ID A0A1J4MFB1_9CRYT Unreviewed; 1019 AA.
AC A0A1J4MFB1;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 24-JAN-2024, entry version 27.
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};
GN ORFNames=cubi_01637 {ECO:0000313|EMBL:OII72687.1};
OS Cryptosporidium ubiquitum.
OC Eukaryota; Sar; Alveolata; Apicomplexa; Conoidasida; Coccidia;
OC Eucoccidiorida; Eimeriorina; Cryptosporidiidae; Cryptosporidium.
OX NCBI_TaxID=857276 {ECO:0000313|EMBL:OII72687.1, ECO:0000313|Proteomes:UP000186176};
RN [1] {ECO:0000313|EMBL:OII72687.1, ECO:0000313|Proteomes:UP000186176}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=39726 {ECO:0000313|EMBL:OII72687.1};
RA Liu S., Roellig D.M., Guo Y., Li N., Frace M.A., Tang K., Zhang L.,
RA Feng Y., Xiao L.;
RT "Reductive evolution of mitochondrial metabolism and differential evolution
RT of invasion-related proteins in Cryptosporidium.";
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
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}.
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:OII72687.1}.
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DR EMBL; LRBP01000020; OII72687.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1J4MFB1; -.
DR VEuPathDB; CryptoDB:cubi_01637; -.
DR OrthoDB; 119516at2759; -.
DR Proteomes; UP000186176; 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 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 283..464
FT /note="DUF3381"
FT /evidence="ECO:0000259|Pfam:PF11861"
FT DOMAIN 780..1006
FT /note="Ribosomal RNA methyltransferase SPB1-like C-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF07780"
FT REGION 238..265
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 386..416
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 531..554
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 635..655
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 714..752
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 788..814
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 991..1019
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 435..468
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03163"
FT COMPBIAS 398..412
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 536..554
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 788..803
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 992..1019
FT /note="Basic 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 1019 AA; 117779 MW; D637F88409EFFB3B CRC64;
MGRRAKTGKD RLDRYYHLAK EQGYRARSAF KLIQLAQKFN IFKNCEILVD LCAAPGGWLQ
VAKRNMGVSS KIIGVDLVAI KGIPGVTTFK CDITTERCKK LIFDELNGIP VDVVLHDGAP
NVGTSWDKDA YIQNELVLHS AKLACEILKP NGIFVTKVFR STDYNSVLWV LSQLFKTVKA
TKPQSSRNVS AEIFLVCLGY KAPKKIDSRF FDPKYVFQSN KGENEGVDLD SFGNNLNKDH
YGDDSDGDSD SDNMDDHENK LLTRKTRKNM KSSLSELIKG IGKRNRDGYE KGDDFRVVSA
YDFFHAENPA LVLLKSNTIN LNPKKADESN TLEREFIDLV LNHPKTTYEI KLLCEDLKVL
GKKELMQLLK WRFLVFKDIK SSQSKKDSLQ GKENNITDSD DDETELDDNG DADNHENDNI
IQESEEEDNC QGEIDQELLD MLKEQRRRNK ILEKKKRLQQ RKREWRASLS KGGFDVEGNE
QDLFKYTKEV AKVLDNEERD VSIDGYFPEG VHFNDNFLLG DDFKISSQEI QDGGNKVRDN
SSDESNDSND EELDHKDLLG IDLDIQDYIK RNKIMQGGDS KLERQKSRLL GQKKETRREK
VISDWVEEMN QFSNKIEEEN QRVLAKKAFD QIYSSDDDTD FEDDNNNDNK KKNKVSETNK
LKSMKDETQE LFDYKNDIKK DTLSNRWFSN SVFNDFIGEE KTQNTEDGTI IRELSDSEIP
QIPMNEKKLK KLKNKKSQDK NKENSKNNEI EFVPKSAGSI NINDGIEECF NQNNNDEYDQ
DQKDMEEEVN FDSVDSDDED TQDSDSERFT KPENEEELKM IQGIGSLLVN KSTRMDLIDG
SYNRYAFHDP AEDLENNVLG LPSWFVEDEN KHNKPELPIT KDLMAQYKAK LREIKNRPIR
KESEALARKK RRYEKIMEKA RKKAQSIADS EEMNEASKSK TINNLIKKAQ KVSSKKRVNV
YTVTRRHGLS KQVKNKDKNI NSTNLKTKFV DKRLKKDKRA VKHINKKKKH MSKKRNKKR
//
