ID M1XK75_NATM8 Unreviewed; 277 AA.
AC M1XK75;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 43.
DE RecName: Full=tRNA pseudouridine synthase {ECO:0000256|RuleBase:RU003792};
DE EC=5.4.99.12 {ECO:0000256|RuleBase:RU003792};
GN Name=truA {ECO:0000313|EMBL:CCQ35392.1};
GN OrderedLocusNames=Nmlp_1182 {ECO:0000313|EMBL:CCQ35392.1};
OS Natronomonas moolapensis (strain DSM 18674 / CECT 7526 / JCM 14361 /
OS 8.8.11).
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC Haloarculaceae; Natronomonas.
OX NCBI_TaxID=268739 {ECO:0000313|EMBL:CCQ35392.1, ECO:0000313|Proteomes:UP000011867};
RN [1] {ECO:0000313|EMBL:CCQ35392.1, ECO:0000313|Proteomes:UP000011867}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 18674 / JCM 14361 / 8.8.11
RC {ECO:0000313|Proteomes:UP000011867};
RX PubMed=23516216; DOI=10.1128/genomeA.00095-13;
RA Dyall-Smith M.L., Pfeiffer F., Oberwinkler T., Klee K., Rampp M., Palm P.,
RA Gross K., Schuster S.C., Oesterhelt D.;
RT "Genome of the haloarchaeon Natronomonas moolapensis, a neutrophilic member
RT of a previously haloalkaliphilic genus.";
RL Genome Announc. 1:e0009513-e0009513(2013).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=uridine(38/39/40) in tRNA = pseudouridine(38/39/40) in tRNA;
CC Xref=Rhea:RHEA:22376, Rhea:RHEA-COMP:10085, Rhea:RHEA-COMP:10087,
CC ChEBI:CHEBI:65314, ChEBI:CHEBI:65315; EC=5.4.99.12;
CC Evidence={ECO:0000256|RuleBase:RU003792};
CC -!- SIMILARITY: Belongs to the tRNA pseudouridine synthase TruA family.
CC {ECO:0000256|ARBA:ARBA00009375, ECO:0000256|RuleBase:RU003792}.
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DR EMBL; HF582854; CCQ35392.1; -; Genomic_DNA.
DR AlphaFoldDB; M1XK75; -.
DR STRING; 268739.Nmlp_1182; -.
DR KEGG; nmo:Nmlp_1182; -.
DR eggNOG; arCOG04449; Archaea.
DR HOGENOM; CLU_014673_4_2_2; -.
DR OrthoDB; 25720at2157; -.
DR Proteomes; UP000011867; Chromosome.
DR GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR GO; GO:0106029; F:tRNA pseudouridine synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0001522; P:pseudouridine synthesis; IEA:InterPro.
DR GO; GO:0008033; P:tRNA processing; IEA:UniProtKB-KW.
DR Gene3D; 3.30.70.660; Pseudouridine synthase I, catalytic domain, C-terminal subdomain; 1.
DR Gene3D; 3.30.70.580; Pseudouridine synthase I, catalytic domain, N-terminal subdomain; 1.
DR InterPro; IPR020103; PsdUridine_synth_cat_dom_sf.
DR InterPro; IPR001406; PsdUridine_synth_TruA.
DR InterPro; IPR020097; PsdUridine_synth_TruA_a/b_dom.
DR InterPro; IPR020095; PsdUridine_synth_TruA_C.
DR InterPro; IPR020094; TruA/RsuA/RluB/E/F_N.
DR PANTHER; PTHR11142; PSEUDOURIDYLATE SYNTHASE; 1.
DR PANTHER; PTHR11142:SF0; TRNA PSEUDOURIDINE SYNTHASE-LIKE 1; 1.
DR Pfam; PF01416; PseudoU_synth_1; 1.
DR PIRSF; PIRSF001430; tRNA_psdUrid_synth; 1.
DR SUPFAM; SSF55120; Pseudouridine synthase; 1.
PE 3: Inferred from homology;
KW Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000256|RuleBase:RU003792};
KW Reference proteome {ECO:0000313|Proteomes:UP000011867};
KW tRNA processing {ECO:0000256|ARBA:ARBA00022694,
KW ECO:0000256|RuleBase:RU003792}.
FT DOMAIN 137..237
FT /note="Pseudouridine synthase I TruA alpha/beta"
FT /evidence="ECO:0000259|Pfam:PF01416"
FT ACT_SITE 55
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR001430-1"
FT BINDING 109
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001430-2"
SQ SEQUENCE 277 AA; 29574 MW; B72503DA95F493D6 CRC64;
MRAFRLAYDG SGYRGFQRQP HGETVEDELF AALRELGVGF DGGSPAGYAA AGRTDAGVSA
RAQTVAFEAP AWLTPRALDG ELPGAIRAWA SADVEPGFHA THDATERVYK YFLHAPAAET
GAREDVTAVD DGRAREACRR LSAEADFHNF TPDDEGTERA VSVSTRRDGP FLILECRAGG
FARQLVRRLV SVVEAVARGV RDPSFITRAL GPEPLSGPDG IAPAAPAPLV LFGVSYPGVD
FDIDPDALES ARGVFRARRR ERLAAARVAG SLVPDDP
//