ID W2S620_9EURO Unreviewed; 834 AA.
AC W2S620;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE RecName: Full=SAM-dependent MTase RsmB/NOP-type domain-containing protein {ECO:0000259|PROSITE:PS51686};
GN ORFNames=HMPREF1541_10697 {ECO:0000313|EMBL:ETN44147.1};
OS Cyphellophora europaea CBS 101466.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Cyphellophoraceae; Cyphellophora.
OX NCBI_TaxID=1220924 {ECO:0000313|EMBL:ETN44147.1, ECO:0000313|Proteomes:UP000030752};
RN [1] {ECO:0000313|EMBL:ETN44147.1, ECO:0000313|Proteomes:UP000030752}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 101466 {ECO:0000313|EMBL:ETN44147.1,
RC ECO:0000313|Proteomes:UP000030752};
RG The Broad Institute Genomics Platform;
RA Cuomo C., de Hoog S., Gorbushina A., Walker B., Young S.K., Zeng Q.,
RA Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Allen A.W., Alvarado L.,
RA Arachchi H.M., Berlin A.M., Chapman S.B., Gainer-Dewar J., Goldberg J.,
RA Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., Ireland A.,
RA Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W., Priest M.,
RA Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Phialophora europaea CBS 101466.";
RL Submitted (MAR-2013) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC superfamily. RsmB/NOP family. {ECO:0000256|ARBA:ARBA00007494,
CC ECO:0000256|PROSITE-ProRule:PRU01023}.
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DR EMBL; KI635846; ETN44147.1; -; Genomic_DNA.
DR RefSeq; XP_008713589.1; XM_008715367.1.
DR AlphaFoldDB; W2S620; -.
DR STRING; 1220924.W2S620; -.
DR GeneID; 19978036; -.
DR VEuPathDB; FungiDB:HMPREF1541_10697; -.
DR eggNOG; KOG2198; Eukaryota.
DR HOGENOM; CLU_005316_4_2_1; -.
DR InParanoid; W2S620; -.
DR OrthoDB; 197651at2759; -.
DR Proteomes; UP000030752; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-KW.
DR GO; GO:0016428; F:tRNA (cytidine-5-)-methyltransferase activity; IEA:InterPro.
DR GO; GO:0000049; F:tRNA binding; IEA:UniProtKB-KW.
DR GO; GO:0030488; P:tRNA methylation; IEA:UniProt.
DR Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR InterPro; IPR018314; Fmu/NOL1/Nop2p_CS.
DR InterPro; IPR049560; MeTrfase_RsmB-F_NOP2_cat.
DR InterPro; IPR001678; MeTrfase_RsmB-F_NOP2_dom.
DR InterPro; IPR023267; RCMT.
DR InterPro; IPR023270; RCMT_NCL1.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR PANTHER; PTHR22808; NCL1 YEAST -RELATED NOL1/NOP2/FMU SUN DOMAIN-CONTAINING; 1.
DR PANTHER; PTHR22808:SF1; RNA CYTOSINE C(5)-METHYLTRANSFERASE NSUN2; 1.
DR Pfam; PF01189; Methyltr_RsmB-F; 1.
DR PRINTS; PR02008; RCMTFAMILY.
DR PRINTS; PR02011; RCMTNCL1.
DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR PROSITE; PS01153; NOL1_NOP2_SUN; 1.
DR PROSITE; PS51686; SAM_MT_RSMB_NOP; 1.
PE 3: Inferred from homology;
KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603, ECO:0000256|PROSITE-
KW ProRule:PRU01023}; Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000030752};
KW RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|PROSITE-
KW ProRule:PRU01023};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691,
KW ECO:0000256|PROSITE-ProRule:PRU01023};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PROSITE-
KW ProRule:PRU01023}; tRNA processing {ECO:0000256|ARBA:ARBA00022694};
KW tRNA-binding {ECO:0000256|ARBA:ARBA00022555}.
FT DOMAIN 58..457
FT /note="SAM-dependent MTase RsmB/NOP-type"
FT /evidence="ECO:0000259|PROSITE:PS51686"
FT REGION 1..36
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 194..222
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 465..485
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 498..517
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 523..576
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 780..834
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 533..564
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 786..800
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 344
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT BINDING 176..182
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT BINDING 231
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT BINDING 258
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT BINDING 291
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
SQ SEQUENCE 834 AA; 93465 MW; 1ABB7E79D9EEDB77 CRC64;
MGKRGGKKGG RGRGGWGGSR GPPRDNRVDK ATIPRKNDKF EQYYNQLDLV SEEEKPQLWE
AMRRDLPNSF RFTGSRSHAL AVQQRLRDFY IPEITSITYD GQLVEPPQPV SWYPNQLAWF
MTTPKHIIRR FPPFKSFQNF LVAETDVGNI TRQEIVSMIP PLLMDIKPGM TVLDLCAAPG
SKSAQLIEML HDGEEERSRK VAENTANGLA RPEGAEYEDD GRSPGLLIAN DVDYKRAHML
VHQVKRLSSP NIIVTNHDAT VFPSIKIPSE PTTEGKPAQN RYLKFDRILA DVPCSGDGTA
RKNLEIWSKW TPSNGLGLHA TQVRILVRAL QMLKVGGRVV YSTCSMNPVE DEAVLSAAIQ
RCGGQSFVQL VETEGYLPGL KRYAGLKKWS IMSKAGRIWH SYDEVLNEQA TRGEDTLSRL
TEGMFPPKDD LPLERAVRVY PHQHDTGAFF IAILEKKAEI KAKSEEKPVA APAMKVETAD
SSGTEVKLAT QLDGQIAAVQ NGAQSPKRKR DDEADVEPAV KRIKADANGS TEEHEAPQPS
KTTETKTSTP AAAASMLQPP IQQNSDRPRK DRNQPFEEPF KYLSPEIPEL ESIRTFYNLS
GRFPSDRFLV RNPAATATKN IYYTTALARD ILTENEGKGI KFVHAGIKMF VKQDAPSPEV
CPWRIQTDGL KVIEPWVGRQ RVIKLWRKET LRKLLVEMFP RFAGEEWRNL GEVGEQIQNV
GMGCCVLVVE PRAEEGDSGF NERMVFPLWK SIQSLNLMLP KEERKAMLLR LFNDSTELVN
LQQHPGGKRP EKKVEETTEQ VRVRNSSSPE SDVPPADAEG VDGEDGGVTL ERET
//
