PUS10_THEPD
ID PUS10_THEPD Reviewed; 444 AA.
AC A1RX33;
DT 03-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT 06-FEB-2007, sequence version 1.
DT 03-AUG-2022, entry version 66.
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=Tpen_0354;
OS Thermofilum pendens (strain DSM 2475 / Hrk 5).
OC Archaea; Crenarchaeota; Thermoprotei; Thermofilales; Thermofilaceae;
OC Thermofilum.
OX NCBI_TaxID=368408;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 2475 / Hrk 5;
RX PubMed=18263724; DOI=10.1128/jb.01949-07;
RA Anderson I., Rodriguez J., Susanti D., Porat I., Reich C., Ulrich L.E.,
RA Elkins J.G., Mavromatis K., Lykidis A., Kim E., Thompson L.S., Nolan M.,
RA Land M., Copeland A., Lapidus A., Lucas S., Detter C., Zhulin I.B.,
RA Olsen G.J., Whitman W., Mukhopadhyay B., Bristow J., Kyrpides N.;
RT "Genome sequence of Thermofilum pendens reveals an exceptional loss of
RT biosynthetic pathways without genome reduction.";
RL J. Bacteriol. 190:2957-2965(2008).
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; CP000505; ABL77763.1; -; Genomic_DNA.
DR AlphaFoldDB; A1RX33; -.
DR SMR; A1RX33; -.
DR STRING; 368408.Tpen_0354; -.
DR EnsemblBacteria; ABL77763; ABL77763; Tpen_0354.
DR KEGG; tpe:Tpen_0354; -.
DR eggNOG; arCOG01015; Archaea.
DR HOGENOM; CLU_028780_2_0_2; -.
DR OMA; DGGLYIK; -.
DR Proteomes; UP000000641; 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; 2.
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..444
FT /note="tRNA pseudouridine synthase Pus10"
FT /id="PRO_0000407397"
FT ACT_SITE 265
FT /note="Nucleophile"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01893"
FT BINDING 333
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01893"
FT BINDING 405
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01893"
SQ SEQUENCE 444 AA; 50205 MW; 9867C6736B3B0F2F CRC64;
MSTGTSASYK RDNAFYALDK VERILLDGYS LCDACTGRLF GLRGYGLSNT ERGRALKTLL
IMKAFQASPR QADLELLRVL ARTGFEPARE LLKKLSGEDV EVKACSICEG LTGRYYELAL
RAVEEAKSYE FNTFEVGVRI DAEVIRREEE LWRRYGLESA ESIRNEASRE VGKIISKLTG
KEYSRNNSEL LIIVDLSAGA IELHPAPVFV YGRYRKYARG LPQNPWPQPD ERIKFNTSIE
ELIVKPALEL FEAEKAKFHA AGREDIDVRT LGTGRPFVLE IKKPRKRNID LKVLAEKINS
GAGGLIEVLD LAYTDRKTIK KLKSLASIAK KAYVARVKFE KPVDDEKLAE ISKVFSNAVI
NQRTPTRVLH RRVDKLRKKI VYRLEARKIS QDEVEFYLET QGGFYVKEFI HGDNGRTTPS
IAEFLGNNVL SIELDVVSIE ETAA