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Database: UniProt
Entry: H3KFU6_9BURK
LinkDB: H3KFU6_9BURK
Original site: H3KFU6_9BURK 
ID   H3KFU6_9BURK            Unreviewed;       492 AA.
AC   H3KFU6;
DT   18-APR-2012, integrated into UniProtKB/TrEMBL.
DT   18-APR-2012, sequence version 1.
DT   27-MAR-2024, entry version 60.
DE   RecName: Full=23S rRNA (uracil(1939)-C(5))-methyltransferase RlmD {ECO:0000256|HAMAP-Rule:MF_01010};
DE            EC=2.1.1.190 {ECO:0000256|HAMAP-Rule:MF_01010};
DE   AltName: Full=23S rRNA(m5U1939)-methyltransferase {ECO:0000256|HAMAP-Rule:MF_01010};
GN   Name=rlmD {ECO:0000256|HAMAP-Rule:MF_01010};
GN   ORFNames=HMPREF9440_01615 {ECO:0000313|EMBL:EHY31015.1};
OS   Sutterella parvirubra YIT 11816.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Sutterellaceae; Sutterella.
OX   NCBI_TaxID=762967 {ECO:0000313|EMBL:EHY31015.1, ECO:0000313|Proteomes:UP000004956};
RN   [1] {ECO:0000313|EMBL:EHY31015.1, ECO:0000313|Proteomes:UP000004956}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=YIT 11816 {ECO:0000313|EMBL:EHY31015.1,
RC   ECO:0000313|Proteomes:UP000004956};
RA   Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., Courtney L.,
RA   Fronick C., Harrison M., Strong C., Farmer C., Delahaunty K., Markovic C.,
RA   Hall O., Minx P., Tomlinson C., Mitreva M., Hou S., Chen J., Wollam A.,
RA   Pepin K.H., Johnson M., Bhonagiri V., Zhang X., Suruliraj S., Warren W.,
RA   Chinwalla A., Mardis E.R., Wilson R.K.;
RL   Submitted (NOV-2011) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the formation of 5-methyl-uridine at position 1939
CC       (m5U1939) in 23S rRNA. {ECO:0000256|HAMAP-Rule:MF_01010}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=S-adenosyl-L-methionine + uridine(1939) in 23S rRNA = 5-
CC         methyluridine(1939) in 23S rRNA + H(+) + S-adenosyl-L-homocysteine;
CC         Xref=Rhea:RHEA:42908, Rhea:RHEA-COMP:10278, Rhea:RHEA-COMP:10279,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC         ChEBI:CHEBI:65315, ChEBI:CHEBI:74447; EC=2.1.1.190;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_01010};
CC   -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC       superfamily. RNA M5U methyltransferase family. RlmD subfamily.
CC       {ECO:0000256|HAMAP-Rule:MF_01010}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EHY31015.1}.
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DR   EMBL; AFBQ01000244; EHY31015.1; -; Genomic_DNA.
DR   AlphaFoldDB; H3KFU6; -.
DR   STRING; 762967.HMPREF9440_01615; -.
DR   PATRIC; fig|762967.3.peg.1268; -.
DR   HOGENOM; CLU_014689_8_2_4; -.
DR   Proteomes; UP000004956; Unassembled WGS sequence.
DR   GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0005506; F:iron ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR   GO; GO:0070041; F:rRNA (uridine-C5-)-methyltransferase activity; IEA:UniProtKB-UniRule.
DR   CDD; cd02440; AdoMet_MTases; 1.
DR   Gene3D; 2.40.50.1070; -; 1.
DR   Gene3D; 2.40.50.140; Nucleic acid-binding proteins; 1.
DR   Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR   HAMAP; MF_01010; 23SrRNA_methyltr_RlmD; 1.
DR   InterPro; IPR001566; 23S_rRNA_MeTrfase_RlmD.
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   NCBIfam; TIGR00479; rumA; 1.
DR   PANTHER; PTHR11061:SF49; 23S RRNA (URACIL(1939)-C(5))-METHYLTRANSFERASE RLMD; 1.
DR   PANTHER; PTHR11061; RNA M5U METHYLTRANSFERASE; 1.
DR   Pfam; PF01938; TRAM; 1.
DR   Pfam; PF05958; tRNA_U5-meth_tr; 1.
DR   SUPFAM; SSF50249; Nucleic acid-binding proteins; 1.
DR   SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 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 {ECO:0000256|ARBA:ARBA00022485, ECO:0000256|HAMAP-Rule:MF_01010};
KW   Iron {ECO:0000256|HAMAP-Rule:MF_01010};
KW   Iron-sulfur {ECO:0000256|HAMAP-Rule:MF_01010};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_01010};
KW   Methyltransferase {ECO:0000256|ARBA:ARBA00022603, ECO:0000256|HAMAP-
KW   Rule:MF_01010}; Reference proteome {ECO:0000313|Proteomes:UP000004956};
KW   rRNA processing {ECO:0000256|ARBA:ARBA00022552, ECO:0000256|HAMAP-
KW   Rule:MF_01010};
KW   S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691, ECO:0000256|HAMAP-
KW   Rule:MF_01010};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW   Rule:MF_01010}.
FT   DOMAIN          10..69
FT                   /note="TRAM"
FT                   /evidence="ECO:0000259|PROSITE:PS50926"
FT   REGION          457..492
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        415
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10015"
FT   ACT_SITE        415
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01010,
FT                   ECO:0000256|PROSITE-ProRule:PRU01024"
FT   BINDING         82
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01010"
FT   BINDING         92
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01010"
FT   BINDING         95
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01010"
FT   BINDING         174
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01010"
FT   BINDING         284
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01010,
FT                   ECO:0000256|PROSITE-ProRule:PRU01024"
FT   BINDING         313
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01010,
FT                   ECO:0000256|PROSITE-ProRule:PRU01024"
FT   BINDING         318
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01010"
FT   BINDING         334
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01010,
FT                   ECO:0000256|PROSITE-ProRule:PRU01024"
FT   BINDING         362
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01010"
FT   BINDING         387
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01010,
FT                   ECO:0000256|PROSITE-ProRule:PRU01024"
SQ   SEQUENCE   492 AA;  54152 MW;  13F698F22F63FB58 CRC64;
     MRRAVMAKRK EKTPEYFTVD VDRLDQEGRG VARNDEGKVV FIEGALPGER VTYERLRSKP
     SYEKGRVVAV HRESVQRVKP ACPHFGIGPG SCGGCAMQHL EANAQVAYKQ KVLMDTLWHI
     GRVKPESVLP AIHGPAWNYR HRARLTVRDV AKKGGVLVGF HEKASSYVAD MTTCKILTKN
     VVAMLMPMRE LVASLSIRQR LPQIEVAVGG DSRTALVFRV LEAPTDDDME KLLAFGREHG
     ADIWLQPKGP ETAHAVLPEN EHALGLSLSE FGVRISFKPT DFTQVNHALN ETMVGRAVRL
     LHVEPEHKVA DFFCGLGNFT LPLATKAAKV IGIEGSEGLV ARARQGAADN GLADKTEFVA
     RNLFTWTEKD WDELWDRMGG IDRVLIDPPR EGAIELAGAL AATDRRPARI VYVSCNPATL
     ARDCAKLHHE GGWHIRAAGI MNMFPHTGHV ESIAVLEPGP KPERRPAEDL QTEAAQDVPA
     ETPANETAET AE
//
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