ID A0A0D1DXE3_USTMA Unreviewed; 563 AA.
AC A0A0D1DXE3;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 24-JAN-2024, entry version 33.
DE RecName: Full=Ribosomal RNA-processing protein 8 {ECO:0000256|RuleBase:RU365074};
DE EC=2.1.1.- {ECO:0000256|RuleBase:RU365074};
GN ORFNames=UMAG_10715 {ECO:0000313|EMBL:KIS67185.1};
OS Ustilago maydis (strain 521 / FGSC 9021) (Corn smut fungus).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC Ustilaginomycetes; Ustilaginales; Ustilaginaceae; Ustilago.
OX NCBI_TaxID=237631 {ECO:0000313|EMBL:KIS67185.1, ECO:0000313|Proteomes:UP000000561};
RN [1] {ECO:0000313|EMBL:KIS67185.1, ECO:0000313|Proteomes:UP000000561}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=521 / FGSC 9021 {ECO:0000313|Proteomes:UP000000561};
RX PubMed=17080091; DOI=10.1038/nature05248;
RA Kamper J., Kahmann R., Bolker M., Ma L.J., Brefort T., Saville B.J.,
RA Banuett F., Kronstad J.W., Gold S.E., Muller O., Perlin M.H., Wosten H.A.,
RA de Vries R., Ruiz-Herrera J., Reynaga-Pena C.G., Snetselaar K., McCann M.,
RA Perez-Martin J., Feldbrugge M., Basse C.W., Steinberg G., Ibeas J.I.,
RA Holloman W., Guzman P., Farman M., Stajich J.E., Sentandreu R.,
RA Gonzalez-Prieto J.M., Kennell J.C., Molina L., Schirawski J.,
RA Mendoza-Mendoza A., Greilinger D., Munch K., Rossel N., Scherer M.,
RA Vranes M., Ladendorf O., Vincon V., Fuchs U., Sandrock B., Meng S.,
RA Ho E.C., Cahill M.J., Boyce K.J., Klose J., Klosterman S.J., Deelstra H.J.,
RA Ortiz-Castellanos L., Li W., Sanchez-Alonso P., Schreier P.H.,
RA Hauser-Hahn I., Vaupel M., Koopmann E., Friedrich G., Voss H., Schluter T.,
RA Margolis J., Platt D., Swimmer C., Gnirke A., Chen F., Vysotskaia V.,
RA Mannhaupt G., Guldener U., Munsterkotter M., Haase D., Oesterheld M.,
RA Mewes H.W., Mauceli E.W., DeCaprio D., Wade C.M., Butler J., Young S.,
RA Jaffe D.B., Calvo S., Nusbaum C., Galagan J., Birren B.W.;
RT "Insights from the genome of the biotrophic fungal plant pathogen Ustilago
RT maydis.";
RL Nature 444:97-101(2006).
RN [2] {ECO:0000313|Proteomes:UP000000561}
RP GENOME REANNOTATION.
RC STRAIN=521 / FGSC 9021 {ECO:0000313|Proteomes:UP000000561};
RA Gueldener U., Muensterkoetter M., Walter M.C., Mannhaupt G., Kahmann R.;
RL Submitted (SEP-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: S-adenosyl-L-methionine-dependent methyltransferase that
CC specifically methylates the N(1) position of adenine in helix 25.1 in
CC 25S rRNA. Required both for ribosomal 40S and 60S subunits biogenesis.
CC Required for efficient pre-rRNA cleavage at site A2.
CC {ECO:0000256|RuleBase:RU365074}.
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus
CC {ECO:0000256|ARBA:ARBA00004604, ECO:0000256|RuleBase:RU365074}.
CC -!- SIMILARITY: Belongs to the methyltransferase superfamily. RRP8 family.
CC {ECO:0000256|ARBA:ARBA00006301, ECO:0000256|RuleBase:RU365074}.
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DR EMBL; CM003154; KIS67185.1; -; Genomic_DNA.
DR RefSeq; XP_011391357.1; XM_011393055.1.
DR AlphaFoldDB; A0A0D1DXE3; -.
DR SMR; A0A0D1DXE3; -.
DR STRING; 237631.A0A0D1DXE3; -.
DR EnsemblFungi; KIS67185; KIS67185; UMAG_10715.
DR GeneID; 23566708; -.
DR KEGG; uma:UMAG_10715; -.
DR VEuPathDB; FungiDB:UMAG_10715; -.
DR eggNOG; KOG3045; Eukaryota.
DR InParanoid; A0A0D1DXE3; -.
DR OrthoDB; 1694at2759; -.
DR Proteomes; UP000000561; Chromosome 15.
DR GO; GO:0005730; C:nucleolus; IBA:GO_Central.
DR GO; GO:0016433; F:rRNA (adenine) methyltransferase activity; IBA:GO_Central.
DR GO; GO:0042273; P:ribosomal large subunit biogenesis; IBA:GO_Central.
DR GO; GO:0031167; P:rRNA methylation; IBA:GO_Central.
DR CDD; cd02440; AdoMet_MTases; 1.
DR Gene3D; 1.10.10.2150; Ribosomal RNA-processing protein 8, N-terminal domain; 1.
DR Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR InterPro; IPR007823; RRP8.
DR InterPro; IPR042036; RRP8_N.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR PANTHER; PTHR12787:SF0; RIBOSOMAL RNA-PROCESSING PROTEIN 8; 1.
DR PANTHER; PTHR12787; UNCHARACTERIZED; 1.
DR Pfam; PF05148; Methyltransf_8; 2.
DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
PE 3: Inferred from homology;
KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603,
KW ECO:0000256|RuleBase:RU365074};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|RuleBase:RU365074};
KW Reference proteome {ECO:0000313|Proteomes:UP000000561};
KW rRNA processing {ECO:0000256|ARBA:ARBA00022552,
KW ECO:0000256|RuleBase:RU365074};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691,
KW ECO:0000256|RuleBase:RU365074};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU365074}.
FT REGION 30..152
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 192..211
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 224..259
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 335..365
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 30..82
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 92..106
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 119..146
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 346..360
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 563 AA; 60789 MW; 05241699D48A3546 CRC64;
MSDALDLDQL QAQLELKRSA LADSILSKLP GLSADTSSSS SSTALPKSAQ HQQNSRPRQA
NLGVGATPKQ QNADSSGSTR GPRSAADLRL KGALTAKRKR WQDQEPAVQN ESDSDDQESS
RVNVISANKK SKHENSQTTS LSNVGIPKPA NKDPFAVNGI QAQKAAQNQP RIVVINGETI
DLSKLSKTQR KKINKQLKAQ HNQQQDDQAQ DEVFKPATTT TLADALSTPE SPLTSCSKAT
SQTPSSNNNQ SSSPSGAALT PLQSQMLSKL SGSRFRTINE KLYTTASDEA VRMIDAAPTM
FDEYHQGFRE QVRSWPKNPL DRIVELFDPS LSIYKDKDKG KGNGKSKSKG TPSQPSGPSD
RSKPRYAPGA LVVDLGAGEG GLAKKLSPKA VKVLCYDLIT TSDGWVRKQD TAAIGGLPLP
GFFLDTDPLG LGATPEGVAQ GVADVAVFCL SLMGTNWIHM LLEAKRVLRT GGELIIAEVS
SRFGDGFEAF IRIVKLLGFG LEHKDASNTH FVLFEFVKLS QRDHLASLSA LQDDSQIDPT
HTSLDELAQH GKTLLKPCIY KRR
//
