ID A5UMY8_METS3 Unreviewed; 401 AA.
AC A5UMY8;
DT 10-JUL-2007, integrated into UniProtKB/TrEMBL.
DT 10-JUL-2007, sequence version 1.
DT 27-MAR-2024, entry version 71.
DE RecName: Full=tRNA pseudouridine synthase Pus10 {ECO:0000256|HAMAP-Rule:MF_01893};
DE EC=5.4.99.25 {ECO:0000256|HAMAP-Rule:MF_01893};
DE AltName: Full=tRNA pseudouridine 54/55 synthase {ECO:0000256|HAMAP-Rule:MF_01893};
DE Short=Psi54/55 synthase {ECO:0000256|HAMAP-Rule:MF_01893};
GN Name=pus10 {ECO:0000256|HAMAP-Rule:MF_01893};
GN OrderedLocusNames=Msm_1361 {ECO:0000313|EMBL:ABQ87566.1};
OS Methanobrevibacter smithii (strain ATCC 35061 / DSM 861 / OCM 144 / PS).
OC Archaea; Euryarchaeota; Methanomada group; Methanobacteria;
OC Methanobacteriales; Methanobacteriaceae; Methanobrevibacter.
OX NCBI_TaxID=420247 {ECO:0000313|EMBL:ABQ87566.1, ECO:0000313|Proteomes:UP000001992};
RN [1] {ECO:0000313|EMBL:ABQ87566.1, ECO:0000313|Proteomes:UP000001992}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35061 / DSM 861 / OCM 144 / PS
RC {ECO:0000313|Proteomes:UP000001992};
RX PubMed=17563350; DOI=10.1073/pnas.0704189104;
RA Samuel B.S., Hansen E.E., Manchester J.K., Coutinho P.M., Henrissat B.,
RA Fulton R., Latreille P., Kim K., Wilson R.K., Gordon J.I.;
RT "Genomic and metabolic adaptations of Methanobrevibacter smithii to the
RT human gut.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:10643-10648(2007).
CC -!- FUNCTION: Responsible for synthesis of pseudouridine from uracil-54 and
CC uracil-55 in the psi GC loop of transfer RNAs. {ECO:0000256|HAMAP-
CC Rule:MF_01893}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=uridine(54) in tRNA = pseudouridine(54) in tRNA;
CC Xref=Rhea:RHEA:57876, Rhea:RHEA-COMP:10193, Rhea:RHEA-COMP:14141,
CC ChEBI:CHEBI:65314, ChEBI:CHEBI:65315; Evidence={ECO:0000256|HAMAP-
CC Rule:MF_01893};
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|HAMAP-Rule:MF_01893};
CC -!- SIMILARITY: Belongs to the pseudouridine synthase Pus10 family.
CC {ECO:0000256|ARBA:ARBA00009652, ECO:0000256|HAMAP-Rule:MF_01893}.
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DR EMBL; CP000678; ABQ87566.1; -; Genomic_DNA.
DR AlphaFoldDB; A5UMY8; -.
DR STRING; 420247.Msm_1361; -.
DR EnsemblBacteria; ABQ87566; ABQ87566; Msm_1361.
DR KEGG; msi:Msm_1361; -.
DR PATRIC; fig|420247.28.peg.1356; -.
DR eggNOG; arCOG01015; Archaea.
DR HOGENOM; CLU_028780_2_0_2; -.
DR Proteomes; UP000001992; Chromosome.
DR GO; GO:0000049; F:tRNA 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 Gene3D; 3.30.70.2510; -; 1.
DR Gene3D; 3.30.70.3190; -; 1.
DR HAMAP; MF_01893; Pus10_arch; 1.
DR InterPro; IPR020103; PsdUridine_synth_cat_dom_sf.
DR InterPro; IPR005912; Pus10.
DR InterPro; IPR039894; Pus10-like.
DR InterPro; IPR048741; Pus10-like_C.
DR InterPro; IPR004114; THUMP_dom.
DR NCBIfam; TIGR01213; pseudo_Pus10arc; 1.
DR PANTHER; PTHR21568:SF0; TRNA PSEUDOURIDINE SYNTHASE PUS10; 1.
DR PANTHER; PTHR21568; UNCHARACTERIZED; 1.
DR Pfam; PF21238; Pus10_C; 1.
DR Pfam; PF02926; THUMP; 1.
DR SUPFAM; SSF55120; Pseudouridine synthase; 1.
PE 3: Inferred from homology;
KW Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000256|HAMAP-Rule:MF_01893};
KW RNA-binding {ECO:0000256|HAMAP-Rule:MF_01893};
KW tRNA processing {ECO:0000256|ARBA:ARBA00022694, ECO:0000256|HAMAP-
KW Rule:MF_01893}.
FT DOMAIN 31..157
FT /note="THUMP"
FT /evidence="ECO:0000259|Pfam:PF02926"
FT DOMAIN 160..398
FT /note="Pus10-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF21238"
FT ACT_SITE 227
FT /note="Nucleophile"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01893"
FT BINDING 295
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01893"
FT BINDING 364
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01893"
SQ SEQUENCE 401 AA; 46270 MW; 367E1E2E82FB3EEA CRC64;
MYDLVKKILK ETNGQICKHC LGRKLSHIVE GRDNINRGEK IFEDLEIPKP ENCVVCGNIF
DKINDELFKK IYDKIDFLNV EFDTFLVGSR IDKQIKTWDD ELSEKFDLDV EPIKKELNRI
IGREIENTLE KEVEFEKQDI VINVDLRKEP KVRIQINPLF IEGKYNKLVR GIPQTKWPCG
KCKGKGCEEC NFTGKQYGES VEELLSEPIL EATNGWQAKF HGAGREDIDV LMLGSGRPFV
LEIKEPKIRK INLDALEEKI NKMTEGKTSY HNLKFCERNR KAEIKVSSSD AYKIYKALVK
CDKPYDRDKL ASLNNLDEIH QQTPLRVLHR RADKVRIKHV HNVSCEIIDD TTFEMTVKTE
GGLYIKELIS GDEDRTKPNV GEVLGVKSIC EQLDVVEVSE K
//
