ID   Y1326_CAUVC             Reviewed;         415 AA.
AC   Q9A8M7;
DT   19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   03-AUG-2022, entry version 98.
DE   RecName: Full=Uncharacterized RNA methyltransferase CC_1326;
DE            EC=2.1.1.-;
GN   OrderedLocusNames=CC_1326;
OS   Caulobacter vibrioides (strain ATCC 19089 / CB15) (Caulobacter crescentus).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Caulobacterales;
OC   Caulobacteraceae; Caulobacter.
OX   NCBI_TaxID=190650;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 19089 / CB15;
RX   PubMed=11259647; DOI=10.1073/pnas.061029298;
RA   Nierman W.C., Feldblyum T.V., Laub M.T., Paulsen I.T., Nelson K.E.,
RA   Eisen J.A., Heidelberg J.F., Alley M.R.K., Ohta N., Maddock J.R.,
RA   Potocka I., Nelson W.C., Newton A., Stephens C., Phadke N.D., Ely B.,
RA   DeBoy R.T., Dodson R.J., Durkin A.S., Gwinn M.L., Haft D.H., Kolonay J.F.,
RA   Smit J., Craven M.B., Khouri H.M., Shetty J., Berry K.J., Utterback T.R.,
RA   Tran K., Wolf A.M., Vamathevan J.J., Ermolaeva M.D., White O.,
RA   Salzberg S.L., Venter J.C., Shapiro L., Fraser C.M.;
RT   "Complete genome sequence of Caulobacter crescentus.";
RL   Proc. Natl. Acad. Sci. U.S.A. 98:4136-4141(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; AE005673; AAK23307.1; -; Genomic_DNA.
DR   PIR; G87413; G87413.
DR   RefSeq; NP_420139.1; NC_002696.2.
DR   RefSeq; WP_010919203.1; NC_002696.2.
DR   AlphaFoldDB; Q9A8M7; -.
DR   SMR; Q9A8M7; -.
DR   STRING; 190650.CC_1326; -.
DR   PRIDE; Q9A8M7; -.
DR   EnsemblBacteria; AAK23307; AAK23307; CC_1326.
DR   KEGG; ccr:CC_1326; -.
DR   PATRIC; fig|190650.5.peg.1354; -.
DR   eggNOG; COG2265; Bacteria.
DR   HOGENOM; CLU_014689_8_0_5; -.
DR   OMA; FYAGDMK; -.
DR   BioCyc; CAULO:CC1326-MON; -.
DR   Proteomes; UP000001816; 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:0006396; P:RNA processing; IEA:InterPro.
DR   Gene3D; 2.40.50.140; -; 1.
DR   Gene3D; 3.40.50.150; -; 1.
DR   InterPro; IPR030390; MeTrfase_TrmA_AS.
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.
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..415
FT                   /note="Uncharacterized RNA methyltransferase CC_1326"
FT                   /id="PRO_0000161962"
FT   DOMAIN          1..52
FT                   /note="TRAM"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00208"
FT   ACT_SITE        373
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01024"
FT   BINDING         62
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000250"
FT   BINDING         68
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000250"
FT   BINDING         71
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000250"
FT   BINDING         147
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000250"
FT   BINDING         252
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01024"
FT   BINDING         279
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01024"
FT   BINDING         299
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01024"
FT   BINDING         347
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01024"
SQ   SEQUENCE   415 AA;  43670 MW;  91F815EB02E574DD CRC64;
     MQDLTINAIG AQGDGLARTA DGKPAFVPLT LPGEVVRAKM DGARGEVVEI LAPSPERVAP
     ACRHYGVCGG CALQHWAAEP YRAWKAEQVR LQLSMEGLET EILPTFAAPP ASRRRVALHA
     RKGGKGQGAR LGFKERRSWN LVSIEECPVT DPRLVAALPA LARLAEPFLE HPKSAPTLHV
     TLTATGLDID ITGVERKSGG LSADARMRAA MAAGEGDFAR VTLAGETIYG ARQPLVKLGQ
     AVVALPPGSF LQAVPAAEKA MVELAVAEAQ GASRVADLYC GVGTFTFPLA EVAQVYAAEM
     SAPAITALKA AIGGAPGLKP ITAEARDLVR RPVLSTELAK TDVVVIDPPR AGAAEQTVEI
     AKSKVAKVLG VSCNPQTFAK DARVLVDAGF KLVRVTPVDQ FVWSPHIELV GVFTR