ID K9IN37_DESRO Unreviewed; 840 AA.
AC K9IN37;
DT 06-FEB-2013, integrated into UniProtKB/TrEMBL.
DT 06-FEB-2013, sequence version 1.
DT 27-MAR-2024, entry version 36.
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};
OS Desmodus rotundus (Vampire bat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Chiroptera; Microchiroptera; Phyllostomidae;
OC Desmodontinae; Desmodus.
OX NCBI_TaxID=9430 {ECO:0000313|EMBL:JAA49193.1};
RN [1] {ECO:0000313|EMBL:JAA49193.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Salivary gland {ECO:0000313|EMBL:JAA49193.1};
RA Francischetti I.M.B., Assumpcao T.C.F., Ma D., Vicente E.C.,
RA Ribeiro J.M.C.;
RT "The Vampirome: Transcriptome and Proteome Analysis of the Submandibular
RT and Accessory Glands of the Vampire Bat and Vector of Human Rabies,
RT Desmodus rotundus.";
RL Submitted (NOV-2012) 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}.
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DR EMBL; GABZ01004332; JAA49193.1; -; mRNA.
DR AlphaFoldDB; K9IN37; -.
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 2: Evidence at transcript level;
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 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..396
FT /note="DUF3381"
FT /evidence="ECO:0000259|Pfam:PF11861"
FT DOMAIN 616..832
FT /note="Ribosomal RNA methyltransferase SPB1-like C-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF07780"
FT REGION 334..365
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 457..510
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 547..646
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 805..840
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 733..770
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03163"
FT COMPBIAS 347..365
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 470..494
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 495..509
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 553..573
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 620..646
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 811..831
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 840 AA; 95645 MW; F2F9C94E5010F6CB CRC64;
MGKKGKVGKS RRDKFYHLAK ETGYRSRSAF KLIQLNRRFQ FLQKARALLD LCAAPGGWLQ
VAAKFMPVSS LIVGVDLVPI KPLPNVVTLQ EDITTERCRQ ALRKELKTWK VDVVLNDGAP
NVGASWVHDA YSQAHLTLMA LRLACDFLAR GGYFITKVFR SRDYQPLLWI FQQLFRHVQA
TKPQASRHES AEIFVVCQGF LAPDKVDSKF FDPKFAFKEV EVQAKTVTEL VTKKKPKAEG
YAEGDLTLYH RTSVTDFLRA ANPVDFLSKA SEIVLDEEEL AQHPATTEDI WVCCQDIKVL
GRKELRSLLN WRTKLRRYVA KKLKEQAKAL DISLSSGEEE EGDEEESTAG NVRQISEEEE
EEQLNRTLAE MKAQEVAELK RKKKKLLREQ RKQRERVELK MDLPGVSIAD EGETGMFSLR
TIRGHQLLEE VTQGDMSAAD TFLSDLPRDD IYVSDVEDDE EASLDSDLDP EELAGVRGHQ
SLKDQKRLSV QFAEAEDDKE EEDEEENPLL VPLEEKAVLQ EEQANLWFSK DGFSGIEDDA
DEALEISQAQ LLYESRRKGQ SQPPPPSSLK TESKPSRYQD EAPKEAKAPS GAEASSGMEA
ATGGEDSNDS SDSDSSSEDE ESLEPRHSKK RSRGPKSDDD GFEIVPIQDP VKHQILDPEG
LALGAIIASS KKAKRDLIDN SFNRYTFNED EGELPEWFVQ EEKQHRIRQL PIDKKEVEHY
RKRWREINAR PIKKVAEAKA RKKRRMLKKL EQTKKKAEAV VNTVDISERE KVAQLRSLYK
KAGLGKEKRH VTYVVAKKGV GRKVRRPAGV RGHFKVVDSR MKKDQRALQR KEQKKKNRRK
//
