ID E4TEH7_CALNY Unreviewed; 248 AA.
AC E4TEH7;
DT 08-FEB-2011, integrated into UniProtKB/TrEMBL.
DT 08-FEB-2011, sequence version 1.
DT 27-MAR-2024, entry version 74.
DE RecName: Full=tRNA pseudouridine synthase A {ECO:0000256|HAMAP-Rule:MF_00171};
DE EC=5.4.99.12 {ECO:0000256|HAMAP-Rule:MF_00171};
DE AltName: Full=tRNA pseudouridine(38-40) synthase {ECO:0000256|HAMAP-Rule:MF_00171};
DE AltName: Full=tRNA pseudouridylate synthase I {ECO:0000256|HAMAP-Rule:MF_00171};
DE AltName: Full=tRNA-uridine isomerase I {ECO:0000256|HAMAP-Rule:MF_00171};
GN Name=truA {ECO:0000256|HAMAP-Rule:MF_00171};
GN OrderedLocusNames=Calni_0390 {ECO:0000313|EMBL:ADR18303.1};
OS Calditerrivibrio nitroreducens (strain DSM 19672 / NBRC 101217 / Yu37-1).
OC Bacteria; Deferribacterota; Deferribacteres; Deferribacterales;
OC Calditerrivibrionaceae.
OX NCBI_TaxID=768670 {ECO:0000313|EMBL:ADR18303.1, ECO:0000313|Proteomes:UP000007039};
RN [1] {ECO:0000313|EMBL:ADR18303.1, ECO:0000313|Proteomes:UP000007039}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 19672 / NBRC 101217 / Yu37-1
RC {ECO:0000313|Proteomes:UP000007039};
RX PubMed=21475587; DOI=10.4056/sigs.1523807;
RA Pitluck S., Sikorski J., Zeytun A., Lapidus A., Nolan M., Lucas S.,
RA Hammon N., Deshpande S., Cheng J.F., Tapia R., Han C., Goodwin L.,
RA Liolios K., Pagani I., Ivanova N., Mavromatis K., Pati A., Chen A.,
RA Palaniappan K., Hauser L., Chang Y.J., Jeffries C.D., Detter J.C.,
RA Brambilla E., Djao O.D., Rohde M., Spring S., Goker M., Woyke T.,
RA Bristow J., Eisen J.A., Markowitz V., Hugenholtz P., Kyrpides N.C.,
RA Klenk H.P., Land M.;
RT "Complete genome sequence of Calditerrivibrio nitroreducens type strain
RT (Yu37-1).";
RL Stand. Genomic Sci. 4:54-62(2011).
CC -!- FUNCTION: Formation of pseudouridine at positions 38, 39 and 40 in the
CC anticodon stem and loop of transfer RNAs. {ECO:0000256|HAMAP-
CC Rule:MF_00171}.
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|HAMAP-Rule:MF_00171,
CC ECO:0000256|RuleBase:RU003792};
CC -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_00171}.
CC -!- SIMILARITY: Belongs to the tRNA pseudouridine synthase TruA family.
CC {ECO:0000256|ARBA:ARBA00009375, ECO:0000256|HAMAP-Rule:MF_00171,
CC ECO:0000256|RuleBase:RU003792}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_00171}.
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DR EMBL; CP002347; ADR18303.1; -; Genomic_DNA.
DR RefSeq; WP_013450519.1; NC_014758.1.
DR AlphaFoldDB; E4TEH7; -.
DR STRING; 768670.Calni_0390; -.
DR KEGG; cni:Calni_0390; -.
DR eggNOG; COG0101; Bacteria.
DR HOGENOM; CLU_014673_0_1_0; -.
DR OrthoDB; 9811823at2; -.
DR Proteomes; UP000007039; 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:0031119; P:tRNA pseudouridine synthesis; IEA:UniProtKB-UniRule.
DR CDD; cd02570; PseudoU_synth_EcTruA; 1.
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 HAMAP; MF_00171; TruA; 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 NCBIfam; TIGR00071; hisT_truA; 1.
DR PANTHER; PTHR11142; PSEUDOURIDYLATE SYNTHASE; 1.
DR PANTHER; PTHR11142:SF0; TRNA PSEUDOURIDINE SYNTHASE-LIKE 1; 1.
DR Pfam; PF01416; PseudoU_synth_1; 2.
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|HAMAP-Rule:MF_00171};
KW Reference proteome {ECO:0000313|Proteomes:UP000007039};
KW tRNA processing {ECO:0000256|ARBA:ARBA00022694, ECO:0000256|HAMAP-
KW Rule:MF_00171}.
FT DOMAIN 12..105
FT /note="Pseudouridine synthase I TruA alpha/beta"
FT /evidence="ECO:0000259|Pfam:PF01416"
FT DOMAIN 149..248
FT /note="Pseudouridine synthase I TruA alpha/beta"
FT /evidence="ECO:0000259|Pfam:PF01416"
FT ACT_SITE 56
FT /note="Nucleophile"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00171,
FT ECO:0000256|PIRSR:PIRSR001430-1"
FT BINDING 114
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00171,
FT ECO:0000256|PIRSR:PIRSR001430-2"
SQ SEQUENCE 248 AA; 28504 MW; CE211330BAD9A1C4 CRC64;
MEPSLYNKKC TVEYDGTEFH GWQFQKGLVT VQSEIEAALS KIYKKQIHII GSGRTDAGVH
ALAQVFNFRA EKYIESEPLN LGLNSLLPRS IIIKKVEDVD VNFHAQKSAK SKTYLYKILN
SELPSAFLRN RVWWVRNSID IEIFSEILSQ FVGTFDFSAM CTMKSLKENS VRTINFINVY
KTEHIINIEI NANGFLHNMV RNIIGTAFFI YRKKLHPSTV MEIIESRDRK KGGPTAPPQG
LYLKEVFY
//
