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Database: UniProt
Entry: A0A100IRV7_ASPNG
LinkDB: A0A100IRV7_ASPNG
Original site: A0A100IRV7_ASPNG 
ID   A0A100IRV7_ASPNG        Unreviewed;       799 AA.
AC   A0A100IRV7;
DT   13-APR-2016, integrated into UniProtKB/TrEMBL.
DT   13-APR-2016, sequence version 1.
DT   24-JAN-2024, entry version 31.
DE   SubName: Full=rRNA methyltransferase Spb1 {ECO:0000313|EMBL:GAQ46200.1};
GN   ORFNames=ABL_08861 {ECO:0000313|EMBL:GAQ46200.1};
OS   Aspergillus niger.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Circumdati.
OX   NCBI_TaxID=5061 {ECO:0000313|EMBL:GAQ46200.1, ECO:0000313|Proteomes:UP000068243};
RN   [1] {ECO:0000313|Proteomes:UP000068243}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=An76 {ECO:0000313|Proteomes:UP000068243};
RX   PubMed=26893421; DOI=10.1128/genomeA.01700-15;
RA   Gong W., Cheng Z., Zhang H., Liu L., Gao P., Wang L.;
RT   "Draft genome sequence of Aspergillus niger strain An76.";
RL   Genome Announc. 4:E0170015-E0170015(2016).
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:GAQ46200.1}.
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DR   EMBL; BCMY01000020; GAQ46200.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A100IRV7; -.
DR   PaxDb; 5061-CADANGAP00013600; -.
DR   VEuPathDB; FungiDB:An18g02230; -.
DR   VEuPathDB; FungiDB:ASPNIDRAFT2_1128456; -.
DR   VEuPathDB; FungiDB:ATCC64974_110100; -.
DR   VEuPathDB; FungiDB:M747DRAFT_252877; -.
DR   OMA; DITTEDC; -.
DR   Proteomes; UP000068243; 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   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   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          234..392
FT                   /note="DUF3381"
FT                   /evidence="ECO:0000259|Pfam:PF11861"
FT   DOMAIN          583..795
FT                   /note="Ribosomal RNA methyltransferase SPB1-like C-
FT                   terminal"
FT                   /evidence="ECO:0000259|Pfam:PF07780"
FT   REGION          367..388
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          432..532
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          549..613
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        443..464
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        465..497
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        498..517
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        549..565
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        566..594
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   799 AA;  90385 MW;  60C020521E6C8FC1 CRC64;
     MAIQKKHGKG RLDKWYRLAK EKGYRARAAF KLIQLNKKYG FLEKSKVVLD LCAAPGSWCQ
     VAAECMPAQS IIVGVDLAPI KPIPRVITFQ SDITTEKCRT TIRQHLKHWK ADTVLHDGAP
     NVGTAWVQDA FSQAELVLQS LKLATEFLAE GGTFVTKVFR SKDYNPLLWV FKQLFASVEA
     TKPPSSRNVS AEIFVVCRNY KAPKRIDPKF LDPKHVFAEL ADPTPNNEAK VFNPEKKKRK
     REGYEEGDYT QFKEVPVTEF INTTDPIAIL GSCNKLSFQQ SPSGDLALAT LERLEETTDE
     IKACCEDLKV LGKKEFRNLL RWRLKVREQF GLAVKKGGQA KEDETEEVAE VAPMDDELAI
     QEELMRLREK ETSKQKKERR KENERKRKEI VRLQMHMTTP MDIGKEQLGP NGEDATFSLK
     RAERGGIRDT LAAGHEATIE SDSEDSASES DFDESDDEED RLERELDNLY EQYQDRKEDR
     DTKLRAKKAR KDFEADSWDG FSDDDKEDGE DSDDEGLGVG SAGDKAPKSA SLSNSASLFF
     DQDIFQGLED IDDVEDEDDE VADEDSAIEV KPKGKESEKK KKAKEAKKPV QAMEDSDEED
     IEELEDPRKK NGQLDIDIIT AEAMALAQQM ATGEKKSSDV VDDGFNRFAF RDSDGLPEWF
     LDDENKHSIQ NRPITKAAAA AIKEKMRAIN ARPIKKVMEA KGRKKFKAAQ RLEKLRKKSA
     LLADDEALSE RDKSQAIARL MSRATKKKPK QQVKLVVAKG NNRGISGRPR GVKGKYKIVD
     SRMKKDIRAQ KRLAKKKKN
//
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