GenomeNet

Database: UniProt
Entry: Q50LB2_9MUSC
LinkDB: Q50LB2_9MUSC
Original site: Q50LB2_9MUSC 
ID   Q50LB2_9MUSC            Unreviewed;       421 AA.
AC   Q50LB2;
DT   07-JUN-2005, integrated into UniProtKB/TrEMBL.
DT   07-JUN-2005, sequence version 1.
DT   27-MAR-2024, entry version 59.
DE   SubName: Full=Uncharacterized protein CG5558 {ECO:0000313|EMBL:BAD98176.1};
GN   ORFNames=CG5558 {ECO:0000313|FlyBase:FBgn0083592};
OS   Drosophila parabipectinata.
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC   Drosophilidae; Drosophila; Sophophora.
OX   NCBI_TaxID=186283 {ECO:0000313|EMBL:BAD98176.1};
RN   [1] {ECO:0000313|EMBL:BAD98176.1}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=16143626; DOI=10.1534/genetics.105.041699;
RA   Nozawa M., Aotsuka T., Tamura K.;
RT   "A novel chimeric gene, siren, with retroposed promoter sequence in the
RT   Drosophila bipectinata complex.";
RL   Genetics 171:1719-1727(2005).
CC   -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC       superfamily. RsmB/NOP family. {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; AB194415; BAD98176.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q50LB2; -.
DR   FlyBase; FBgn0083592; Dpbp\CG5558.
DR   GO; GO:0031410; C:cytoplasmic vesicle; IEA:UniProtKB-KW.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0008173; F:RNA methyltransferase activity; IEA:InterPro.
DR   GO; GO:0001510; P:RNA methylation; IEA:InterPro.
DR   GO; GO:0070072; P:vacuolar proton-transporting V-type ATPase complex assembly; IEA:InterPro.
DR   Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR   InterPro; IPR049560; MeTrfase_RsmB-F_NOP2_cat.
DR   InterPro; IPR001678; MeTrfase_RsmB-F_NOP2_dom.
DR   InterPro; IPR023267; RCMT.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   InterPro; IPR019013; Vma21.
DR   PANTHER; PTHR22807:SF4; 28S RRNA (CYTOSINE-C(5))-METHYLTRANSFERASE; 1.
DR   PANTHER; PTHR22807; NOP2 YEAST -RELATED NOL1/NOP2/FMU SUN DOMAIN-CONTAINING; 1.
DR   Pfam; PF01189; Methyltr_RsmB-F; 1.
DR   Pfam; PF09446; VMA21; 1.
DR   PRINTS; PR02008; RCMTFAMILY.
DR   SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR   PROSITE; PS51686; SAM_MT_RSMB_NOP; 1.
PE   3: Inferred from homology;
KW   Cytoplasmic vesicle {ECO:0000256|ARBA:ARBA00023329};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Methyltransferase {ECO:0000256|ARBA:ARBA00022603, ECO:0000256|PROSITE-
KW   ProRule:PRU01023};
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}; Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        38..59
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        79..97
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          128..415
FT                   /note="SAM-dependent MTase RsmB/NOP-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51686"
FT   REGION          1..30
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        345
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT   BINDING         247
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT   BINDING         274
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT   BINDING         292
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
SQ   SEQUENCE   421 AA;  47674 MW;  488D935E12464B20 CRC64;
     MGKRGKKQQA KEVVAEEDAP QALPVQRSPQ EEDTSAEVFL WLLAYSVLMF TLPFLGFYGV
     RSWLLESFPD LDRFTVNCWS VLTAVVIVNL VVAMYVLKAF REKVPPPLEP VEEAEDELES
     TEPKKYHLSQ ALEYLASEDW RRKELPADAS YADFLAAVKA LEEDEFMTDL QVEGVLVFHH
     KWSSYWSSHE FVKQKKFILQ NKGTCLAAEL LAPPSGSTVL DMCAAPGMKT LHLCNFMKNK
     GRIYAVEQST ERYRVLCNIT SEAGCDIVTP ILGDALRMNA ENCPEVEYIL VDPSCSGNGM
     QSRMNVCDEE KDDQRLFKLA GLQVKILSHA MTAFPNVKRI AYCTCSLYKE ENEEVVKRCL
     QVNPSFKLLS CKKALRNKWH NVGDTEYAKI GKNVLYCLPD SDLTDGIFLA LFEKRRDGEA
     D
//
DBGET integrated database retrieval system