ID A0A0E3WUU3_METBA Unreviewed; 431 AA.
AC A0A0E3WUU3;
DT 24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT 24-JUN-2015, sequence version 1.
DT 24-JAN-2024, entry version 42.
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=MSBR3_0432 {ECO:0000313|EMBL:AKB81010.1};
OS Methanosarcina barkeri 3.
OC Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC Methanosarcinales; Methanosarcinaceae; Methanosarcina.
OX NCBI_TaxID=1434107 {ECO:0000313|EMBL:AKB81010.1, ECO:0000313|Proteomes:UP000033066};
RN [1] {ECO:0000313|EMBL:AKB81010.1, ECO:0000313|Proteomes:UP000033066}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=3 {ECO:0000313|EMBL:AKB81010.1,
RC ECO:0000313|Proteomes:UP000033066};
RA Henriksen J.R., Luke J., Reinhart S., Benedict M.N., Youngblut N.D.,
RA Metcalf M.E., Whitaker R.J., Metcalf W.W.;
RT "Methanogenic archaea and the global carbon cycle.";
RL Submitted (JUL-2014) 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; CP009517; AKB81010.1; -; Genomic_DNA.
DR RefSeq; WP_048106215.1; NZ_CP009517.1.
DR AlphaFoldDB; A0A0E3WUU3; -.
DR STRING; 1434107.MSBR3_0432; -.
DR GeneID; 24787894; -.
DR KEGG; mbak:MSBR3_0432; -.
DR PATRIC; fig|1434107.4.peg.567; -.
DR HOGENOM; CLU_028780_2_0_2; -.
DR OrthoDB; 10348at2157; -.
DR Proteomes; UP000033066; 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 SMART; SM00981; THUMP; 1.
DR SUPFAM; SSF55120; Pseudouridine synthase; 1.
DR SUPFAM; SSF143437; THUMP domain-like; 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 59..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 395
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01893"
SQ SEQUENCE 431 AA; 48189 MW; ABE45CA71DC512AC CRC64;
MDVLDISKKI LHEGPICDNC LGRQFAKLST GLSNRERGQS LKLALVLEGD RIYKAEKDDS
LLKELAPCSA FARKALGTEG EDEQCWVCLD QFKKLDEWAD EAVKALEGLE YSTFLVGTKV
SGLLSENEEM LWAEAGTAYA EQLKTELNRE VGKRIAEKVQ KDVDFENPDI TITLDLAKNK
LDLQLRSVYI LGRYRKLLRG IPQTRWPCRK CKGKGCERCN FTGKQYQESV DELIKGPVTE
VFQAADTAFH GSGREDIDAL MLGSGRPFVV EAKSPVKRST DLEKLMQNIN EKAAGKVEVR
ELSFTGKDMI ETLKSSKADK TYKLKVTFKE PVSEEKLKSS LEALNGIEIS QQTPKRVVHR
RADLVRKRHV HSIRLDELTD EGYAYITVNC EGGLYVKELI SGDEGRTNPS LSGLLGVPAL
VEDLDVVNVD I
//
