(data stored in SCRATCH zone)

SWISSPROT: C8W418_DESAS

ID   C8W418_DESAS            Unreviewed;       250 AA.
AC   C8W418;
DT   03-NOV-2009, integrated into UniProtKB/TrEMBL.
DT   03-NOV-2009, sequence version 1.
DT   08-MAY-2019, entry version 68.
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=Dtox_0319 {ECO:0000313|EMBL:ACV61272.1};
OS   Desulfotomaculum acetoxidans (strain ATCC 49208 / DSM 771 / VKM
OS   B-1644) (Desulfofarcimen acetoxidans).
OC   Bacteria; Firmicutes; Clostridia; Clostridiales; Peptococcaceae;
OC   Desulfofarcimen.
OX   NCBI_TaxID=485916 {ECO:0000313|EMBL:ACV61272.1, ECO:0000313|Proteomes:UP000002217};
RN   [1] {ECO:0000313|EMBL:ACV61272.1, ECO:0000313|Proteomes:UP000002217}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 49208 / DSM 771 / VKM B-1644
RC   {ECO:0000313|Proteomes:UP000002217};
RX   PubMed=21304664; DOI=10.4056/sigs.39508;
RA   Spring S., Lapidus A., Schroder M., Gleim D., Sims D., Meincke L.,
RA   Glavina Del Rio T., Tice H., Copeland A., Cheng J.F., Lucas S.,
RA   Chen F., Nolan M., Bruce D., Goodwin L., Pitluck S., Ivanova N.,
RA   Mavromatis K., Mikhailova N., Pati A., Chen A., Palaniappan K.,
RA   Land M., Hauser L., Chang Y.J., Jeffries C.D., Chain P., Saunders E.,
RA   Brettin T., Detter J.C., Goker M., Bristow J., Eisen J.A.,
RA   Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P., Han C.;
RT   "Complete genome sequence of Desulfotomaculum acetoxidans type strain
RT   (5575).";
RL   Stand. Genomic Sci. 1:242-253(2009).
CC   -!- FUNCTION: Formation of pseudouridine at positions 38, 39 and 40 in
CC       the anticodon stem and loop of transfer RNAs. {ECO:0000256|HAMAP-
CC       Rule:MF_00171}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=tRNA uridine(38-40) = tRNA pseudouridine(38-40);
CC         Xref=Rhea:RHEA:22376, Rhea:RHEA-COMP:10085, Rhea:RHEA-
CC         COMP:10087, 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
CC       family. {ECO:0000256|HAMAP-Rule:MF_00171,
CC       ECO:0000256|RuleBase:RU003792, ECO:0000256|SAAS:SAAS00543779}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation
CC       of feature annotation. {ECO:0000256|HAMAP-Rule:MF_00171}.
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DR   EMBL; CP001720; ACV61272.1; -; Genomic_DNA.
DR   RefSeq; WP_015755993.1; NC_013216.1.
DR   STRING; 485916.Dtox_0319; -.
DR   EnsemblBacteria; ACV61272; ACV61272; Dtox_0319.
DR   KEGG; dae:Dtox_0319; -.
DR   eggNOG; ENOG4105DI7; Bacteria.
DR   eggNOG; COG0101; LUCA.
DR   HOGENOM; HOG000248673; -.
DR   KO; K06173; -.
DR   OMA; FLYGMVR; -.
DR   OrthoDB; 1075262at2; -.
DR   BioCyc; DACE485916:G1GFV-334-MONOMER; -.
DR   Proteomes; UP000002217; 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   Gene3D; 3.30.70.660; -; 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   PANTHER; PTHR11142; PTHR11142; 1.
DR   Pfam; PF01416; PseudoU_synth_1; 2.
DR   PIRSF; PIRSF001430; tRNA_psdUrid_synth; 1.
DR   SUPFAM; SSF55120; SSF55120; 1.
DR   TIGRFAMs; TIGR00071; hisT_truA; 1.
PE   3: Inferred from homology;
DR   PRODOM; C8W418.
DR   SWISS-2DPAGE; C8W418.
KW   Complete proteome {ECO:0000313|Proteomes:UP000002217};
KW   Isomerase {ECO:0000256|HAMAP-Rule:MF_00171,
KW   ECO:0000256|RuleBase:RU003792, ECO:0000256|SAAS:SAAS00119851,
KW   ECO:0000313|EMBL:ACV61272.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002217};
KW   tRNA processing {ECO:0000256|HAMAP-Rule:MF_00171,
KW   ECO:0000256|RuleBase:RU003792, ECO:0000256|SAAS:SAAS00427419}.
FT   DOMAIN       12    110       PseudoU_synth_1. {ECO:0000259|Pfam:
FT                                PF01416}.
FT   DOMAIN      151    250       PseudoU_synth_1. {ECO:0000259|Pfam:
FT                                PF01416}.
FT   ACT_SITE     57     57       Nucleophile. {ECO:0000256|HAMAP-Rule:
FT                                MF_00171, ECO:0000256|PIRSR:PIRSR001430-
FT                                1}.
FT   BINDING     116    116       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_00171, ECO:0000256|PIRSR:PIRSR001430-
FT                                2}.
SQ   SEQUENCE   250 AA;  28457 MW;  8BC3254F79D217E6 CRC64;
     MNRGRNIKVI LAYDGTNYHG FQIQKGKRLP TIQGVLQREL SHLAKETITV TTAGRTDSGV
     HARGQVFNFF TGNWQIPVDR VIYALNSVLP PDIRALSAEE VDLGFHARYS ALAKTYCYYI
     SRDQIVSPFT RLYSYQYNYP LDLDDMRQAV LHITGEHDFK SFMASGSLVK STIRTIYQID
     LIEKDKMLIF TFRGNGFLYH MVRIITGTLL QVGTGKIHYS EIETILKKCD RKSAGATVPA
     LGLFLERVEY
//

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