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Database: UniProt
Entry: G2NMD1_STREK
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Original site: G2NMD1_STREK 
ID   G2NMD1_STREK            Unreviewed;       301 AA.
AC   G2NMD1;
DT   16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT   16-NOV-2011, sequence version 1.
DT   27-MAR-2024, entry version 71.
DE   RecName: Full=tRNA pseudouridine synthase B {ECO:0000256|HAMAP-Rule:MF_01080};
DE            EC=5.4.99.25 {ECO:0000256|HAMAP-Rule:MF_01080};
DE   AltName: Full=tRNA pseudouridine(55) synthase {ECO:0000256|HAMAP-Rule:MF_01080};
DE            Short=Psi55 synthase {ECO:0000256|HAMAP-Rule:MF_01080};
DE   AltName: Full=tRNA pseudouridylate synthase {ECO:0000256|HAMAP-Rule:MF_01080};
DE   AltName: Full=tRNA-uridine isomerase {ECO:0000256|HAMAP-Rule:MF_01080};
GN   Name=truB {ECO:0000256|HAMAP-Rule:MF_01080};
GN   ORFNames=SACTE_4883 {ECO:0000313|EMBL:AEN12709.1};
OS   Streptomyces sp. (strain SirexAA-E / ActE).
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=862751 {ECO:0000313|EMBL:AEN12709.1, ECO:0000313|Proteomes:UP000001397};
RN   [1] {ECO:0000313|EMBL:AEN12709.1, ECO:0000313|Proteomes:UP000001397}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SirexAA-E / ActE {ECO:0000313|Proteomes:UP000001397};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA   Peters L., Ovchinnikova G., Davenport K., Detter J.C., Han C., Tapia R.,
RA   Land M., Hauser L., Kyrpides N., Ivanova N., Pagani I., Adams A., Raffa K.,
RA   Adams S., Book A., Currie C., Woyke T.;
RT   "Complete sequence of Streptomyces sp. SirexAA-E.";
RL   Submitted (AUG-2011) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:AEN12709.1, ECO:0000313|Proteomes:UP000001397}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SirexAA-E / ActE {ECO:0000313|Proteomes:UP000001397};
RX   PubMed=24710170; DOI=10.1371/journal.pone.0094166;
RA   Takasuka T.E., Acheson J.F., Bianchetti C.M., Prom B.M., Bergeman L.F.,
RA   Book A.J., Currie C.R., Fox B.G.;
RT   "Biochemical properties and atomic resolution structure of a
RT   proteolytically processed beta-mannanase from cellulolytic Streptomyces sp.
RT   SirexAA-E.";
RL   PLoS ONE 9:e94166-E94166(2014).
CC   -!- FUNCTION: Responsible for synthesis of pseudouridine from uracil-55 in
CC       the psi GC loop of transfer RNAs. {ECO:0000256|HAMAP-Rule:MF_01080}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=uridine(55) in tRNA = pseudouridine(55) in tRNA;
CC         Xref=Rhea:RHEA:42532, Rhea:RHEA-COMP:10101, Rhea:RHEA-COMP:10102,
CC         ChEBI:CHEBI:65314, ChEBI:CHEBI:65315; EC=5.4.99.25;
CC         Evidence={ECO:0000256|ARBA:ARBA00000385, ECO:0000256|HAMAP-
CC         Rule:MF_01080};
CC   -!- SIMILARITY: Belongs to the pseudouridine synthase TruB family. Type 1
CC       subfamily. {ECO:0000256|ARBA:ARBA00005642, ECO:0000256|HAMAP-
CC       Rule:MF_01080}.
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DR   EMBL; CP002993; AEN12709.1; -; Genomic_DNA.
DR   RefSeq; WP_014048660.1; NC_015953.1.
DR   AlphaFoldDB; G2NMD1; -.
DR   STRING; 862751.SACTE_4883; -.
DR   KEGG; ssx:SACTE_4883; -.
DR   PATRIC; fig|862751.12.peg.5062; -.
DR   eggNOG; COG0130; Bacteria.
DR   HOGENOM; CLU_032087_0_0_11; -.
DR   OrthoDB; 9802309at2; -.
DR   Proteomes; UP000001397; Chromosome.
DR   GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR   GO; GO:0106029; F:tRNA pseudouridine synthase activity; IEA:UniProtKB-EC.
DR   GO; GO:0031119; P:tRNA pseudouridine synthesis; IEA:UniProtKB-UniRule.
DR   CDD; cd02573; PseudoU_synth_EcTruB; 1.
DR   Gene3D; 3.30.2350.10; Pseudouridine synthase; 1.
DR   Gene3D; 2.30.130.10; PUA domain; 1.
DR   HAMAP; MF_01080; TruB_bact; 1.
DR   InterPro; IPR020103; PsdUridine_synth_cat_dom_sf.
DR   InterPro; IPR002501; PsdUridine_synth_N.
DR   InterPro; IPR015947; PUA-like_sf.
DR   InterPro; IPR036974; PUA_sf.
DR   InterPro; IPR015225; tRNA_psdUridine_synth_fam2_C.
DR   InterPro; IPR014780; tRNA_psdUridine_synth_TruB.
DR   InterPro; IPR032819; TruB_C.
DR   NCBIfam; TIGR00431; TruB; 1.
DR   PANTHER; PTHR13767:SF2; PSEUDOURIDYLATE SYNTHASE TRUB1; 1.
DR   PANTHER; PTHR13767; TRNA-PSEUDOURIDINE SYNTHASE; 1.
DR   Pfam; PF09142; TruB_C; 1.
DR   Pfam; PF16198; TruB_C_2; 1.
DR   Pfam; PF01509; TruB_N; 1.
DR   SUPFAM; SSF55120; Pseudouridine synthase; 1.
DR   SUPFAM; SSF88697; PUA domain-like; 1.
PE   3: Inferred from homology;
KW   Isomerase {ECO:0000256|HAMAP-Rule:MF_01080};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001397};
KW   tRNA processing {ECO:0000256|HAMAP-Rule:MF_01080}.
FT   DOMAIN          33..189
FT                   /note="Pseudouridine synthase II N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF01509"
FT   DOMAIN          190..230
FT                   /note="tRNA pseudouridylate synthase B C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF16198"
FT   DOMAIN          245..300
FT                   /note="tRNA pseudouridine synthase II TruB subfamily 2 C-
FT                   terminal"
FT                   /evidence="ECO:0000259|Pfam:PF09142"
FT   ACT_SITE        47
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01080"
SQ   SEQUENCE   301 AA;  31811 MW;  5A7DEDAE7A94142A CRC64;
     MTQNKQDKTP DGLVVVDKPA GFTSHDVVAK MRGIARTRRV GHAGTLDPMA TGVLVLGVER
     ATKLLGHLAL TEKEYLGTIR LGQDTVTDDA EGEITSSTDA SGVTREAVDA GIAALTGAIM
     QVPSKVSAIK IDGKRSYARV RGGEEFEIPA RPVTVSSFRV YDVREAVAED GTPVLDLVVS
     VVCSSGTYIR ALARDLGAGL GVGGHLTALR RTRVGPYGID AARTLDQHQE ELTVMPVAEA
     AASAFPRWDV DEKRARLLLN GVRVDMPAYP PGPVGVFGPD GAFLVLVEEQ KGKAKSLAVF
     A
//
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