ID A4NZS1_HAEIF Unreviewed; 143 AA.
AC A4NZS1;
DT 15-MAY-2007, integrated into UniProtKB/TrEMBL.
DT 15-MAY-2007, sequence version 1.
DT 24-JAN-2024, entry version 52.
DE RecName: Full=tRNA-2-methylthio-N(6)-dimethylallyladenosine synthase {ECO:0000256|ARBA:ARBA00033765};
DE EC=2.8.4.3 {ECO:0000256|ARBA:ARBA00033765};
GN ORFNames=CGSHiR3021_01202 {ECO:0000313|EMBL:EDK13337.1};
OS Haemophilus influenzae 22.4-21.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Haemophilus.
OX NCBI_TaxID=375063 {ECO:0000313|EMBL:EDK13337.1, ECO:0000313|Proteomes:UP000005596};
RN [1] {ECO:0000313|EMBL:EDK13337.1, ECO:0000313|Proteomes:UP000005596}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=22.4-21 {ECO:0000313|EMBL:EDK13337.1,
RC ECO:0000313|Proteomes:UP000005596};
RX PubMed=17550610; DOI=10.1186/gb-2007-8-6-r103;
RA Hogg J.S., Hu F.Z., Janto B., Boissy R., Hayes J., Keefe R., Post J.C.,
RA Ehrlich G.D.;
RT "Characterization and modeling of the Haemophilus influenzae core and
RT supragenomes based on the complete genomic sequences of Rd and 12 clinical
RT nontypeable strains.";
RL Genome Biol. 8:R103.1-R103.18(2007).
CC -!- FUNCTION: Catalyzes the methylthiolation of N6-(dimethylallyl)adenosine
CC (i(6)A), leading to the formation of 2-methylthio-N6-
CC (dimethylallyl)adenosine (ms(2)i(6)A) at position 37 in tRNAs that read
CC codons beginning with uridine. {ECO:0000256|ARBA:ARBA00003234}.
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DR EMBL; AAZJ01000010; EDK13337.1; -; Genomic_DNA.
DR AlphaFoldDB; A4NZS1; -.
DR BioCyc; HINF375063:G119K-1728-MONOMER; -.
DR Proteomes; UP000005596; Unassembled WGS sequence.
DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR Gene3D; 3.30.750.200; -; 1.
DR Gene3D; 2.40.50.140; Nucleic acid-binding proteins; 1.
DR InterPro; IPR012340; NA-bd_OB-fold.
DR InterPro; IPR002792; TRAM_dom.
DR PANTHER; PTHR43020; CDK5 REGULATORY SUBUNIT-ASSOCIATED PROTEIN 1; 1.
DR PANTHER; PTHR43020:SF2; MITOCHONDRIAL TRNA METHYLTHIOTRANSFERASE CDK5RAP1; 1.
DR Pfam; PF01938; TRAM; 1.
DR SUPFAM; SSF102114; Radical SAM enzymes; 1.
DR PROSITE; PS50926; TRAM; 1.
PE 4: Predicted;
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 47..110
FT /note="TRAM"
FT /evidence="ECO:0000259|PROSITE:PS50926"
SQ SEQUENCE 143 AA; 16330 MW; F7A317E8FF544097 CRC64;
MSFSFVYSAR PGTPAADMPD DVTEDEKKQR LYVLQERINQ QAAQFSRRML GTEQRVLVEG
PSKKDIMELT GRTETNRIVN FQGSPEMIGK FVDVKITDVY TNSLRGEVVR TEDEMGLRIA
QSPQEVMNRT RKEDELGVGR YHG
//
