Y1606_STRP1
ID Y1606_STRP1 Reviewed; 451 AA.
AC Q99YP3; Q48XI8;
DT 19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 131.
DE RecName: Full=Uncharacterized RNA methyltransferase SPy_1606/M5005_Spy1319;
DE EC=2.1.1.-;
GN OrderedLocusNames=SPy_1606, M5005_Spy1319;
OS Streptococcus pyogenes serotype M1.
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=301447;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700294 / SF370 / Serotype M1;
RX PubMed=11296296; DOI=10.1073/pnas.071559398;
RA Ferretti J.J., McShan W.M., Ajdic D.J., Savic D.J., Savic G., Lyon K.,
RA Primeaux C., Sezate S., Suvorov A.N., Kenton S., Lai H.S., Lin S.P.,
RA Qian Y., Jia H.G., Najar F.Z., Ren Q., Zhu H., Song L., White J., Yuan X.,
RA Clifton S.W., Roe B.A., McLaughlin R.E.;
RT "Complete genome sequence of an M1 strain of Streptococcus pyogenes.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:4658-4663(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-947 / MGAS5005 / Serotype M1;
RX PubMed=16088826; DOI=10.1086/432514;
RA Sumby P., Porcella S.F., Madrigal A.G., Barbian K.D., Virtaneva K.,
RA Ricklefs S.M., Sturdevant D.E., Graham M.R., Vuopio-Varkila J., Hoe N.P.,
RA Musser J.M.;
RT "Evolutionary origin and emergence of a highly successful clone of serotype
RT M1 group A Streptococcus involved multiple horizontal gene transfer
RT events.";
RL J. Infect. Dis. 192:771-782(2005).
CC -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC superfamily. RNA M5U methyltransferase family. {ECO:0000255|PROSITE-
CC ProRule:PRU01024}.
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DR EMBL; AE004092; AAK34383.1; -; Genomic_DNA.
DR EMBL; CP000017; AAZ51937.1; -; Genomic_DNA.
DR RefSeq; NP_269662.1; NC_002737.2.
DR AlphaFoldDB; Q99YP3; -.
DR SMR; Q99YP3; -.
DR STRING; 1314.HKU360_01358; -.
DR PaxDb; Q99YP3; -.
DR EnsemblBacteria; AAK34383; AAK34383; SPy_1606.
DR KEGG; spy:SPy_1606; -.
DR KEGG; spz:M5005_Spy1319; -.
DR PATRIC; fig|160490.10.peg.1400; -.
DR HOGENOM; CLU_014689_7_1_9; -.
DR OMA; YCGVGGF; -.
DR Proteomes; UP000000750; Chromosome.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008173; F:RNA methyltransferase activity; IEA:InterPro.
DR GO; GO:0034470; P:ncRNA processing; IEA:UniProt.
DR Gene3D; 2.40.50.140; -; 1.
DR Gene3D; 3.40.50.150; -; 1.
DR InterPro; IPR030390; MeTrfase_TrmA_AS.
DR InterPro; IPR030391; MeTrfase_TrmA_CS.
DR InterPro; IPR012340; NA-bd_OB-fold.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR InterPro; IPR002792; TRAM_dom.
DR InterPro; IPR010280; U5_MeTrfase_fam.
DR PANTHER; PTHR11061; PTHR11061; 1.
DR Pfam; PF01938; TRAM; 1.
DR Pfam; PF05958; tRNA_U5-meth_tr; 1.
DR SUPFAM; SSF50249; SSF50249; 1.
DR SUPFAM; SSF53335; SSF53335; 1.
DR PROSITE; PS51687; SAM_MT_RNA_M5U; 1.
DR PROSITE; PS50926; TRAM; 1.
DR PROSITE; PS01230; TRMA_1; 1.
DR PROSITE; PS01231; TRMA_2; 1.
PE 3: Inferred from homology;
KW 4Fe-4S; Iron; Iron-sulfur; Metal-binding; Methyltransferase;
KW Reference proteome; S-adenosyl-L-methionine; Transferase.
FT CHAIN 1..451
FT /note="Uncharacterized RNA methyltransferase
FT SPy_1606/M5005_Spy1319"
FT /id="PRO_0000162036"
FT DOMAIN 2..60
FT /note="TRAM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00208"
FT ACT_SITE 408
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01024"
FT BINDING 73
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250"
FT BINDING 79
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250"
FT BINDING 82
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250"
FT BINDING 162
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250"
FT BINDING 283
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01024"
FT BINDING 312
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01024"
FT BINDING 333
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01024"
FT BINDING 381
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01024"
SQ SEQUENCE 451 AA; 50716 MW; D3E095E027A46750 CRC64;
MVVKVKQKIP LKIKRMGING EGIGFYQKTL VFVPGALKGE DIFCQITAVK RNFAEAKLLT
VNKASKNRVK PACSVYETCG GCQIMHLAYP KQLDFKDDVI RQALKKFKPT GYEQFEIRPT
LGMKKPDHYR AKLQFQLRSF GGTVKAGLFS QGSHRLVPID NCLVQDQLTQ DIINKITQLV
DKYKLPIYNE RKIAGIRTIM VRKAQASDQV QIIVVSSKEV RLANFIGELT KAFPQVKTVA
LNSNRSKSSE IYGDETEILW GQEAIHEEVL DYGFALSPRA FYQLNPQQTE VLYGEVVKAL
DVGSKDHIID AYCGVGSIGF AFAGKVKSVR GMDIIPEAIE DAQKNAKAMG FDNAYYEAGK
AEDIISKWYK QGYRADAVIV DPPRTGLDDK LLKTILHYQP KQMVYVSCNT STLARDLVQL
TKVYDVHYIQ SVDMFPHTAR TEAVVKLQKR V
