GenomeNet

Database: UniProt
Entry: A0A139X9V8_9CYAN
LinkDB: A0A139X9V8_9CYAN
Original site: A0A139X9V8_9CYAN 
ID   A0A139X9V8_9CYAN        Unreviewed;       275 AA.
AC   A0A139X9V8;
DT   11-MAY-2016, integrated into UniProtKB/TrEMBL.
DT   11-MAY-2016, sequence version 1.
DT   24-JAN-2024, entry version 35.
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   ORFNames=WA1_21505 {ECO:0000313|EMBL:KYC41465.1};
OS   Scytonema hofmannii PCC 7110.
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Nostocales; Scytonemataceae;
OC   Scytonema.
OX   NCBI_TaxID=128403 {ECO:0000313|EMBL:KYC41465.1, ECO:0000313|Proteomes:UP000076925};
RN   [1] {ECO:0000313|EMBL:KYC41465.1, ECO:0000313|Proteomes:UP000076925}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PCC 7110 {ECO:0000313|EMBL:KYC41465.1,
RC   ECO:0000313|Proteomes:UP000076925};
RX   PubMed=23221676; DOI=10.1093/gbe/evs117;
RA   Dagan T., Roettger M., Stucken K., Landan G., Koch R., Major P.,
RA   Gould S.B., Goremykin V.V., Rippka R., Tandeau de Marsac N., Gugger M.,
RA   Lockhart P.J., Allen J.F., Brune I., Maus I., Puhler A., Martin W.F.;
RT   "Genomes of Stigonematalean cyanobacteria (subsection V) and the evolution
RT   of oxygenic photosynthesis from prokaryotes to plastids.";
RL   Genome Biol. Evol. 5:31-44(2013).
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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KYC41465.1}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; ANNX02000021; KYC41465.1; -; Genomic_DNA.
DR   RefSeq; WP_026135261.1; NZ_KQ976354.1.
DR   AlphaFoldDB; A0A139X9V8; -.
DR   STRING; 128403.WA1_21505; -.
DR   OrthoDB; 9811823at2; -.
DR   Proteomes; UP000076925; Unassembled WGS sequence.
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:UP000076925};
KW   tRNA processing {ECO:0000256|ARBA:ARBA00022694, ECO:0000256|HAMAP-
KW   Rule:MF_00171}.
FT   DOMAIN          18..114
FT                   /note="Pseudouridine synthase I TruA alpha/beta"
FT                   /evidence="ECO:0000259|Pfam:PF01416"
FT   DOMAIN          154..256
FT                   /note="Pseudouridine synthase I TruA alpha/beta"
FT                   /evidence="ECO:0000259|Pfam:PF01416"
FT   ACT_SITE        62
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00171,
FT                   ECO:0000256|PIRSR:PIRSR001430-1"
FT   BINDING         120
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00171,
FT                   ECO:0000256|PIRSR:PIRSR001430-2"
SQ   SEQUENCE   275 AA;  31541 MW;  733F16EB9A3799A7 CRC64;
     MLDSQQPKPR TYRVALVIQY LGTHFHGWQR QKQQRTVQEE IEKAIATVLG YPVTLYGAGR
     TDAGVHAAAQ VAHFNVTSPI PACKWAVILN SYLPNDILIR ASAEVNDRWH ARFSAIYRRY
     RYTLYTEGLP NLFASAVSWH YYIDPLDESL MQAALKPLIG HHHLAAFHRA NSVRKHSWVD
     IQAAECYRNG SFLHIEIQAN GFLYGMVRLL VGMLVQVGSG QRTPENFTDL WKYERREEVK
     HAAPSQGLCL LRVGYPDFPF PPEIWFDTQP KFVFS
//
DBGET integrated database retrieval system