ID   Y1029_STRPN             Reviewed;         543 AA.
AC   Q97R12;
DT   19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2001, sequence version 1.
DT   03-AUG-2022, entry version 110.
DE   RecName: Full=Uncharacterized RNA methyltransferase SP_1029;
DE            EC=2.1.1.-;
GN   OrderedLocusNames=SP_1029;
OS   Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=170187;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-334 / TIGR4;
RX   PubMed=11463916; DOI=10.1126/science.1061217;
RA   Tettelin H., Nelson K.E., Paulsen I.T., Eisen J.A., Read T.D.,
RA   Peterson S.N., Heidelberg J.F., DeBoy R.T., Haft D.H., Dodson R.J.,
RA   Durkin A.S., Gwinn M.L., Kolonay J.F., Nelson W.C., Peterson J.D.,
RA   Umayam L.A., White O., Salzberg S.L., Lewis M.R., Radune D.,
RA   Holtzapple E.K., Khouri H.M., Wolf A.M., Utterback T.R., Hansen C.L.,
RA   McDonald L.A., Feldblyum T.V., Angiuoli S.V., Dickinson T., Hickey E.K.,
RA   Holt I.E., Loftus B.J., Yang F., Smith H.O., Venter J.C., Dougherty B.A.,
RA   Morrison D.A., Hollingshead S.K., Fraser C.M.;
RT   "Complete genome sequence of a virulent isolate of Streptococcus
RT   pneumoniae.";
RL   Science 293:498-506(2001).
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; AE005672; AAK75144.1; -; Genomic_DNA.
DR   PIR; G95118; G95118.
DR   RefSeq; WP_000914584.1; NZ_AKVY01000001.1.
DR   PDB; 5XJ1; X-ray; 1.75 A; A=1-454.
DR   PDB; 5XJ2; X-ray; 2.84 A; A/B/C/D=1-454.
DR   PDB; 5ZQ0; X-ray; 2.00 A; A=1-452.
DR   PDB; 5ZQ1; X-ray; 3.10 A; A=1-452.
DR   PDB; 5ZQ8; X-ray; 2.18 A; A/B=1-454.
DR   PDB; 5ZTH; X-ray; 3.24 A; A=1-452.
DR   PDBsum; 5XJ1; -.
DR   PDBsum; 5XJ2; -.
DR   PDBsum; 5ZQ0; -.
DR   PDBsum; 5ZQ1; -.
DR   PDBsum; 5ZQ8; -.
DR   PDBsum; 5ZTH; -.
DR   AlphaFoldDB; Q97R12; -.
DR   SMR; Q97R12; -.
DR   STRING; 170187.SP_1029; -.
DR   EnsemblBacteria; AAK75144; AAK75144; SP_1029.
DR   KEGG; spn:SP_1029; -.
DR   eggNOG; COG2265; Bacteria.
DR   OMA; FYAGDMK; -.
DR   PhylomeDB; Q97R12; -.
DR   BioCyc; SPNE170187:G1FZB-1058-MON; -.
DR   BRENDA; 2.1.1.189; 1960.
DR   BRENDA; 2.1.1.190; 1960.
DR   Proteomes; UP000000585; Chromosome.
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; 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   1: Evidence at protein level;
KW   3D-structure; Methyltransferase; S-adenosyl-L-methionine; Transferase.
