SPB1_PONAB
ID SPB1_PONAB Reviewed; 841 AA.
AC Q5RAS1;
DT 16-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 83.
DE RecName: Full=pre-rRNA 2'-O-ribose RNA methyltransferase FTSJ3 {ECO:0000255|HAMAP-Rule:MF_03163};
DE EC=2.1.1.- {ECO:0000255|HAMAP-Rule:MF_03163};
DE AltName: Full=Protein ftsJ homolog 3 {ECO:0000255|HAMAP-Rule:MF_03163};
DE AltName: Full=Putative rRNA methyltransferase 3 {ECO:0000255|HAMAP-Rule:MF_03163};
GN Name=FTSJ3 {ECO:0000255|HAMAP-Rule:MF_03163};
OS Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney;
RG The German cDNA consortium;
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: RNA 2'-O-methyltransferase involved in the processing of the
CC 34S pre-rRNA to 18S rRNA and in 40S ribosomal subunit formation.
CC {ECO:0000255|HAMAP-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 -!- SUBUNIT: Interacts with NIP7. {ECO:0000255|HAMAP-Rule:MF_03163}.
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000255|HAMAP-
CC Rule:MF_03163}.
CC -!- PTM: Citrullinated by PADI4. {ECO:0000250|UniProtKB:Q9DBE9}.
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; CR858941; CAH91139.1; -; mRNA.
DR RefSeq; NP_001125667.1; NM_001132195.1.
DR AlphaFoldDB; Q5RAS1; -.
DR SMR; Q5RAS1; -.
DR STRING; 9601.ENSPPYP00000009585; -.
DR Ensembl; ENSPPYT00000009969; ENSPPYP00000009586; ENSPPYG00000008532.
DR GeneID; 100172587; -.
DR KEGG; pon:100172587; -.
DR CTD; 117246; -.
DR eggNOG; KOG1098; Eukaryota.
DR GeneTree; ENSGT00550000075004; -.
DR InParanoid; Q5RAS1; -.
DR OrthoDB; 1362679at2759; -.
DR Proteomes; UP000001595; Chromosome 17.
DR GO; GO:0005694; C:chromosome; IEA:Ensembl.
DR GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
DR GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR GO; GO:0030688; C:preribosome, small subunit precursor; IEA:UniProtKB-UniRule.
DR GO; GO:0062105; F:RNA 2'-O-methyltransferase activity; ISS:UniProtKB.
DR GO; GO:0008649; F:rRNA methyltransferase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0000453; P:enzyme-directed rRNA 2'-O-methylation; IEA:UniProtKB-UniRule.
DR GO; GO:0001510; P:RNA methylation; ISS:UniProtKB.
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 2: Evidence at transcript level;
KW Citrullination; Coiled coil; Isopeptide bond; Methyltransferase; Nucleus;
KW Phosphoprotein; Reference proteome; Ribosome biogenesis; rRNA processing;
KW S-adenosyl-L-methionine; Transferase; Ubl conjugation.
FT CHAIN 1..841
FT /note="pre-rRNA 2'-O-ribose RNA methyltransferase FTSJ3"
FT /id="PRO_0000155579"
FT REGION 332..366
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 454..482
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 579..654
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 805..841
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 356..404
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03163"
FT COILED 733..771
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03163"
FT COMPBIAS 351..366
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 454..470
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 621..654
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 812..829
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 157
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03163"
FT BINDING 56
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03163"
FT BINDING 58
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03163"
FT BINDING 76
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03163"
FT BINDING 92
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03163"
FT BINDING 117
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03163"
FT MOD_RES 333
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8IY81"
FT MOD_RES 335
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8IY81"
FT MOD_RES 336
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8IY81"
FT MOD_RES 347
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8IY81"
FT MOD_RES 356
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8IY81"
FT MOD_RES 389
FT /note="Citrulline"
FT /evidence="ECO:0000250|UniProtKB:Q9DBE9"
FT MOD_RES 547
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8IY81"
FT MOD_RES 567
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q8IY81"
FT MOD_RES 578
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8IY81"
FT MOD_RES 638
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8IY81"
FT MOD_RES 670
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8IY81"
FT MOD_RES 682
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8IY81"
FT MOD_RES 777
FT /note="Citrulline"
FT /evidence="ECO:0000250|UniProtKB:Q9DBE9"
FT CROSSLNK 357
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q8IY81"
FT CROSSLNK 573
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q8IY81"
FT CROSSLNK 637
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q8IY81"
FT CROSSLNK 653
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q8IY81"
FT CROSSLNK 672
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q8IY81"
FT CROSSLNK 704
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q8IY81"
SQ SEQUENCE 841 AA; 95795 MW; 6D1B7960B1184BF6 CRC64;
MGKKGKVGKS RRDKFYHLAK ETGYRSRSAF KLIQLNRRFQ FLQKARALLD LCAAPGGWLQ
VAAKFMPVSS LIVGVDLVPI KPLPNVVTLQ EDITTERCRQ ALRKELKTWK VDVVLNDGAP
NVGASWVHDA YSQAHLTLMA LRLACDFLAR GGSFITKVFR SRDYQPLLWI FQQLFRRVQA
TKPQASRHES AEIFVVCQGF LAPDKVDSKF FDPKFAFKEV EVQAKTVTEL VTKKKPKAEG
YAEGDLTLYH RTSVTDFLRA ANPVDFLSKA SEIMVDDEEL AQHPATTEDI RVCCQDIRVL
GRKELRSLLN WRTKLRRYVA KKLKEQAKAL DISLSSGEED EGNEEDSTAG TTEQPSKEEE
EEEQLNQTLA EMKAQEVAEL KRKKKKLLRE QRKQRERVEL KMDLPGVSIA DEGETGMFSL
RTIRGQQLLE EVTQGDMSAA DTFLSDLPRD DIYVSDVEDD GDDTSLDSDL DPEELAGVRG
HQGLRDQKRV RLTEVQDDKE EEEEEENPLL VPLEEKAVLQ EEQANLWFSK GSFAGIEDDA
DEALEISQAQ LLFESQRKGR QQQLPQTLPS CLKTEIMSPL YQDEAPKGTE ASSGTEAATG
LKGEEKDGIS DSDSSSSSEE EESWEPVRGK KRSRGPKSDD DGFEIVPIED PAKHRILDPE
GLALGAVIAS SKKAKRDLID NSFNRYTFNE DEGELPEWFV QEEKQHRIRQ LPIGKKEMEH
YRKRWREINA RPIKKVAEAK ARKKRRMLKR LEQTRKKAEA VVNTVDISER EKVAQLRSLY
KKAGLGKEKR HVTYVVAKKG VGRKVRRPAG VRGHFKVVDS RMKKDQRAQQ RKEQKKKHKR
K
