PUS10_METST
ID PUS10_METST Reviewed; 407 AA.
AC Q2NE45;
DT 03-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT 07-FEB-2006, sequence version 1.
DT 03-AUG-2022, entry version 74.
DE RecName: Full=tRNA pseudouridine synthase Pus10 {ECO:0000255|HAMAP-Rule:MF_01893};
DE EC=5.4.99.25 {ECO:0000255|HAMAP-Rule:MF_01893};
DE AltName: Full=tRNA pseudouridine 54/55 synthase {ECO:0000255|HAMAP-Rule:MF_01893};
DE Short=Psi54/55 synthase {ECO:0000255|HAMAP-Rule:MF_01893};
GN Name=pus10 {ECO:0000255|HAMAP-Rule:MF_01893}; OrderedLocusNames=Msp_1541;
OS Methanosphaera stadtmanae (strain ATCC 43021 / DSM 3091 / JCM 11832 /
OS MCB-3).
OC Archaea; Euryarchaeota; Methanomada group; Methanobacteria;
OC Methanobacteriales; Methanobacteriaceae; Methanosphaera.
OX NCBI_TaxID=339860;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43021 / DSM 3091 / JCM 11832 / MCB-3;
RX PubMed=16385054; DOI=10.1128/jb.188.2.642-658.2006;
RA Fricke W.F., Seedorf H., Henne A., Kruer M., Liesegang H., Hedderich R.,
RA Gottschalk G., Thauer R.K.;
RT "The genome sequence of Methanosphaera stadtmanae reveals why this human
RT intestinal archaeon is restricted to methanol and H2 for methane formation
RT and ATP synthesis.";
RL J. Bacteriol. 188:642-658(2006).
CC -!- FUNCTION: Responsible for synthesis of pseudouridine from uracil-54 and
CC uracil-55 in the psi GC loop of transfer RNAs. {ECO:0000255|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:0000255|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:0000255|HAMAP-Rule:MF_01893};
CC -!- SIMILARITY: Belongs to the pseudouridine synthase Pus10 family.
CC {ECO:0000255|HAMAP-Rule:MF_01893}.
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DR EMBL; CP000102; ABC57908.1; -; Genomic_DNA.
DR RefSeq; WP_011407107.1; NC_007681.1.
DR AlphaFoldDB; Q2NE45; -.
DR SMR; Q2NE45; -.
DR STRING; 339860.Msp_1541; -.
DR PRIDE; Q2NE45; -.
DR EnsemblBacteria; ABC57908; ABC57908; Msp_1541.
DR GeneID; 41326117; -.
DR KEGG; mst:Msp_1541; -.
DR eggNOG; arCOG01015; Archaea.
DR HOGENOM; CLU_028780_2_0_2; -.
DR OMA; DGGLYIK; -.
DR OrthoDB; 61936at2157; -.
DR Proteomes; UP000001931; 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 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; IPR004114; THUMP_dom.
DR PANTHER; PTHR21568; PTHR21568; 1.
DR Pfam; PF02926; THUMP; 1.
DR SUPFAM; SSF55120; SSF55120; 1.
DR TIGRFAMs; TIGR01213; pseudo_Pus10arc; 1.
PE 3: Inferred from homology;
KW Isomerase; Reference proteome; RNA-binding; tRNA processing.
FT CHAIN 1..407
FT /note="tRNA pseudouridine synthase Pus10"
FT /id="PRO_0000407391"
FT ACT_SITE 232
FT /note="Nucleophile"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01893"
FT BINDING 300
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01893"
FT BINDING 369
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01893"
SQ SEQUENCE 407 AA; 47445 MW; FEC798DC947FA70D CRC64;
MTEKEYNTRQ TQNYALCPKC LSRIYRNPKD RDNSIIPLIN NTQKCSICNN LLLNEDKIFK
LILKKIKMLK IEFDTFLIAT QINNQTITKN QKEIYKITNY HGNNDIKHQI RRDISRLIEE
KLGKTYDYKN PEVVIMVKIR KKPYKHNPYP EISNVNIFID SNPIFIEGKY RKLVRGIPQT
KWPCTHCKGK GCEACDYTGQ QYKDTVEDLI SREILPMTNG NTTKFHGSGR EDIDVRMLGE
GRPFVIEVKH PFKRKIDLKF LRVLVNSHSD GKIEINDLKY VTKERKASIK NSSVESYKIY
SAIAEFENGV TSKDIYNIEK LKTIDQRTPI RVEHRRADLI RTREIKNIEV ERINSKKLHL
IIKCQGGLYI KELISGDNNR TKPSVSSITN NQAECTQLDV LKVHIPE