SPB1_DICDI
ID SPB1_DICDI Reviewed; 833 AA.
AC Q54NX0;
DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 03-AUG-2022, entry version 98.
DE RecName: Full=pre-rRNA 2'-O-ribose RNA methyltransferase {ECO:0000255|HAMAP-Rule:MF_03163};
DE EC=2.1.1.- {ECO:0000255|HAMAP-Rule:MF_03163};
GN Name=fsjC; Synonyms=ftsj3; ORFNames=DDB_G0284945;
OS Dictyostelium discoideum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=44689;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4;
RX PubMed=15875012; DOI=10.1038/nature03481;
RA Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT "The genome of the social amoeba Dictyostelium discoideum.";
RL Nature 435:43-57(2005).
CC -!- FUNCTION: RNA 2'-O-methyltransferase involved in the maturation of rRNA
CC and in the biogenesis of ribosomal subunits. {ECO:0000255|HAMAP-
CC Rule:MF_03163}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a ribonucleotide in rRNA + S-adenosyl-L-methionine = a 2'-O-
CC methylribonucleotide in rRNA + H(+) + S-adenosyl-L-homocysteine;
CC Xref=Rhea:RHEA:48628, Rhea:RHEA-COMP:12164, Rhea:RHEA-COMP:12165,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC ChEBI:CHEBI:90675, ChEBI:CHEBI:90676; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_03163};
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000255|HAMAP-
CC Rule:MF_03163}.
CC -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC superfamily. RNA methyltransferase RlmE family. SPB1 subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_03163}.
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DR EMBL; AAFI02000073; EAL64936.1; -; Genomic_DNA.
DR RefSeq; XP_639947.1; XM_634855.1.
DR AlphaFoldDB; Q54NX0; -.
DR STRING; 44689.DDB0238604; -.
DR PaxDb; Q54NX0; -.
DR PRIDE; Q54NX0; -.
DR EnsemblProtists; EAL64936; EAL64936; DDB_G0284945.
DR GeneID; 8624859; -.
DR KEGG; ddi:DDB_G0284945; -.
DR dictyBase; DDB_G0284945; fsjC.
DR eggNOG; KOG1098; Eukaryota.
DR HOGENOM; CLU_009422_8_1_1; -.
DR InParanoid; Q54NX0; -.
DR OMA; LMWVFQQ; -.
DR PhylomeDB; Q54NX0; -.
DR PRO; PR:Q54NX0; -.
DR Proteomes; UP000002195; Chromosome 4.
DR GO; GO:0005730; C:nucleolus; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; ISS:dictyBase.
DR GO; GO:0030687; C:preribosome, large subunit precursor; IBA:GO_Central.
DR GO; GO:0008173; F:RNA methyltransferase activity; IBA:GO_Central.
DR GO; GO:0016435; F:rRNA (guanine) methyltransferase activity; IBA:GO_Central.
DR GO; GO:0008650; F:rRNA (uridine-2'-O-)-methyltransferase activity; IBA:GO_Central.
DR GO; GO:0008649; F:rRNA methyltransferase activity; ISS:dictyBase.
DR GO; GO:0000453; P:enzyme-directed rRNA 2'-O-methylation; IEA:UniProtKB-UniRule.
DR GO; GO:0000466; P:maturation of 5.8S rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA); IBA:GO_Central.
DR GO; GO:0000463; P:maturation of LSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA); IBA:GO_Central.
DR GO; GO:0001510; P:RNA methylation; IBA:GO_Central.
DR GO; GO:0031167; P:rRNA methylation; ISS:dictyBase.
DR Gene3D; 3.40.50.150; -; 1.
DR HAMAP; MF_01547; RNA_methyltr_E; 1.
DR HAMAP; MF_03163; RNA_methyltr_E_SPB1; 1.
DR InterPro; IPR002877; RNA_MeTrfase_FtsJ_dom.
DR InterPro; IPR015507; rRNA-MeTfrase_E.
DR InterPro; IPR012920; rRNA_MeTfrase_SPB1-like_C.
DR InterPro; IPR024576; rRNA_MeTfrase_Spb1_DUF3381.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR InterPro; IPR028589; SPB1-like.
DR Pfam; PF11861; DUF3381; 1.
DR Pfam; PF01728; FtsJ; 1.
DR Pfam; PF07780; Spb1_C; 1.
DR SUPFAM; SSF53335; SSF53335; 1.
PE 3: Inferred from homology;
KW Coiled coil; Methyltransferase; Nucleus; Reference proteome;
KW Ribosome biogenesis; rRNA processing; S-adenosyl-L-methionine; Transferase.
FT CHAIN 1..833
FT /note="pre-rRNA 2'-O-ribose RNA methyltransferase"
FT /id="PRO_0000328496"
FT REGION 323..349
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 363..453
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 475..640
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 730..767
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 779..833
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 336..386
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03163"
FT COILED 455..485
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03163"
FT COMPBIAS 323..345
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 378..423
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 424..445
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 475..491
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 575..597
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 750..767
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 794..826
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 158
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03163"
FT BINDING 57
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03163"
FT BINDING 59
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03163"
FT BINDING 77
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03163"
FT BINDING 93
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03163"
FT BINDING 118
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03163"
SQ SEQUENCE 833 AA; 95880 MW; A7AAF9C8C837BFB9 CRC64;
MGQKKKKLAK GRLDKFYYMA KEQGYRSRAA FKLIQLNKKY NFLGTAKACL DLCAAPGGWM
QVASKYMPVQ SLIVGVDLVP IRQVRNCIGL TEDITTQKCR TEIKKALKTW KVDVCLHDGA
PNMGTSWVQD AYQQAELTLH ALKLATEFLT TGGWFVTKVF RGSDYNSLIW VFNKLFKKVE
STKPPSSRNA SAEIFVVCQG FLNPKRIDPK LLDPKFVFKE IQEVKKVDVL SEKKKVNRAG
YEDGVTVLYK KGFISDFVNS NEHLQDLANF NAFEFDEAAK IFEQHELTTP EIKELVKDLK
VLNKNDFQKI IKWKKAMAAY KEKLDNPDEE ETEKPEEKKE LTAEEMEENL QEEMKEYLAL
VEKKKRKEKK RQNELKRKHQ RKIELTMHIP GDKIEETTDG DLYSMKGKDE FDEDIVADHS
DISSDEFDSD DSDDDDDDDN NGDSKLIDDD EYLEQQLDEQ YKLYQQRIRK KAAKLDDVKV
KKDKIGQDGY NEDDEEFVEE QEESNPLLVG NKRKEPDAQA VSSLFFDNEL FGGVEYRNPG
DSESEPEQDG DDDQDDENNK PIDISKLKKQ KPQAAQPITK KQKTTNSAEF GKQKSKYQKN
PTLDDKDDQD DDDDKGNSIK GFEEVPVQEE VEYESDSDED IDDKIKTKAL GEFLIRKKSR
QDLIDDSFNK YAFNDTGLPN WFTDDENRHN KAQTPLTKEM VDEIRRKIKE IDDRPIKKIA
EAKARKKYRL GKKMEKTRDK ASSIVDNPEM SNREKSKAIE KLYSGTDKKN MKPKKIIMIA
KKSKTAGGGT GKYKIVDKRM KKDLRAQKNK LKTVGRSKDS SKKSKPSGGK NKK
