ID N1QKF3_SPHMS Unreviewed; 674 AA.
AC N1QKF3;
DT 26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT 26-JUN-2013, sequence version 1.
DT 27-MAR-2024, entry version 42.
DE SubName: Full=NOL1/NOP2/sun family putative RNA met {ECO:0000313|EMBL:EMF12280.1};
GN ORFNames=SEPMUDRAFT_149983 {ECO:0000313|EMBL:EMF12280.1};
OS Sphaerulina musiva (strain SO2202) (Poplar stem canker fungus) (Septoria
OS musiva).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetidae; Mycosphaerellales; Mycosphaerellaceae; Sphaerulina.
OX NCBI_TaxID=692275 {ECO:0000313|EMBL:EMF12280.1, ECO:0000313|Proteomes:UP000016931};
RN [1] {ECO:0000313|EMBL:EMF12280.1, ECO:0000313|Proteomes:UP000016931}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SO2202 {ECO:0000313|EMBL:EMF12280.1,
RC ECO:0000313|Proteomes:UP000016931};
RX PubMed=23236275; DOI=10.1371/journal.ppat.1003037;
RA Ohm R.A., Feau N., Henrissat B., Schoch C.L., Horwitz B.A., Barry K.W.,
RA Condon B.J., Copeland A.C., Dhillon B., Glaser F., Hesse C.N., Kosti I.,
RA LaButti K., Lindquist E.A., Lucas S., Salamov A.A., Bradshaw R.E.,
RA Ciuffetti L., Hamelin R.C., Kema G.H.J., Lawrence C., Scott J.A.,
RA Spatafora J.W., Turgeon B.G., de Wit P.J.G.M., Zhong S., Goodwin S.B.,
RA Grigoriev I.V.;
RT "Diverse lifestyles and strategies of plant pathogenesis encoded in the
RT genomes of eighteen Dothideomycetes fungi.";
RL PLoS Pathog. 8:E1003037-E1003037(2012).
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus
CC {ECO:0000256|ARBA:ARBA00004604}.
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}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU01023}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; KB456265; EMF12280.1; -; Genomic_DNA.
DR RefSeq; XP_016760401.1; XM_016905890.1.
DR AlphaFoldDB; N1QKF3; -.
DR STRING; 692275.N1QKF3; -.
DR GeneID; 27903027; -.
DR eggNOG; KOG1122; Eukaryota.
DR HOGENOM; CLU_005316_3_2_1; -.
DR OMA; PIGSWTK; -.
DR OrthoDB; 1268at2759; -.
DR Proteomes; UP000016931; Unassembled WGS sequence.
DR GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0008173; F:RNA methyltransferase activity; IEA:InterPro.
DR GO; GO:0008757; F:S-adenosylmethionine-dependent methyltransferase activity; IEA:InterPro.
DR GO; GO:0042254; P:ribosome biogenesis; IEA:UniProtKB-KW.
DR GO; GO:0001510; P:RNA methylation; IEA:InterPro.
DR GO; GO:0006396; P:RNA processing; IEA:InterPro.
DR CDD; cd02440; AdoMet_MTases; 1.
DR Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR InterPro; IPR018314; Fmu/NOL1/Nop2p_CS.
DR InterPro; IPR031341; Methyltr_RsmF_N.
DR InterPro; IPR049560; MeTrfase_RsmB-F_NOP2_cat.
DR InterPro; IPR001678; MeTrfase_RsmB-F_NOP2_dom.
DR InterPro; IPR011023; Nop2p.
DR InterPro; IPR023267; RCMT.
DR InterPro; IPR023273; RCMT_NOP2.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR NCBIfam; TIGR00446; nop2p; 1.
DR PANTHER; PTHR22807:SF30; 28S RRNA (CYTOSINE(4447)-C(5))-METHYLTRANSFERASE-RELATED; 1.
DR PANTHER; PTHR22807; NOP2 YEAST -RELATED NOL1/NOP2/FMU SUN DOMAIN-CONTAINING; 1.
DR Pfam; PF01189; Methyltr_RsmB-F; 1.
DR Pfam; PF17125; Methyltr_RsmF_N; 1.
DR PRINTS; PR02008; RCMTFAMILY.
DR PRINTS; PR02012; RCMTNOP2.
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 Coiled coil {ECO:0000256|SAM:Coils};
KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603, ECO:0000256|PROSITE-
KW ProRule:PRU01023}; Reference proteome {ECO:0000313|Proteomes:UP000016931};
KW Ribosome biogenesis {ECO:0000256|ARBA:ARBA00022517};
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}.
FT DOMAIN 277..565
FT /note="SAM-dependent MTase RsmB/NOP-type"
FT /evidence="ECO:0000259|PROSITE:PS51686"
FT REGION 1..154
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 573..674
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 168..202
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 45..59
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 87..133
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 134..149
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 580..594
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 604..622
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 494
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT BINDING 369..375
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT BINDING 393
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT BINDING 437
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
SQ SEQUENCE 674 AA; 73761 MW; 6460F0802179CC2A CRC64;
MGKKQADPGP LDESLVTRKR KSGAPTNGAI KKQKVVEQRP QKPAKTLKRA QTNVSKQTVP
GKPLKVKKAK KAAAATPPTD SDDDAASLNG DAIDDPDVLE DAVGGIAEDL DFDDDSFGSD
ADDFADAPSD DDVDVSDTEM RKGKMWSDDE DSDAEETLTA ANIAGLSRKL DQERAQEAAE
AAEELQDDAL QTNIAAAELS DDEEGGARLA PDLQLLRTRI TEIVRVLTSF KELGEPGKSR
AEYTQSLLKD ICTYYGYSPF LAEKLFSLFP PQEALQFFDA NETPRPMVIR TNTLRTHRRD
LAHSLINRGV TLEPVGKWSK VGLQIFESQV PLGATPEYLA GHYILQAASS FLPVMALAPQ
EHERVLDMAA APGGKTTHLA ALMRNTGVIF SNDSNKDRAK GLIGNIHRLG VKNTIVCNYS
ALEFPKVMGG FDRVLLDAPC SGTGVIAKDA SVKTNKTEAD FLRLPHLQKQ LLLAAVDSVD
HASKTGGYIV YSTCSVTVEE NEQVVQYVLN KRPNVKLVPT GLVFGKEGFT KFQSKRFYPS
MKETRRYYPH AYNVDGFFVA KFKKIAVTPT NAVRAQGSAE EKKQQQKHSG NGEEEEEIVD
NEEIFDDEKN KNADGTEKDA DDDFGGFDSE EDNKVMERLM RKKLKKKGLN PNAKDSKAVK
TMLGGGGKKT AVVK
//
