ID F9P5I3_STRCV Unreviewed; 280 AA.
AC F9P5I3;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 27-MAR-2024, entry version 49.
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=HMPREF1042_0737 {ECO:0000313|EMBL:EGV10964.1};
OS Streptococcus constellatus subsp. pharyngis SK1060 = CCUG 46377.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus; Streptococcus anginosus group.
OX NCBI_TaxID=1035184 {ECO:0000313|EMBL:EGV10964.1, ECO:0000313|Proteomes:UP000003287};
RN [1] {ECO:0000313|EMBL:EGV10964.1, ECO:0000313|Proteomes:UP000003287}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SK1060 {ECO:0000313|EMBL:EGV10964.1,
RC ECO:0000313|Proteomes:UP000003287};
RA Harkins D.M., Madupu R., Durkin A.S., Torralba M., Methe B., Sutton G.G.,
RA Nelson K.E.;
RL Submitted (JUN-2011) to the EMBL/GenBank/DDBJ databases.
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; AFUP01000001; EGV10964.1; -; Genomic_DNA.
DR AlphaFoldDB; F9P5I3; -.
DR eggNOG; COG0130; Bacteria.
DR Proteomes; UP000003287; Unassembled WGS sequence.
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 HAMAP; MF_01080; TruB_bact; 1.
DR InterPro; IPR020103; PsdUridine_synth_cat_dom_sf.
DR InterPro; IPR002501; PsdUridine_synth_N.
DR InterPro; IPR014780; tRNA_psdUridine_synth_TruB.
DR NCBIfam; TIGR00431; TruB; 1.
DR PANTHER; PTHR13767:SF2; PSEUDOURIDYLATE SYNTHASE TRUB1; 1.
DR PANTHER; PTHR13767; TRNA-PSEUDOURIDINE SYNTHASE; 1.
DR Pfam; PF01509; TruB_N; 1.
DR SUPFAM; SSF55120; Pseudouridine synthase; 1.
PE 3: Inferred from homology;
KW Isomerase {ECO:0000256|HAMAP-Rule:MF_01080};
KW tRNA processing {ECO:0000256|HAMAP-Rule:MF_01080}.
FT DOMAIN 11..165
FT /note="Pseudouridine synthase II N-terminal"
FT /evidence="ECO:0000259|Pfam:PF01509"
FT ACT_SITE 26
FT /note="Nucleophile"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01080"
SQ SEQUENCE 280 AA; 30991 MW; FDBC08357B6B0BAE CRC64;
MTSHDAVFKL RKILQTKKIG HGGTLDPDVV GVLPIAVGKA TRLVEFMQDE GKIYEGEVTL
GFSTTTEDAS GEVLAKTPVL APLDAKLVDE AIASLTGLIT QIPPMYSAVK VNGRKLYEYA
RTGEAVEKPK RQVAIYSFER TSPIFYENQT ARFNFRVRCG KGTYIRTLAV DFGVKLGYAS
HMSQLTRTSA AGMLLEEALT LDEIAEQVTV GDFSFLQPLE LGIGDLVKID LTKEQAEDVR
FGRFIDVNSN ETQVAGFFQG KLLAILEKRN KEYKPRKVFL
//