FT   CHAIN           1..543
FT                   /note="Uncharacterized RNA methyltransferase SP_1029"
FT                   /id="PRO_0000162031"
FT   DOMAIN          1..59
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         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"
FT   STRAND          7..11
FT                   /evidence="ECO:0007829|PDB:5XJ1"
FT   STRAND          21..25
FT                   /evidence="ECO:0007829|PDB:5XJ1"
FT   STRAND          28..32
FT                   /evidence="ECO:0007829|PDB:5XJ1"
FT   STRAND          40..48
FT                   /evidence="ECO:0007829|PDB:5XJ1"
FT   STRAND          50..62
FT                   /evidence="ECO:0007829|PDB:5XJ1"
FT   STRAND          65..67
FT                   /evidence="ECO:0007829|PDB:5ZQ8"
FT   HELIX           74..77
FT                   /evidence="ECO:0007829|PDB:5XJ1"
FT   TURN            78..80
FT                   /evidence="ECO:0007829|PDB:5ZQ8"
FT   TURN            82..85
FT                   /evidence="ECO:0007829|PDB:5XJ1"
FT   HELIX           88..107
FT                   /evidence="ECO:0007829|PDB:5XJ1"
FT   STRAND          111..114
FT                   /evidence="ECO:0007829|PDB:5ZQ1"
FT   STRAND          127..137
FT                   /evidence="ECO:0007829|PDB:5XJ1"
FT   STRAND          140..146
FT                   /evidence="ECO:0007829|PDB:5XJ1"
FT   STRAND          153..155
FT                   /evidence="ECO:0007829|PDB:5XJ1"
FT   STRAND          160..162
FT                   /evidence="ECO:0007829|PDB:5XJ1"
FT   HELIX           164..179
FT                   /evidence="ECO:0007829|PDB:5XJ1"
FT   STRAND          184..186
FT                   /evidence="ECO:0007829|PDB:5XJ2"
FT   TURN            187..190
FT                   /evidence="ECO:0007829|PDB:5XJ1"
FT   STRAND          193..201
FT                   /evidence="ECO:0007829|PDB:5XJ1"
FT   TURN            203..205
FT                   /evidence="ECO:0007829|PDB:5XJ1"
FT   STRAND          208..217
FT                   /evidence="ECO:0007829|PDB:5XJ1"
FT   HELIX           222..232
FT                   /evidence="ECO:0007829|PDB:5XJ1"
FT   STRAND          236..243
FT                   /evidence="ECO:0007829|PDB:5XJ1"
FT   STRAND          246..249
FT                   /evidence="ECO:0007829|PDB:5XJ1"
FT   STRAND          254..261
FT                   /evidence="ECO:0007829|PDB:5XJ1"
FT   STRAND          263..269
FT                   /evidence="ECO:0007829|PDB:5XJ1"
FT   STRAND          272..277
FT                   /evidence="ECO:0007829|PDB:5XJ1"
FT   STRAND          278..280
FT                   /evidence="ECO:0007829|PDB:5ZQ1"
FT   HELIX           286..300
FT                   /evidence="ECO:0007829|PDB:5XJ1"
FT   STRAND          307..312
FT                   /evidence="ECO:0007829|PDB:5XJ1"
FT   TURN            314..316
FT                   /evidence="ECO:0007829|PDB:5ZTH"
FT   HELIX           317..322
FT                   /evidence="ECO:0007829|PDB:5XJ1"
FT   HELIX           323..325
FT                   /evidence="ECO:0007829|PDB:5XJ1"
FT   STRAND          326..334
FT                   /evidence="ECO:0007829|PDB:5XJ1"
FT   HELIX           336..348
FT                   /evidence="ECO:0007829|PDB:5XJ1"
FT   STRAND          353..359
FT                   /evidence="ECO:0007829|PDB:5XJ1"
FT   HELIX           361..370
FT                   /evidence="ECO:0007829|PDB:5XJ1"
FT   STRAND          377..380
FT                   /evidence="ECO:0007829|PDB:5XJ1"
FT   HELIX           389..397
FT                   /evidence="ECO:0007829|PDB:5XJ1"
FT   STRAND          401..408
FT                   /evidence="ECO:0007829|PDB:5XJ1"
FT   HELIX           410..422
FT                   /evidence="ECO:0007829|PDB:5XJ1"
FT   STRAND          426..433
FT                   /evidence="ECO:0007829|PDB:5XJ1"
FT   STRAND          443..449
FT                   /evidence="ECO:0007829|PDB:5XJ1"
SQ   SEQUENCE   543 AA;  61818 MW;  29047F4ECCF99714 CRC64;
     MLKKNDIVEV EIVDLTHEGA GVAKVDGLVF FVENALPSEK ILMRVLKVNK KIGFGKVEKY
     LVQSPHRNQD LDLAYLRSGI ADLGHLSYPE QLKFKTKQVK DSLYKIAGIA DVEVAETLGM
     EHPVKYRNKA QVPVRRVNGV LETGFFRKNS HNLMPLEDFF IQDPVIDQVV VALRDLLRRF
     DLKPYDEKEQ SGLIRNLVVR RGHYSGQIMV VLVTTRPKVF RVDQLIEQVI KQFPEIVSVM
     QNINDQNTNA IFGKEWRTLY GQDYITDQML GNDFQIAGPA FYQVNTEMAE KLYQTAIDFA
     ELKKDDVIID AYSGIGTIGL SVAKHVKEVY GVELIPEAVE NSQKNASLNK ITNAHYVCDT
     AENAMKKWLK EGIQPTVILV DPPRKGLTES FIKASAQTGA DRIAYISCNV ATMARDIKLY
     QELGYELKKV QPVDLFPQTH HVETVALLSK LDVDKHISVE IELDEMDLTS AESKATYAQI
     KEYVWNKFEL KVSTLYIAQI KKKCGIELRE HYNKSKKDKQ IIPQCTPEKE EAIMDALRHF
     KMI