PUS10_METKA
ID PUS10_METKA Reviewed; 436 AA.
AC Q8TUV7;
DT 03-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 71.
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=MK1646;
OS Methanopyrus kandleri (strain AV19 / DSM 6324 / JCM 9639 / NBRC 100938).
OC Archaea; Euryarchaeota; Methanopyri; Methanopyrales; Methanopyraceae;
OC Methanopyrus.
OX NCBI_TaxID=190192;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AV19 / DSM 6324 / JCM 9639 / NBRC 100938;
RX PubMed=11930014; DOI=10.1073/pnas.032671499;
RA Slesarev A.I., Mezhevaya K.V., Makarova K.S., Polushin N.N.,
RA Shcherbinina O.V., Shakhova V.V., Belova G.I., Aravind L., Natale D.A.,
RA Rogozin I.B., Tatusov R.L., Wolf Y.I., Stetter K.O., Malykh A.G.,
RA Koonin E.V., Kozyavkin S.A.;
RT "The complete genome of hyperthermophile Methanopyrus kandleri AV19 and
RT monophyly of archaeal methanogens.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:4644-4649(2002).
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; AE009439; AAM02859.1; -; Genomic_DNA.
DR AlphaFoldDB; Q8TUV7; -.
DR SMR; Q8TUV7; -.
DR STRING; 190192.MK1646; -.
DR PRIDE; Q8TUV7; -.
DR EnsemblBacteria; AAM02859; AAM02859; MK1646.
DR KEGG; mka:MK1646; -.
DR PATRIC; fig|190192.8.peg.1809; -.
DR HOGENOM; CLU_028780_2_0_2; -.
DR OMA; DGGLYIK; -.
DR Proteomes; UP000001826; 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..436
FT /note="tRNA pseudouridine synthase Pus10"
FT /id="PRO_0000407389"
FT ACT_SITE 254
FT /note="Nucleophile"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01893"
FT BINDING 322
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01893"
FT BINDING 394
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01893"
SQ SEQUENCE 436 AA; 50019 MW; 10983DC963276DB4 CRC64;
MIDRLREALK RFNPCDSCLG RAFGYGLTGL ENRERGRAIK LYLGMRAHLE GEEETLELLA
RSGLEEAAAV LDDPPEPEPC GVCRGVLDKV DEFAEVVACE LKDLEFRGFV VGSRWPEEIR
KAEKELWETL GVEGEPIKRE FNREVGKRVE HLLDVRADPR NPDIEVVFDF RPSLEDPKFE
VHVRPIYVRG RYLKLRRGIP QTKWPCPRCR GAGCPNCDFT GKLYTESVEE LIGMVLKDAF
LAESHKFHAA GREDIDVRML GNGRPFVMEL LYPKRRNVDL KEIEGEINRK VGDDVQVVGL
EYGDPEDVGK VKDLSERSRK RYRAWVKFGK PVPEDKLREV LKGLERSVIE QRTPRRVLHR
RADKVRRKRV HEAKLIEYDG DRAVIEFLCD PGLYVKELIS GDAGRTRPSL AELVEVEAEC
ERLDVIEFLD EGGDRS