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Database: UniProt
Entry: H6BPU3_EXODN
LinkDB: H6BPU3_EXODN
Original site: H6BPU3_EXODN 
ID   H6BPU3_EXODN            Unreviewed;       717 AA.
AC   H6BPU3;
DT   18-APR-2012, integrated into UniProtKB/TrEMBL.
DT   18-APR-2012, sequence version 1.
DT   27-MAR-2024, entry version 46.
DE   SubName: Full=Ribosomal RNA small subunit methyltransferase F {ECO:0000313|EMBL:EHY54444.1};
GN   ORFNames=HMPREF1120_02613 {ECO:0000313|EMBL:EHY54444.1};
OS   Exophiala dermatitidis (strain ATCC 34100 / CBS 525.76 / NIH/UT8656) (Black
OS   yeast) (Wangiella dermatitidis).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Exophiala.
OX   NCBI_TaxID=858893 {ECO:0000313|EMBL:EHY54444.1, ECO:0000313|Proteomes:UP000007304};
RN   [1] {ECO:0000313|EMBL:EHY54444.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=NIH/UT8656 {ECO:0000313|EMBL:EHY54444.1};
RG   The Broad Institute Genome Sequencing Platform;
RA   Cuomo C., Wang Z., Hunicke-Smith S., Szanislo P.J., Earl A., Young S.K.,
RA   Zeng Q., Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Alvarado L.,
RA   Arachchi H.M., Berlin A., Brown A., Chapman S.B., Chen Z., Dunbar C.,
RA   Freedman E., Gearin G., Gellesch M., Goldberg J., Griggs A., Gujja S.,
RA   Heiman D., Howarth C., Larson L., Lui A., MacDonald P.J.P., Montmayeur A.,
RA   Murphy C., Neiman D., Pearson M., Priest M., Roberts A., Saif S., Shea T.,
RA   Shenoy N., Sisk P., Stolte C., Sykes S., Wortman J., Nusbaum C., Birren B.;
RT   "The Genome Sequence of Exophiala (Wangiella) dermatitidis NIH/UT8656.";
RL   Submitted (JUL-2011) to the EMBL/GenBank/DDBJ databases.
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}.
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DR   EMBL; JH226131; EHY54444.1; -; Genomic_DNA.
DR   RefSeq; XP_009154905.1; XM_009156657.1.
DR   AlphaFoldDB; H6BPU3; -.
DR   STRING; 858893.H6BPU3; -.
DR   GeneID; 20307252; -.
DR   VEuPathDB; FungiDB:HMPREF1120_02613; -.
DR   eggNOG; KOG1122; Eukaryota.
DR   HOGENOM; CLU_005316_3_2_1; -.
DR   InParanoid; H6BPU3; -.
DR   OMA; PIGSWTK; -.
DR   OrthoDB; 1268at2759; -.
DR   Proteomes; UP000007304; 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   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:UP000007304};
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          296..586
FT                   /note="SAM-dependent MTase RsmB/NOP-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51686"
FT   REGION          1..169
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          614..717
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          170..212
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        23..81
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        98..148
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        149..163
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        639..698
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        514
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT   BINDING         388..394
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT   BINDING         412
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT   BINDING         439
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT   BINDING         457
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
SQ   SEQUENCE   717 AA;  78808 MW;  D3B32667619AC96B CRC64;
     MGPGRRMKKQ GPPATLEELG INLKRKSNLD GPKEPAKKRR RSDEHGPKKL VKLDRAIRSE
     QPPKNEAKAG KKEKKKQRLV NKDAQITVPP AMPILQTEEQ GDDEEEIDED DDAVDMPLDE
     ISSSDMEDDE IDQADLDQED VSDDSVFDSD PDEQPRRMFS EDEDDSDAEA QLTAANIEGL
     SRKLDQQQAQ VEAEAQQELE DAALQTNIAK DEGVLDSVAG PGQVGHGLAP DLAMIRNRMT
     ETIRILGNFS QLADKTKSRT EYIDQLLSDI CVYYGYTPYL AEKLFSLFTP AEAFAFFEAN
     ETPRPVVLRT NTLRTNRRTL AQALINRGVV LEPVGKWSKV GLQVFEAPVP LGATPEYLAG
     HYILQAASSF LPVMALAPQP NERILDMAAA PGGKTTYISA LMRNTGVVFA NDANKQRAKG
     LIGNIHRLGC KNTIVCNYDA QKAFPKVLGG FDRVLLDAPC SGTGVIGKDP SVKTSKNERD
     FLALPHMQKQ LLLAAIDSTD HSSKTGGYIV YSTCSVTVEE NEAVVQYVLR KRPNVKIVDT
     GLGNFGSEGF KSYMNKKFDD KMSLTRRYFP HRENVDGFFV AKLKKIGPMP KNVGSANGGD
     AADAEPKTAR INGDAKAGAN GVEDGEKEAD DFGGFNDEED KEIIERSEKK WLKARGLDPR
     VADRKKAVAV NGPKEEKSQK NGVDPKQKEK STASGGDKKK HKKKEKMATG SKSKDSK
//
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