ID A0A218UAT1_9PASE Unreviewed; 834 AA.
AC A0A218UAT1;
DT 27-SEP-2017, integrated into UniProtKB/TrEMBL.
DT 27-SEP-2017, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=pre-rRNA processing protein FTSJ3 {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};
DE AltName: Full=Protein ftsJ homolog 3 {ECO:0000256|HAMAP-Rule:MF_03163};
DE AltName: Full=Putative rRNA methyltransferase 3 {ECO:0000256|HAMAP-Rule:MF_03163};
GN Name=FTSJ3 {ECO:0000256|HAMAP-Rule:MF_03163,
GN ECO:0000313|EMBL:OWK50701.1};
GN ORFNames=RLOC_00011144 {ECO:0000313|EMBL:OWK50701.1};
OS Lonchura striata domestica (Bengalese finch).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Passeriformes; Passeroidea; Estrildidae;
OC Estrildinae; Lonchura.
OX NCBI_TaxID=299123 {ECO:0000313|EMBL:OWK50701.1, ECO:0000313|Proteomes:UP000197619};
RN [1] {ECO:0000313|EMBL:OWK50701.1, ECO:0000313|Proteomes:UP000197619}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=White83orange57 {ECO:0000313|EMBL:OWK50701.1};
RA Colquitt B.M., Brainard M.S.;
RT "Genome of assembly of the Bengalese finch, Lonchura striata domestica.";
RL Submitted (MAY-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Probable methyltransferase involved in the processing of the
CC 34S pre-rRNA to 18S rRNA and in 40S ribosomal subunit formation.
CC {ECO:0000256|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:0000256|HAMAP-
CC Rule:MF_03163};
CC -!- SUBUNIT: Interacts with NIP7. {ECO:0000256|HAMAP-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}.
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:OWK50701.1}.
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DR EMBL; MUZQ01000513; OWK50701.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A218UAT1; -.
DR STRING; 299123.ENSLSDP00000004322; -.
DR OrthoDB; 119516at2759; -.
DR Proteomes; UP000197619; Unassembled WGS sequence.
DR GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
DR GO; GO:0030688; C:preribosome, small subunit precursor; IEA:UniProtKB-UniRule.
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 Coiled coil {ECO:0000256|HAMAP-Rule:MF_03163};
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 Reference proteome {ECO:0000313|Proteomes:UP000197619};
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 24..200
FT /note="Ribosomal RNA methyltransferase FtsJ"
FT /evidence="ECO:0000259|Pfam:PF01728"
FT DOMAIN 232..399
FT /note="DUF3381"
FT /evidence="ECO:0000259|Pfam:PF11861"
FT DOMAIN 621..827
FT /note="Ribosomal RNA methyltransferase SPB1-like C-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF07780"
FT REGION 334..354
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 442..526
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 547..635
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 799..834
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 728..765
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03163"
FT COMPBIAS 456..475
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 616..635
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 157
FT /note="Proton acceptor"
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 58
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03163"
FT BINDING 76
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03163"
FT BINDING 92
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03163"
FT BINDING 117
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03163"
SQ SEQUENCE 834 AA; 95442 MW; B573DB2812F6B0D5 CRC64;
MGKKSKLGKS RRDKFYHLAK ETGFRSRSSF KLLQLNRKFQ FLQKARALLD LCAAPGGWLQ
VASKFMPVSS LIIGVDLVPI KPIPNVVTLQ EDITTEKCRQ ALRKELQTWK VDVVLNDGAP
NVGASWVHDA YSQANLTLMA LKLACEFLCK GGWFITKVFR SRDYQSLLWI FQQFFQKVQA
TKPQASRNES AEIFVVCQGY QAPDKIDSKF FDPKYAFKDV EVATKSVSEL VSKKKPKAEG
YAEGDTTLYH RFTLMDFLKA PNPVDFLSKA NEITLGDGEL ENHSSTTEEL RQCCRDIRVL
GRKELRALLN WRTKLRRFLA KKLKEQAKEL DINLSSGEEE EGREEEKKEK MEAKAAAAEE
AKEQEEVELA LAEMKAKELA ELKRKKKKIL KEQRKQRERV ELQMDLPGVS IADDGDTSMF
SLKSIHRTPL LDELSRGDMA SADALLENGP GDDDIYVSDH DEEDDVSLAS DLDPEELLEI
EARQRKLQRE QRGKRAKFKQ KEEEEDDDEG QDVENPLLVP LEEKSVLEER QTSLWFGKDA
FAGIEDDADE ELELGQAQML AERQREAQRD KTTKKGQKKK KKVAQEEVPA EPTPTAAAAP
DASEAQEEQS SDDDSSSEDE RPLAPVGRKR GRVEPCGFEV VPIENPVKRV LDAEGLALGS
VIATSKKARR DLIDDSFNRY SYNEEEGELP EWFTEEERQH RRRQLPVDKQ TVEAYRQRWK
EINARPIKKV AEAKARKKRR MLKKLEQMKK KAEAVVSTVD ISEREKVAQL RRIYKKAGLA
KEKRQVTYLV AKKGVGRRVR RPPGVKGQFK VVDSRLKKDV RAQKRKEQKK KRHK
//
