(data stored in SCRATCH zone)

SWISSPROT: E6V3E5_VARPE

ID   E6V3E5_VARPE            Unreviewed;       366 AA.
AC   E6V3E5;
DT   08-MAR-2011, integrated into UniProtKB/TrEMBL.
DT   08-MAR-2011, sequence version 1.
DT   08-MAY-2019, entry version 48.
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=mnmA {ECO:0000256|HAMAP-Rule:MF_00144};
GN   OrderedLocusNames=Varpa_0413 {ECO:0000313|EMBL:ADU34635.1};
OS   Variovorax paradoxus (strain EPS).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Comamonadaceae; Variovorax.
OX   NCBI_TaxID=595537 {ECO:0000313|EMBL:ADU34635.1, ECO:0000313|Proteomes:UP000008917};
RN   [1] {ECO:0000313|Proteomes:UP000008917}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=EPS {ECO:0000313|Proteomes:UP000008917};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Cheng J.-F., Goodwin L.,
RA   Pitluck S., Teshima H., Detter J.C., Han C., Tapia R., Land M.,
RA   Hauser L., Kyrpides N., Ivanova N., Ovchinnikova G., Orwin P.,
RA   Han J.-I.G., Woyke T.;
RT   "Complete sequence of Variovorax paradoxus EPS.";
RL   Submitted (DEC-2010) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:ADU34635.1, ECO:0000313|Proteomes:UP000008917}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=EPS {ECO:0000313|EMBL:ADU34635.1,
RC   ECO:0000313|Proteomes:UP000008917};
RX   PubMed=24158554;
RA   Han J.I., Spain J.C., Leadbetter J.R., Ovchinnikova G., Goodwin L.A.,
RA   Han C.S., Woyke T., Davenport K.W., Orwin P.M.;
RT   "Genome of the Root-Associated Plant Growth-Promoting Bacterium
RT   Variovorax paradoxus Strain EPS.";
RL   Genome Announc. 1:e00843-13(2013).
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:
CC       Reaction=AH2 + ATP + S-sulfanyl-L-cysteinyl-[protein] +
CC         uridine(34) in tRNA = 2-thiouridine(34) in tRNA + A + AMP +
CC         diphosphate + H(+) + L-cysteinyl-[protein];
CC         Xref=Rhea:RHEA:47032, Rhea:RHEA-COMP:10131, Rhea:RHEA-
CC         COMP:11726, Rhea:RHEA-COMP:11727, Rhea:RHEA-COMP:11728,
CC         ChEBI:CHEBI:13193, ChEBI:CHEBI:15378, ChEBI:CHEBI:17499,
CC         ChEBI:CHEBI:29950, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019,
CC         ChEBI:CHEBI:61963, ChEBI:CHEBI:65315, ChEBI:CHEBI:87170,
CC         ChEBI:CHEBI:456215; EC=2.8.1.13; Evidence={ECO:0000256|HAMAP-
CC         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; CP002417; ADU34635.1; -; Genomic_DNA.
DR   RefSeq; WP_013538881.1; NC_014931.1.
DR   STRING; 595537.Varpa_0413; -.
DR   EnsemblBacteria; ADU34635; ADU34635; Varpa_0413.
DR   GeneID; 29715090; -.
DR   KEGG; vpe:Varpa_0413; -.
DR   eggNOG; ENOG4105CCJ; Bacteria.
DR   eggNOG; COG0482; LUCA.
DR   HOGENOM; HOG000218046; -.
DR   KO; K00566; -.
DR   OMA; AVCTGHY; -.
DR   OrthoDB; 1054741at2; -.
DR   BioCyc; VPAR595537:G1GQO-415-MONOMER; -.
DR   Proteomes; UP000008917; Chromosome.
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-UniRule.
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   TIGRFAMs; TIGR00420; trmU; 1.
PE   3: Inferred from homology;
DR   PRODOM; E6V3E5.
DR   SWISS-2DPAGE; E6V3E5.
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_00144};
KW   Complete proteome {ECO:0000313|Proteomes:UP000008917};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00144};
KW   Methyltransferase {ECO:0000313|EMBL:ADU34635.1};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00144};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008917};
KW   RNA-binding {ECO:0000256|HAMAP-Rule:MF_00144};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_00144,
KW   ECO:0000313|EMBL:ADU34635.1};
KW   tRNA processing {ECO:0000256|HAMAP-Rule:MF_00144};
KW   tRNA-binding {ECO:0000256|HAMAP-Rule:MF_00144}.
FT   NP_BIND       9     16       ATP. {ECO:0000256|HAMAP-Rule:MF_00144}.
FT   REGION       95     97       Interaction with target base in tRNA.
FT                                {ECO:0000256|HAMAP-Rule:MF_00144}.
FT   REGION      148    150       Interaction with tRNA.
FT                                {ECO:0000256|HAMAP-Rule:MF_00144}.
FT   REGION      316    317       Interaction with tRNA.
FT                                {ECO:0000256|HAMAP-Rule:MF_00144}.
FT   ACT_SITE    100    100       Nucleophile. {ECO:0000256|HAMAP-Rule:
FT                                MF_00144}.
FT   ACT_SITE    198    198       Cysteine persulfide intermediate.
FT                                {ECO:0000256|HAMAP-Rule:MF_00144}.
FT   BINDING      35     35       ATP; via amide nitrogen and carbonyl
FT                                oxygen. {ECO:0000256|HAMAP-Rule:
FT                                MF_00144}.
FT   BINDING     124    124       ATP; via amide nitrogen.
FT                                {ECO:0000256|HAMAP-Rule:MF_00144}.
FT   SITE        125    125       Interaction with tRNA.
FT                                {ECO:0000256|HAMAP-Rule:MF_00144}.
FT   SITE        349    349       Interaction with tRNA.
FT                                {ECO:0000256|HAMAP-Rule:MF_00144}.
SQ   SEQUENCE   366 AA;  40281 MW;  243310134B3CE401 CRC64;
     MAKQRIVVGL SGGVDSAVTA HLLKQQGHEV VGIFMKNWED DDDSEYCSSN IDFIDAASVA
     DVLGIEIEHV NFAADYKDRV FAEFLREYKA GRTPNPDVLC NAEIKFKAFL DHAMRLGAEK
     IATGHYARVR HNEVTGRHEL LKGLDPSKDQ SYFLHRLNQA QLSKTLFPVG ELHKTEVRRI
     AEEIGLPNAK KKDSTGICFI GERPFRDFLN RYISKEPGPI KDDRGRKLGE HQGLSFYTLG
     QRQGLGIGGV KEKGAQRGSG DHSPWFVARK DIEKNTLWVV QGHDHPWLLS SALNADDASW
     VSGEAPAAGS YGSKARYRQA DAGCELSDDA NGAFSLRFGA PQWAVTPGQS AVLYDGERCL
     GGGVIV
//

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