ID E8ZKC5_MYCHL Unreviewed; 368 AA.
AC E8ZKC5;
DT 05-APR-2011, integrated into UniProtKB/TrEMBL.
DT 05-APR-2011, sequence version 1.
DT 27-MAR-2024, entry version 52.
DE RecName: Full=tRNA-uridine 2-sulfurtransferase {ECO:0000256|ARBA:ARBA00011949};
DE EC=2.8.1.13 {ECO:0000256|ARBA:ARBA00011949};
GN Name=mnmA {ECO:0000313|EMBL:CBY92091.1};
GN OrderedLocusNames=HF1_00830 {ECO:0000313|EMBL:CBY92091.1};
OS Mycoplasma haemofelis (strain Langford 1) (Haemobartonella felis).
OC Bacteria; Mycoplasmatota; Mollicutes; Mycoplasmataceae; Mycoplasma.
OX NCBI_TaxID=941640 {ECO:0000313|EMBL:CBY92091.1, ECO:0000313|Proteomes:UP000008637};
RN [1] {ECO:0000313|EMBL:CBY92091.1, ECO:0000313|Proteomes:UP000008637}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Langford 1 {ECO:0000313|EMBL:CBY92091.1,
RC ECO:0000313|Proteomes:UP000008637};
RX PubMed=21317334; DOI=10.1128/JB.00076-11;
RA Barker E.N., Helps C.R., Peters I.R., Darby A.C., Radford A.D., Tasker S.;
RT "Complete genome sequence of Mycoplasma haemofelis, a hemotropic
RT mycoplasma.";
RL J. Bacteriol. 193:2060-2061(2011).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=AH2 + ATP + S-sulfanyl-L-cysteinyl-[protein] + uridine(34) in
CC tRNA = 2-thiouridine(34) in tRNA + A + AMP + diphosphate + H(+) + L-
CC cysteinyl-[protein]; Xref=Rhea:RHEA:47032, Rhea:RHEA-COMP:10131,
CC Rhea:RHEA-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;
CC Evidence={ECO:0000256|ARBA:ARBA00001042};
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DR EMBL; FR773153; CBY92091.1; -; Genomic_DNA.
DR RefSeq; WP_014582871.1; NC_014970.1.
DR AlphaFoldDB; E8ZKC5; -.
DR KEGG; mha:HF1_00830; -.
DR HOGENOM; CLU_035188_1_0_14; -.
DR OrthoDB; 9800696at2; -.
DR Proteomes; UP000008637; Chromosome.
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:0032259; P:methylation; IEA:UniProtKB-KW.
DR GO; GO:0008033; P:tRNA processing; IEA:UniProtKB-KW.
DR CDD; cd01998; tRNA_Me_trans; 1.
DR Gene3D; 2.30.30.280; Adenine nucleotide alpha hydrolases-like domains; 1.
DR Gene3D; 3.40.50.620; HUPs; 1.
DR Gene3D; 2.40.30.10; Translation factors; 1.
DR InterPro; IPR046885; MnmA-like_C.
DR InterPro; IPR046884; MnmA-like_central.
DR InterPro; IPR023382; MnmA-like_central_sf.
DR InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR InterPro; IPR004506; tRNA-specific_2-thiouridylase.
DR NCBIfam; TIGR00420; trmU; 1.
DR PANTHER; PTHR11933:SF5; MITOCHONDRIAL TRNA-SPECIFIC 2-THIOURIDYLASE 1; 1.
DR PANTHER; PTHR11933; TRNA 5-METHYLAMINOMETHYL-2-THIOURIDYLATE -METHYLTRANSFERASE; 1.
DR Pfam; PF03054; tRNA_Me_trans; 1.
DR Pfam; PF20258; tRNA_Me_trans_C; 1.
DR Pfam; PF20259; tRNA_Me_trans_M; 1.
DR SUPFAM; SSF52402; Adenine nucleotide alpha hydrolases-like; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW Methyltransferase {ECO:0000313|EMBL:CBY92091.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW RNA-binding {ECO:0000256|ARBA:ARBA00022884};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:CBY92091.1};
KW tRNA processing {ECO:0000256|ARBA:ARBA00022694};
KW tRNA-binding {ECO:0000256|ARBA:ARBA00022555}.
FT DOMAIN 214..278
FT /note="tRNA-specific 2-thiouridylase MnmA-like central"
FT /evidence="ECO:0000259|Pfam:PF20259"
FT DOMAIN 293..363
FT /note="tRNA-specific 2-thiouridylase MnmA-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF20258"
SQ SEQUENCE 368 AA; 42431 MW; 74A82E28F27B4021 CRC64;
MDSMKKVVIA LSGGVDSAIS AFLLKQKNHD LHAVYMQNWD SQVNEENAED SGCSSREDLK
YVKEICNKLN IPLTVYNFVP EYWEYVFEPY LNLVQNNLLS NPDILCNSKI KFGVLLNRII
QDFGPDIKLA TGHWARVINR DGRYMLAVCS NPNKDQTYFL SRLAPDQLKY ILFPLQDIQS
KEEIREIAKD LELSVWNRRD STGICFIGKR KYSDFMENFI DHEEGDLVDI ETGKILGTHK
GSHLYALHQR SGLALKGYEE RYYVCKKDPK KNVVYLCRES QIPLYLHTTS TFCSDIHWIN
EAPNVGEELF IKARHTPSFL KVKLRSLENG ECHITHEKTH ITSPGQYVVF YDLDRNICLG
SGIYKDGK
//
