ID A0A2T4H2S5_FUSCU Unreviewed; 830 AA.
AC A0A2T4H2S5;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 24-JAN-2024, entry version 23.
DE SubName: Full=AdoMet-dependent rRNA methyltransferase SPB1 {ECO:0000313|EMBL:PTD10102.1};
GN ORFNames=FCULG_00007859 {ECO:0000313|EMBL:PTD10102.1};
OS Fusarium culmorum.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium.
OX NCBI_TaxID=5516 {ECO:0000313|EMBL:PTD10102.1, ECO:0000313|Proteomes:UP000241587};
RN [1] {ECO:0000313|EMBL:PTD10102.1, ECO:0000313|Proteomes:UP000241587}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PV {ECO:0000313|EMBL:PTD10102.1,
RC ECO:0000313|Proteomes:UP000241587};
RA Schmidt R.;
RT "Fusarium culmorum secondary metabolites in fungal-bacterial-plant
RT interactions.";
RL Submitted (FEB-2018) to the EMBL/GenBank/DDBJ databases.
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:PTD10102.1}.
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DR EMBL; PVEM01000003; PTD10102.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2T4H2S5; -.
DR OMA; DITTEDC; -.
DR Proteomes; UP000241587; 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 Reference proteome {ECO:0000313|Proteomes:UP000241587};
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 241..381
FT /note="DUF3381"
FT /evidence="ECO:0000259|Pfam:PF11861"
FT DOMAIN 620..827
FT /note="Ribosomal RNA methyltransferase SPB1-like C-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF07780"
FT REGION 352..380
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 423..549
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 589..639
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 736..763
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03163"
FT COMPBIAS 457..493
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 494..523
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 620..639
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 830 AA; 93916 MW; 3E339360739BC8AD CRC64;
MAVTKEKAKG RLDKWYRLAK EKGYRARAAF KLIQLNKKYG FLEKSRVLID LCAAPGSWLQ
VAAEVMPQGS LIVGCDLSPI KPIPRVTSFQ SDITSEDCRA TLKRLIKSFP VDTVIHDGAP
NVGTAWTQDA FDQNALVLQS LKLATEFLKP DGTFVTKVFR SKDYNSLLWV FKQLFNKVEA
TKPSSSRNVS SEIFVVCRGY KAPKKMDPRF LDPTYVFAEL AGPTPNNEAK VYNPKSRSAS
EMFKEMPASE FIQTTDPIAV LGSYNKLSFQ QPRNGDVALA ALDKLPETTD EIRNSCSDLR
VLGRKDFKLL LKWRLKVREI FGFETKKALG TAETEEVAEV ESMDEELKIQ QELEDMKDKE
NSKRRREKRR ENERKQREIV RMQLNMTAPM DIGMEEAGPI GEGAMFSLKK VDKTDAMRRL
NRGKMIVPSQ APQKQLDSGL GSSGETDDES DPEEDRLERE LDSMYDHYKE RKSEIDAKYR
AKKARKEHGD DEWEGLSGEE ADEKNDSSDL EEDDSSDDDD EDAAPSQGLI RDLDSSKGAN
GLSKRATNFF NQDVFQGITG IVPEEEEESA EDSADEEINR DAAAVVAQQS KARKVETPAA
KPVEINDTTV DSDSDMEGNE NGFEVVKRTE EDDWDKDQRR ADGRLDIDII TAEAMTLAHQ
LATGQKTTHD AIDDGFNKYA FRDRDGLPDW FVEDETKHDR LQKPITKAAA QAIKEKMRAF
NARPIKKVRE AKARKKFKAA QQLEKLKKKS DMLNNDENMT EKEKAESIGR LMARAQKKKP
VKQAAKLVVA RGLNRGIKGR PKGVKGRYRI VDPRMKKELR AQKRISKKKK
//
