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Database: UniProt
Entry: A0A0H3C6A3_CAUVN
LinkDB: A0A0H3C6A3_CAUVN
Original site: A0A0H3C6A3_CAUVN 
ID   A0A0H3C6A3_CAUVN        Unreviewed;       412 AA.
AC   A0A0H3C6A3;
DT   16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT   16-SEP-2015, sequence version 1.
DT   24-JAN-2024, entry version 41.
DE   RecName: Full=Pseudouridine synthase {ECO:0000256|RuleBase:RU003887};
DE            EC=5.4.99.- {ECO:0000256|RuleBase:RU003887};
GN   OrderedLocusNames=CCNA_00230 {ECO:0000313|EMBL:ACL93697.2};
OS   Caulobacter vibrioides (strain NA1000 / CB15N) (Caulobacter crescentus).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Caulobacterales;
OC   Caulobacteraceae; Caulobacter.
OX   NCBI_TaxID=565050 {ECO:0000313|EMBL:ACL93697.2, ECO:0000313|Proteomes:UP000001364};
RN   [1] {ECO:0000313|EMBL:ACL93697.2, ECO:0000313|Proteomes:UP000001364}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NA1000 / CB15N {ECO:0000313|Proteomes:UP000001364};
RX   PubMed=20472802; DOI=10.1128/JB.00255-10;
RA   Marks M.E., Castro-Rojas C.M., Teiling C., Du L., Kapatral V.,
RA   Walunas T.L., Crosson S.;
RT   "The genetic basis of laboratory adaptation in Caulobacter crescentus.";
RL   J. Bacteriol. 192:3678-3688(2010).
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; CP001340; ACL93697.2; -; Genomic_DNA.
DR   RefSeq; WP_024265520.1; NC_011916.1.
DR   RefSeq; YP_002515605.2; NC_011916.1.
DR   AlphaFoldDB; A0A0H3C6A3; -.
DR   GeneID; 7330276; -.
DR   KEGG; ccs:CCNA_00230; -.
DR   PATRIC; fig|565050.3.peg.226; -.
DR   HOGENOM; CLU_024979_1_0_5; -.
DR   OrthoDB; 9807213at2; -.
DR   PhylomeDB; A0A0H3C6A3; -.
DR   Proteomes; UP000001364; Chromosome.
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; cd02556; PseudoU_synth_RluB; 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: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   Lyase {ECO:0000313|EMBL:ACL93697.2};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001364};
KW   RNA-binding {ECO:0000256|PROSITE-ProRule:PRU00182}.
FT   DOMAIN          26..83
FT                   /note="RNA-binding S4"
FT                   /evidence="ECO:0000259|SMART:SM00363"
FT   REGION          1..25
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          267..412
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..24
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        299..325
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   412 AA;  43962 MW;  3B53484BB0506358 CRC64;
     MTKPHDPLYE PHLDGQDGDL DGGPGERVAK ALARAGVASR REVERLIEAG RVAINGKVLT
     TPAVKVAPGD FLTVDGQLVA EREPTRIFRY HKPTGLMTTH NDPKGRPTVF GALPKDLPRL
     ISVGRLDLNS EGLLLLTNDG ELSRALETPS NAWVRRYRAR AFGDTTQAKL DKLKDGVTIE
     GVTYGAIEAK LDKAHEKAGG GKNVWITVSL SEGKNREVRK VLESIGLKVN RLIRLSYGPF
     ALGTLAAGQI EEVGPRVIRE LLEGVVSPEN MPTGDRPKFA GIANPTKAPG TEGGGELQRR
     GAPRADRAVI LDTPEKPEKP VYKPGWAKPK KKASPHGPPK GAGKGPAKGP AKAKRPAKSI
     ESKFIDIGKP AARGKPAAPR PGAKPADGAA RRLSERPGKP TTRSGPPRGP KR
//
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