3461; -.
DR eggNOG; COG1187; Bacteria.
DR HOGENOM; CLU_024979_1_0_5; -.
DR Proteomes; UP000001492; Chromosome 2.
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:UP000001492};
KW RNA-binding {ECO:0000256|PROSITE-ProRule:PRU00182}.
FT DOMAIN 46..104
FT /note="RNA-binding S4"
FT /evidence="ECO:0000259|SMART:SM00363"
FT REGION 1..46
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 284..342
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 359..658
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 300..342
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 359..613
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 658 AA; 74241 MW; F2AAE63D9E53C17B CRC64;
MMSEDNNMPE SATPSEVVAN DAPKKSYVKK PAGKKGPPPK PARPPERIAK VLARAGLASR
REVERLIGLG KIAVNGRLLD TPATTVSPDD LITVEGKPIR KAEPTRVWRY HKPVGLMTTH
QDPQGRPTVF NSLPQELPRV ISVGRLDINS EGLLLLTNDG ELARALELPT TGWTRVYRVR
ALGRTTQEAL DTLKTGVTVE GVQYGPIEAK LDKAQEKADG RANLWITVSL NEGKNREVRK
VLDSLGLKVN RLIRLAYGPF QLGDIEPGEV EEIGPRVVRE LLGDKIDPRN LPSENETQTR
TPMRLRRTDG EGAPRTGRRG GGDRFASKSE GREERRERPL SRDEAFRRKY EAKEFGERDF
DERPRFEGDG QARDRRPERE EREWTPRAER PRRDFNTGEF RPRAEGSFKP RGDRNFGDKP
RFDKPRGERP SGDRPQRDFK PRGEGDFKPR GERNFGDKPR FDKPRGERPA GDRPQRDFKP
RGEGDFKPRG ERNFGDKPRF DKPRGERPAG DRPQRDFKPR GEGDFKPRGE RNFGDKPRFD
KPRGERPAGD RPQRDFKPRG EGNFKPRGER NFGDKPRFDK PRGERPAGDR PQRDFKPRGE
GDFKPRGERS FGDRPAGRSF GGKPGGGKSF GGKPGGFKSG GRPGGFAGKD ASRKPRPE
//
