(data stored in ACNUC7421 zone)

SWISSPROT: D4YXN3_SPHJU

ID   D4YXN3_SPHJU            Unreviewed;       373 AA.
AC   D4YXN3;
DT   15-JUN-2010, integrated into UniProtKB/TrEMBL.
DT   15-JUN-2010, sequence version 1.
DT   07-JUN-2017, entry version 45.
DE   RecName: Full=tRNA-specific 2-thiouridylase MnmA {ECO:0000256|HAMAP-Rule:MF_00144};
DE            EC=2.8.1.13 {ECO:0000256|HAMAP-Rule:MF_00144};
GN   Name=trmU {ECO:0000313|EMBL:BAI95115.1};
GN   Synonyms=mnmA {ECO:0000256|HAMAP-Rule:MF_00144};
GN   OrderedLocusNames=SJA_C1-02810 {ECO:0000313|EMBL:BAI95115.1};
OS   Sphingobium japonicum (strain NBRC 101211 / UT26S).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Sphingomonadales;
OC   Sphingomonadaceae; Sphingobium.
OX   NCBI_TaxID=452662 {ECO:0000313|EMBL:BAI95115.1, ECO:0000313|Proteomes:UP000007753};
RN   [1] {ECO:0000313|EMBL:BAI95115.1, ECO:0000313|Proteomes:UP000007753}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NBRC 101211 / UT26S {ECO:0000313|Proteomes:UP000007753};
RX   PubMed=20817768; DOI=10.1128/JB.00961-10;
RA   Nagata Y., Ohtsubo Y., Endo R., Ichikawa N., Ankai A., Oguchi A.,
RA   Fukui S., Fujita N., Tsuda M.;
RT   "Complete genome sequence of the representative gamma-
RT   hexachlorocyclohexane-degrading bacterium Sphingobium japonicum
RT   UT26.";
RL   J. Bacteriol. 192:5852-5853(2010).
CC   -!- FUNCTION: Catalyzes the 2-thiolation of uridine at the wobble
CC       position (U34) of tRNA, leading to the formation of s(2)U34.
CC       {ECO:0000256|HAMAP-Rule:MF_00144}.
CC   -!- CATALYTIC ACTIVITY: A [protein]-S-sulfanyl-L-cysteine +
CC       uridine(34) in tRNA + ATP + reduced acceptor = a [protein]-L-
CC       cysteine + 2-thiouridine(34) in tRNA + AMP + diphosphate +
CC       acceptor. {ECO:0000256|HAMAP-Rule:MF_00144}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00144}.
CC   -!- SIMILARITY: Belongs to the MnmA/TRMU family. {ECO:0000256|HAMAP-
CC       Rule:MF_00144}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation
CC       of feature annotation. {ECO:0000256|HAMAP-Rule:MF_00144}.
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DR   EMBL; AP010803; BAI95115.1; -; Genomic_DNA.
DR   RefSeq; WP_013038914.1; NC_014006.1.
DR   ProteinModelPortal; D4YXN3; -.
DR   STRING; 452662.SJA_C1-02810; -.
DR   EnsemblBacteria; BAI95115; BAI95115; SJA_C1-02810.
DR   GeneID; 29271984; -.
DR   KEGG; sjp:SJA_C1-02810; -.
DR   eggNOG; ENOG4105CCJ; Bacteria.
DR   eggNOG; COG0482; LUCA.
DR   HOGENOM; HOG000218045; -.
DR   KO; K00566; -.
DR   OMA; AVCTGHY; -.
DR   OrthoDB; POG091H02F0; -.
DR   Proteomes; UP000007753; Chromosome 1.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0008168; F:methyltransferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0016783; F:sulfurtransferase activity; IEA:InterPro.
DR   GO; GO:0000049; F:tRNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0006400; P:tRNA modification; IEA:UniProtKB-HAMAP.
DR   CDD; cd01998; tRNA_Me_trans; 1.
DR   Gene3D; 2.30.30.280; -; 1.
DR   Gene3D; 3.40.50.620; -; 1.
DR   HAMAP; MF_00144; tRNA_thiouridyl_MnmA; 1.
DR   InterPro; IPR023382; Adenine_a_hdrlase_dom.
DR   InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR   InterPro; IPR004506; tRNA-specific_2-thiouridylase.
DR   PANTHER; PTHR11933; PTHR11933; 1.
DR   TIGRFAMs; TIGR00420; trmU; 1.
PE   3: Inferred from homology;
DR   PRODOM; D4YXN3.
DR   SWISS-2DPAGE; D4YXN3.
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_00144};
KW   Complete proteome {ECO:0000313|Proteomes:UP000007753};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00144};
KW   Methyltransferase {ECO:0000313|EMBL:BAI95115.1};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00144};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007753};
KW   RNA-binding {ECO:0000256|HAMAP-Rule:MF_00144};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_00144,
KW   ECO:0000313|EMBL:BAI95115.1};
KW   tRNA processing {ECO:0000256|HAMAP-Rule:MF_00144};
KW   tRNA-binding {ECO:0000256|HAMAP-Rule:MF_00144}.
FT   NP_BIND      24     31       ATP. {ECO:0000256|HAMAP-Rule:MF_00144}.
FT   REGION      164    166       Interaction with tRNA.
FT                                {ECO:0000256|HAMAP-Rule:MF_00144}.
FT   ACT_SITE    118    118       Nucleophile. {ECO:0000256|HAMAP-Rule:
FT                                MF_00144}.
FT   ACT_SITE    214    214       Cysteine persulfide intermediate.
FT                                {ECO:0000256|HAMAP-Rule:MF_00144}.
FT   BINDING      50     50       ATP; via amide nitrogen and carbonyl
FT                                oxygen. {ECO:0000256|HAMAP-Rule:
FT                                MF_00144}.
FT   BINDING     142    142       ATP; via amide nitrogen.
FT                                {ECO:0000256|HAMAP-Rule:MF_00144}.
FT   SITE        143    143       Interaction with tRNA.
FT                                {ECO:0000256|HAMAP-Rule:MF_00144}.
FT   SITE        346    346       Interaction with tRNA.
FT                                {ECO:0000256|HAMAP-Rule:MF_00144}.
SQ   SEQUENCE   373 AA;  39748 MW;  9EEE914D26089E5E CRC64;
     MQPPFQPAQF DLKAPPDARR IVVAMSGGVD SSVVAALAAR TGAETIGVTL QLYDHGAAVG
     RTGSCCAGQD IRDARAVADR IGIAHYVFDY ESRFRDSVIA DFADEYMAGR TPIPCVKCNM
     GVKFTDLFQI ARDLGADCLA TGHYVRRVEG PQGAELHRAA DSARDQSYFL FATTQAQLDY
     LRFPLGGLPK PQVREIAAEL GLSVALKPDS QDICFVPDGD YAKIVRKLRP DADEGGDIVH
     IDGRLMGTHK GMIHYTVGQR KGLEIGGQAE PLYVVRLDAE ARRVIVGPKA ALAVSAARLS
     DINWLGGDFA GPLTAKVRSM AKPVPARLEG DRLVFDAPEY GVAPGQAAVL YAGDRVLGGG
     WIAATEAALA EAA
//

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