ID A0A0E3NT53_9EURY Unreviewed; 431 AA.
AC A0A0E3NT53;
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=MSWH1_1371 {ECO:0000313|EMBL:AKB21642.1};
OS Methanosarcina sp. WH1.
OC Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC Methanosarcinales; Methanosarcinaceae; Methanosarcina.
OX NCBI_TaxID=1434102 {ECO:0000313|EMBL:AKB21642.1, ECO:0000313|Proteomes:UP000033112};
RN [1] {ECO:0000313|EMBL:AKB21642.1, ECO:0000313|Proteomes:UP000033112}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WH1 {ECO:0000313|EMBL:AKB21642.1,
RC ECO:0000313|Proteomes:UP000033112};
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; CP009504; AKB21642.1; -; Genomic_DNA.
DR RefSeq; WP_048127387.1; NZ_CP009504.1.
DR AlphaFoldDB; A0A0E3NT53; -.
DR GeneID; 24837148; -.
DR KEGG; mef:MSWH1_1371; -.
DR PATRIC; fig|1434102.4.peg.1755; -.
DR HOGENOM; CLU_028780_2_0_2; -.
DR Proteomes; UP000033112; 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.
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; 48161 MW; F8F5755BF29A16F9 CRC64;
MDVLEISKKI LHEGPVCDHC MGRQFAKLST GLSNRERGQA MKLALVLEGD RIYKSENDDS
LLKELVPCSA LARKTLRIEG EDEQCWVCLD QFKKLDEWAD KAAKALEGLE YSTFLVGTKV
SGLLSENEEM LWAEAGTAYA EQLKTELNRE VGKRIAEKVD KEVDFENPDI VITLDLATTN
FELQVRSVYV YGRYLKKVRG IPQTRWPCRK CKGRGCESCG FTGKQYPESV DELIKGPVIE
TFEAVDTAFH GSGREDIDAL MLGNGRPFVV EAKSPVKRMA DLEMLTALIN ENAAGKVEVR
DLRFVEKSMI EILKSSKADK TYKLKVTFKE PVSEEKLKSC LESLSGTEIA QQTPKRVVHR
RADLVRKRHV HSITLDELTD NGHAHITVNC EGGLYVKELI SGDEGRTNPS LTGLLGVPAL
VEDLDVVNVE I
//
