ID E9F3S2_METRA Unreviewed; 840 AA.
AC E9F3S2;
DT 05-APR-2011, integrated into UniProtKB/TrEMBL.
DT 05-APR-2011, sequence version 1.
DT 08-NOV-2023, entry version 53.
DE SubName: Full=AdoMet-dependent rRNA methyltransferase spb1 {ECO:0000313|EMBL:EFY97608.1};
GN ORFNames=MAA_06833 {ECO:0000313|EMBL:EFY97608.1};
OS Metarhizium robertsii (strain ARSEF 23 / ATCC MYA-3075) (Metarhizium
OS anisopliae (strain ARSEF 23)).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Clavicipitaceae; Metarhizium.
OX NCBI_TaxID=655844 {ECO:0000313|EMBL:EFY97608.1, ECO:0000313|Proteomes:UP000002498};
RN [1] {ECO:0000313|EMBL:EFY97608.1, ECO:0000313|Proteomes:UP000002498}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ARSEF 23 / ATCC MYA-3075 {ECO:0000313|Proteomes:UP000002498};
RX PubMed=21253567; DOI=10.1371/journal.pgen.1001264;
RA Gao Q., Jin K., Ying S.H., Zhang Y., Xiao G., Shang Y., Duan Z., Hu X.,
RA Xie X.Q., Zhou G., Peng G., Luo Z., Huang W., Wang B., Fang W., Wang S.,
RA Zhong Y., Ma L.J., St Leger R.J., Zhao G.P., Pei Y., Feng M.G., Xia Y.,
RA Wang C.;
RT "Genome sequencing and comparative transcriptomics of the model
RT entomopathogenic fungi Metarhizium anisopliae and M. acridum.";
RL PLoS Genet. 7:E1001264-E1001264(2011).
RN [2] {ECO:0000313|EMBL:EFY97608.1, ECO:0000313|Proteomes:UP000002498}
RP GENOME REANNOTATION.
RC STRAIN=ARSEF 23 / ATCC MYA-3075 {ECO:0000313|Proteomes:UP000002498};
RX PubMed=25368161; DOI=10.1073/pnas.1412662111;
RA Hu X., Xiao G., Zheng P., Shang Y., Su Y., Zhang X., Liu X., Zhan S.,
RA St Leger R.J., Wang C.;
RT "Trajectory and genomic determinants of fungal-pathogen speciation and host
RT adaptation.";
RL Proc. Natl. Acad. Sci. U.S.A. 111:16796-16801(2014).
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:EFY97608.1}.
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DR EMBL; ADNJ02000005; EFY97608.1; -; Genomic_DNA.
DR RefSeq; XP_007823022.1; XM_007824831.1.
DR AlphaFoldDB; E9F3S2; -.
DR GeneID; 19261119; -.
DR KEGG; maj:MAA_06833; -.
DR HOGENOM; CLU_009422_8_1_1; -.
DR OrthoDB; 119516at2759; -.
DR Proteomes; UP000002498; Unassembled WGS sequence.
DR GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
DR GO; GO:0008649; F:rRNA methyltransferase activity; IEA:InterPro.
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 234..392
FT /note="DUF3381"
FT /evidence="ECO:0000259|Pfam:PF11861"
FT DOMAIN 627..835
FT /note="Ribosomal RNA methyltransferase SPB1-like C-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF07780"
FT REGION 364..388
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 439..554
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 595..649
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 802..840
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 739..766
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03163"
FT COMPBIAS 455..471
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 472..503
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 504..539
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 595..621
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 622..649
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 814..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: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; 94842 MW; 64F8582BAE774D86 CRC64;
MAIQKKHGKG RLDKWYKLAK EKGYRARAAF KLIQLNKKYG FLEKSKVLLD LCAAPGSWCQ
VAAEVMPMNS LIVGVDLAPI KPIPRVITFQ SDITTENCRA TIRQHLKTWK ADTVLHDGAP
NVGTAWAQDS FNQAELALQS MKLATEFLVE GGTFVTKVFR SKDYNPLLWV LNQLFTKVEA
TKPPSSRNVS AEIFVVCRGF KAPKRIDPRF LDPRYVFAEL TGATPNNEAK VYNPEVKKRK
REGYDEGDYI LYKEVPASEF IQTTDPIAIL GSCNKLTFSQ PRGGDIALAA LDKLPETTEE
IRQCCQDLKV LGRKDFKLLL KWRLKARGIF GFSTKEKDQE EAAIGEEVVE VESMDEELRL
QEELQSMKDK ENSKKKRERR KENEKKQREI VRMQLNMVAP MDIGMEESGP IGEGAMFSLK
SADKSGALRR LNRGKMVVVP GQTPVAAQNV AEESDGGENE NDDEEDFLER ELDSMYENYR
ERKAEADAKY RAKKAREERP DDEWEGLSAD EDAEKSDSSE LEEEEDDSSD DEEDEPARSL
LTDLDDSAPS SDGLSKRAAA FFSQDIFKDF TTSEKDVDII GNNFAEKLAV NGQSSKNKQL
NGAHASSKKA VQSQTQTNQT HSQEHNDDED NDFEVVKSNN ADDWEEDKRL PDGKLDIDII
TAEAMTLAHQ LASGQKTSHD AIDDGFNKHA FRDREGLPEW FIDDEGKHDK PHKPITKAAA
NAIKEKLRAF NARPIKKVRE AKARKKLKAA QKLEKLKKKS DMLANDEGMT EKEKAESIAK
LLSKAARKKP TQPAKLVVAR GLNRGVQGRP KGVRGRYRMV DPRMKKELRA QKRISQKKKR
//
