ID I1PY11_ORYGL Unreviewed; 819 AA.
AC I1PY11;
DT 13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT 13-JUN-2012, sequence version 1.
DT 24-JAN-2024, entry version 49.
DE RecName: Full=Putative rRNA methyltransferase {ECO:0000256|HAMAP-Rule:MF_03163};
DE EC=2.1.1.- {ECO:0000256|HAMAP-Rule:MF_03163};
DE AltName: Full=2'-O-ribose RNA methyltransferase SPB1 homolog {ECO:0000256|HAMAP-Rule:MF_03163};
OS Oryza glaberrima (African rice).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Oryza.
OX NCBI_TaxID=4538 {ECO:0000313|EnsemblPlants:ORGLA05G0225900.1, ECO:0000313|Proteomes:UP000007306};
RN [1] {ECO:0000313|Proteomes:UP000007306}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IRGC 96717 {ECO:0000313|Proteomes:UP000007306};
RA Wing R.A., Yu Y., Rounsley S., Reddy-Marri P., Goicoechea J.L.,
RA Sisneros N., Lee S., Song X., Angelova A., Kudrna D.P., de Baynast K.,
RA Zuccolo A.;
RT "The complete genome of Oryza glaberrima.";
RL Submitted (JUN-2010) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EnsemblPlants:ORGLA05G0225900.1}
RP IDENTIFICATION.
RG EnsemblPlants;
RL Submitted (JUN-2015) to UniProtKB.
CC -!- FUNCTION: Probable methyltransferase involved in the maturation of rRNA
CC and in the biogenesis of ribosomal subunits. {ECO:0000256|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:0000256|HAMAP-
CC Rule:MF_03163};
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000256|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:0000256|HAMAP-Rule:MF_03163}.
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DR AlphaFoldDB; I1PY11; -.
DR STRING; 4538.I1PY11; -.
DR EnsemblPlants; ORGLA05G0225900.1; ORGLA05G0225900.1; ORGLA05G0225900.
DR Gramene; ORGLA05G0225900.1; ORGLA05G0225900.1; ORGLA05G0225900.
DR eggNOG; KOG1098; Eukaryota.
DR HOGENOM; CLU_009422_8_1_1; -.
DR OMA; DITTEDC; -.
DR Proteomes; UP000007306; Unassembled WGS sequence.
DR GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
DR GO; GO:0008649; F:rRNA methyltransferase activity; IEA:UniProtKB-UniRule.
DR Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 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 PANTHER; PTHR10920:SF13; PRE-RRNA 2'-O-RIBOSE RNA METHYLTRANSFERASE FTSJ3; 1.
DR PANTHER; PTHR10920; RIBOSOMAL RNA METHYLTRANSFERASE; 1.
DR Pfam; PF11861; DUF3381; 1.
DR Pfam; PF01728; FtsJ; 1.
DR Pfam; PF07780; Spb1_C; 1.
DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
PE 3: Inferred from homology;
KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603, ECO:0000256|HAMAP-
KW Rule:MF_03163};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|HAMAP-Rule:MF_03163};
KW Ribosome biogenesis {ECO:0000256|ARBA:ARBA00022517, ECO:0000256|HAMAP-
KW Rule:MF_03163}; rRNA processing {ECO:0000256|HAMAP-Rule:MF_03163};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691, ECO:0000256|HAMAP-
KW Rule:MF_03163};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_03163}.
FT DOMAIN 22..201
FT /note="Ribosomal RNA methyltransferase FtsJ"
FT /evidence="ECO:0000259|Pfam:PF01728"
FT DOMAIN 234..382
FT /note="DUF3381"
FT /evidence="ECO:0000259|Pfam:PF11861"
FT DOMAIN 590..789
FT /note="Ribosomal RNA methyltransferase SPB1-like C-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF07780"
FT REGION 225..246
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 362..395
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 422..453
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 470..626
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 713..732
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 772..819
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 364..381
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 424..450
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 470..493
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 494..516
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 537..555
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 557..609
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 610..626
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 718..732
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 783..805
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 158
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03163"
FT BINDING 54
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03163"
FT BINDING 56
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03163"
FT BINDING 74
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03163"
FT BINDING 90
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03163"
FT BINDING 118
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03163"
SQ SEQUENCE 819 AA; 92343 MW; A4CD868A4B1656E5 CRC64;
MGKTKGKQRQ DKFYHLAKEQ GYRSRAAFKL LQLDARFRFL PTARAVLDLC AAPGGWVQVA
VNHAPVGAFV VGVDLVPIRP IRGAHSLTED ITTTKCRAAV RRLMDSNGVA AFDVVLHDGS
PNVGGAWAQE ATAQSSLVID AVRLATMFLA PKGAFITKVF RSQDYNAIMY CLKQLFEKVE
VTKPTASRST SAEIYIICLR YKAPAKIQPE LLDIKHLFSV DPDPKKVRDP LKPDRQKRNR
DGYEEGNTTL RKVGLASDFI WSEGQTPLEF LGSFNAISFD DPASLPIKNH ELTTDEIKAL
CEDLYVLDKN SFKHILKWRI RIRKALSSSE VTKKTDDTAV EVNVKDDDQL LQEMEELTSV
IDRKKKREKK RQSKRRAKDK ARKATGMQID ATGDNYGDPD LFSISAIKGG KELQAIESAE
LNVEDAQGDS ENEDIQTREY SDEEMDSDEE QQRYDAQLEE MLDEAYERYV TKKGGEVKQE
RKRAKRVNTD ADEELLEGGE DDGDDVDMDQ GSDEEQDQET NPLLLSLDAE KPTKEQMMEQ
WFSQDVFTEA GTGVVEQSDS EDEREQLTRI AKKKADSGKK EKPAKAKRLQ QDDFEIVPAE
PVRTEDDSSS SSDESDELDE DLDDDTKAEV LAYAKKMLRK KQREQILDDA YNKYMFDDEG
LPKWFAEDEK RHNQPMKPVT KEEVAAMRAQ FKEIDARPAK KVAEAKARKK RVAMKKLDKA
RQKADAIADQ NDINEQSKRK MIDRIYKKAI PKKPQKEYVV AKKGVQVRAG KGKILVDKRM
KKDKRASKVK GGKGAKGKGK KGGGQKGGMR GKAGRKAQN
//
