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Database: UniProt
Entry: A0A3P8QQ52_ASTCA
LinkDB: A0A3P8QQ52_ASTCA
Original site: A0A3P8QQ52_ASTCA 
ID   A0A3P8QQ52_ASTCA        Unreviewed;       496 AA.
AC   A0A3P8QQ52;
DT   13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT   13-FEB-2019, sequence version 1.
DT   27-MAR-2024, entry version 23.
DE   SubName: Full=NOP2/Sun RNA methyltransferase 5 {ECO:0000313|Ensembl:ENSACLP00000031117.1};
OS   Astatotilapia calliptera (Eastern happy) (Chromis callipterus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Ovalentaria; Cichlomorphae; Cichliformes; Cichlidae; African cichlids;
OC   Pseudocrenilabrinae; Haplochromini; Astatotilapia.
OX   NCBI_TaxID=8154 {ECO:0000313|Ensembl:ENSACLP00000031117.1, ECO:0000313|Proteomes:UP000265100};
RN   [1] {ECO:0000313|Ensembl:ENSACLP00000031117.1, ECO:0000313|Proteomes:UP000265100}
RP   NUCLEOTIDE SEQUENCE.
RA   Datahose.;
RL   Submitted (MAY-2018) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSACLP00000031117.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2023) to UniProtKB.
CC   -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC       superfamily. RsmB/NOP family. {ECO:0000256|PROSITE-ProRule:PRU01023}.
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DR   AlphaFoldDB; A0A3P8QQ52; -.
DR   SMR; A0A3P8QQ52; -.
DR   STRING; 8154.ENSACLP00000031117; -.
DR   Ensembl; ENSACLT00000031848.1; ENSACLP00000031117.1; ENSACLG00000021086.1.
DR   GeneTree; ENSGT00940000155974; -.
DR   OMA; SFKSRIY; -.
DR   OrthoDB; 102852at2759; -.
DR   Proteomes; UP000265100; Chromosome 20.
DR   Bgee; ENSACLG00000021086; Expressed in testis and 8 other cell types or tissues.
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   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; IPR049561; NSUN5_7_fdxn-like.
DR   InterPro; IPR048889; NSUN5_RCM1_N.
DR   InterPro; IPR023267; RCMT.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
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; PF21148; NSUN5_fdxn-like; 1.
DR   Pfam; PF21153; NSUN5_N; 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   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}.
FT   DOMAIN          124..418
FT                   /note="SAM-dependent MTase RsmB/NOP-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51686"
FT   REGION          431..496
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        476..490
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        356
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT   BINDING         231..237
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT   BINDING         255
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT   BINDING         282
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT   BINDING         302
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
SQ   SEQUENCE   496 AA;  55303 MW;  854B61A01FD2E1DE CRC64;
     MALYLKAAEI TEKVEGKQGA LKTLVYDSQF KNIKQLFALV CETQKFSSVL QEIIESTKLL
     RHTKLKMPLA KVLVYDLLIG QGLKCGGSWK AMMMKHRSRL QAELARMKVK QKVSRNEDLL
     PCSVKHPAGD QLPRYVRVNT LKTTVEDVVD YLKRDGFSYL GKASRLEDLS LKDRYFLSDL
     HLPELLVFSP KTDFHDHFLY KAGHIVLQDK ASCLPAHLLS PPPGSHIIDA CAAPGNKTSQ
     LAAIMKNKGR LFAFDLDGKR LATMSTLLLR AGVTCQQLAN QDFLKVDPDN PQYKDVEYIL
     LDPSCSGSGM VCLQDNTSAD QEKEQARLAS LASFQLRCLN HALRFPSLKR LVYSTCSIHK
     QENEEVVAAC LQQNPGFRLV PLLAEWPERG LEPLPQCLRA STAKTLTHGF FVALLEKHSE
     PGNTKQELAV QISGPEVKPS NLPSSEKRPA ASEEDCEASE TEDRPTPVGG QTGSKPNNKK
     KRRKRKKKKK GAETAE
//
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