ID A0A1I4NTR8_9EURY Unreviewed; 430 AA.
AC A0A1I4NTR8;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 22.
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 ORFNames=SAMN04488696_0254 {ECO:0000313|EMBL:SFM18826.1};
OS Methanolobus profundi.
OC Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC Methanosarcinales; Methanosarcinaceae; Methanolobus.
OX NCBI_TaxID=487685 {ECO:0000313|EMBL:SFM18826.1, ECO:0000313|Proteomes:UP000198535};
RN [1] {ECO:0000313|EMBL:SFM18826.1, ECO:0000313|Proteomes:UP000198535}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Mob M {ECO:0000313|EMBL:SFM18826.1,
RC ECO:0000313|Proteomes:UP000198535};
RA de Groot N.N.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
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; FOUJ01000001; SFM18826.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I4NTR8; -.
DR STRING; 487685.SAMN04488696_0254; -.
DR OrthoDB; 10348at2157; -.
DR Proteomes; UP000198535; Unassembled WGS sequence.
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.
DR PROSITE; PS51165; THUMP; 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, ECO:0000256|PROSITE-
KW ProRule:PRU00529};
KW tRNA processing {ECO:0000256|ARBA:ARBA00022694, ECO:0000256|HAMAP-
KW Rule:MF_01893}.
FT DOMAIN 69..187
FT /note="THUMP"
FT /evidence="ECO:0000259|PROSITE:PS51165"
FT ACT_SITE 256
FT /note="Nucleophile"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01893"
FT BINDING 322
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01893"
FT BINDING 394
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01893"
SQ SEQUENCE 430 AA; 47584 MW; 4F982354CC2EDB74 CRC64;
MSILETAKKI IEEGPICDHC MGRQFAKLST GLTNVERGQA IKLSMVMEGD ALYKENGDES
LLEELAHSSA YARKSLKISG EDEKCWVCLG IFEDLDVWAD RAIESIGDRE YSTFLVGTKV
SGLIGENEEI LWSECGITQA EQFKTEMNRE VGKLIAARTG KEVAFERPDI LVTMDIAEGT
TSVQVKSLYI QGRYRKLVRG IPQTRWPCRS CGGRGCEQCD NTGKQYPESV DELIGVEVVK
AANGTDTKFH GAGREDIDAL MLGTGRPFVV EALDPTIRSV DVWELEKKIN EFAGGKVEVE
GLKIVEKAVI ETLKSSKADK VYNLKVTFKE PVSTDKLEGA INSLIGVQIH QRTPQRVAHR
RADLVRKRYV HNIQLKEKTD EYAIIEVHCD GGLYVKELTS GDDGRTEPSI TGNLGIQATV
AELNVVNVDI
//
