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Database: UniProt/SWISS-PROT
Entry: TRUA_METMJ
LinkDB: TRUA_METMJ
Original site: TRUA_METMJ 
ID   TRUA_METMJ              Reviewed;         270 AA.
AC   A3CXX4;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   20-MAR-2007, sequence version 1.
DT   19-FEB-2014, entry version 45.
DE   RecName: Full=tRNA pseudouridine synthase A;
DE            EC=5.4.99.12;
DE   AltName: Full=tRNA pseudouridine(38-40) synthase;
DE   AltName: Full=tRNA pseudouridylate synthase I;
DE   AltName: Full=tRNA-uridine isomerase I;
GN   Name=truA; OrderedLocusNames=Memar_2301;
OS   Methanoculleus marisnigri (strain ATCC 35101 / DSM 1498 / JR1).
OC   Archaea; Euryarchaeota; Methanomicrobia; Methanomicrobiales;
OC   Methanomicrobiaceae; Methanoculleus.
OX   NCBI_TaxID=368407;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35101 / DSM 1498 / JR1;
RX   PubMed=21304656; DOI=10.4056/sigs.32535;
RA   Anderson I.J., Sieprawska-Lupa M., Lapidus A., Nolan M., Copeland A.,
RA   Glavina Del Rio T., Tice H., Dalin E., Barry K., Saunders E., Han C.,
RA   Brettin T., Detter J.C., Bruce D., Mikhailova N., Pitluck S.,
RA   Hauser L., Land M., Lucas S., Richardson P., Whitman W.B.,
RA   Kyrpides N.C.;
RT   "Complete genome sequence of Methanoculleus marisnigri Romesser et al.
RT   1981 type strain JR1.";
RL   Stand. Genomic Sci. 1:189-196(2009).
CC   -!- FUNCTION: Formation of pseudouridine at positions 38, 39 and 40 in
CC       the anticodon stem and loop of transfer RNAs (By similarity).
CC   -!- CATALYTIC ACTIVITY: tRNA uridine(38-40) = tRNA pseudouridine(38-
CC       40).
CC   -!- SIMILARITY: Belongs to the tRNA pseudouridine synthase TruA
CC       family.
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DR   EMBL; CP000562; ABN58224.1; -; Genomic_DNA.
DR   RefSeq; YP_001048206.1; NC_009051.1.
DR   ProteinModelPortal; A3CXX4; -.
DR   STRING; 368407.Memar_2301; -.
DR   EnsemblBacteria; ABN58224; ABN58224; Memar_2301.
DR   GeneID; 4848144; -.
DR   KEGG; mem:Memar_2301; -.
DR   eggNOG; COG0101; -.
DR   HOGENOM; HOG000248673; -.
DR   KO; K06173; -.
DR   OMA; GKSFLWE; -.
DR   ProtClustDB; PRK14589; -.
DR   BioCyc; MMAR368407:GH7L-2354-MONOMER; -.
DR   GO; GO:0009982; F:pseudouridine synthase activity; IEA:UniProtKB-HAMAP.
DR   GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR   GO; GO:0031119; P:tRNA pseudouridine synthesis; IEA:UniProtKB-HAMAP.
DR   Gene3D; 3.30.70.580; -; 1.
DR   Gene3D; 3.30.70.660; -; 1.
DR   HAMAP; MF_00171; TruA; 1.
DR   InterPro; IPR020103; PsdUridine_synth_cat_dom.
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; PsdUridine_synth_TruA_N.
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;
KW   Complete proteome; Isomerase; tRNA processing.
FT   CHAIN         1    270       tRNA pseudouridine synthase A.
FT                                /FTId=PRO_1000017115.
FT   ACT_SITE     55     55       Nucleophile (By similarity).
FT   BINDING     110    110       Substrate (By similarity).
SQ   SEQUENCE   270 AA;  30287 MW;  C33FD09EE5A10A2C CRC64;
     MNLAFRFSYF GDRFFGSQMQ PDLCTVEGEF IGACRLLRLF DDWREANFAT AGRTDRGVHA
     RSQVCSFLTD KPERAIEALN RVLPADIWCT GWAEAPDGFH PRYSAVSRTY RYYFSAPGDA
     AAMHEAAQEF LGRHDFSAFA RAGDRNPERR ILASRVFIDG EFAVFEVTGE SFLWNMVRCM
     ATMLGRVGRG EAEAGEIARL LTGPVERRVA AAPPEGLILW DIDYGIPFTP LPIDAGSSRH
     LGDRHRYHVL MAKISAHLAQ DHRQPDTPGI
//
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